SecA is the peripheral ATP-hydrolyzing motor of the Escherichia coli Sec translocase. It binds SecB-delivered and other signal-peptide-bearing preproteins at the cytoplasmic face of the inner-membrane SecYEG channel, recognizes preprotein signal and mature regions, engages the SecY pore, and couples ATP binding and hydrolysis to stepwise polypeptide movement across the plasma membrane. A soluble SecA pool exchanges with the membrane-associated translocase, a C-terminal zinc site stabilizes its SecB-binding region, and ribosome binding can support cotranslational targeting of at least a subset of substrates.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005515 protein binding | IPI PMID:15690043 Interaction network containing conserved and essential prote... | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:15811382 Asymmetric binding between SecA and SecB two symmetric prote... | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:16294310 A protein network for phospholipid synthesis uncovered by a ... | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:17060619 Different modes of SecY-SecA interactions revealed by site-d... | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:17229438 Structure of dimeric SecA, the Escherichia coli preprotein t... | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:18022369 Structural basis for signal-sequence recognition by the tran... | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:18022369 Structural basis for signal-sequence recognition by the tran... | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:18761620 Assembly of the translocase motor onto the preprotein-conduc... | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:18761620 Assembly of the translocase motor onto the preprotein-conduc... | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:18761620 Assembly of the translocase motor onto the preprotein-conduc... | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:18923526 A role for the two-helix finger of the SecA ATPase in protei... | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:19924216 Signal peptides are allosteric activators of the protein tra... | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:20479269 The action of cardiolipin on the bacterial translocon. | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:20479269 The action of cardiolipin on the bacterial translocon. | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:20479269 The action of cardiolipin on the bacterial translocon. | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:21037004 Orientation of SecA and SecB in complex, derived from disulf... | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:2170023 The binding cascade of SecB to SecA to SecY/E mediates prepr... | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:24561554 The binary protein-protein interaction landscape of Escheric... | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:24561554 The binary protein-protein interaction landscape of Escheric... | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005515 protein binding | IPI PMID:9111035 Identification of a region of interaction between Escherichi... | REMOVE | Summary: The row records a physical interaction, but GO:0005515 protein binding is too generic to describe the Sec component activity. Reason: The interaction itself is not rejected. The problem is that GO:0005515 does not say whether the gene product is the SecA motor, the SecY pore, a SecYEG clamp/accessory subunit, or an export precursor. This row should be removed in favor of the more informative Sec molecular-function and process annotations. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md Generic protein-binding IPI rows for SecA should be removed as uninformative interaction records, not because the reported interactions are false. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005524 ATP binding | IEA GO_REF:0000120 | ACCEPT | Summary: SecA binds ATP as the nucleotide substrate for its Sec translocation ATPase cycle. Reason: ATP binding is an expected substrate-binding aspect of the SecA protein-exporting ATPase. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0005737 cytoplasm | IDA PMID:1837021 Characterization of membrane-associated and soluble states o... | ACCEPT | Summary: SecA has a soluble cytoplasmic pool in addition to its SecYEG-associated membrane pool. Reason: Cell fractionation showed that SecA partitions between cytoplasm and inner membrane; both pools are consistent with its precursor-targeting and translocase motor cycle. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is partitioned between cytosol and inner membrane, and the membrane-associated fraction is functionally relevant. PMID:1837021 In a wild-type strain approximately half of the cellular SecA content was found to be associated with the inner membrane, while the remainder was soluble. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: SecA has a soluble cytoplasmic pool in addition to its SecYEG-associated membrane pool. Reason: Cell fractionation showed that SecA partitions between cytoplasm and inner membrane; both pools are consistent with its precursor-targeting and translocase motor cycle. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is partitioned between cytosol and inner membrane, and the membrane-associated fraction is functionally relevant. PMID:1837021 In a wild-type strain approximately half of the cellular SecA content was found to be associated with the inner membrane, while the remainder was soluble. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: SecA acts at the plasma membrane by binding the inner-membrane SecYEG channel. Reason: The SecA motor is peripherally associated with the plasma membrane during preprotein delivery and translocation through SecYEG. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000770133 · PANTHER:PTN000770133 SUPPORTS TRANSFER The PAINT trace is consistent with the Sec-family placement; the review action reflects whether the GOA term and qualifier are at the right specificity for this E. coli subunit. UniProtKB:P10408 · UniProtKB:P10408 SUPPORTS TRANSFER The PAINT trace is consistent with the Sec-family placement; the review action reflects whether the GOA term and qualifier are at the right specificity for this E. coli subunit. UniProtKB:P28366 · UniProtKB:P28366 SUPPORTS TRANSFER The PAINT trace is consistent with the Sec-family placement; the review action reflects whether the GOA term and qualifier are at the right specificity for this E. coli subunit. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:1837021 In a wild-type strain approximately half of the cellular SecA content was found to be associated with the inner membrane, while the remainder was soluble. |
| GO:0005886 plasma membrane | IDA PMID:1837021 Characterization of membrane-associated and soluble states o... | ACCEPT | Summary: SecA acts at the plasma membrane by binding the inner-membrane SecYEG channel. Reason: The SecA motor is peripherally associated with the plasma membrane during preprotein delivery and translocation through SecYEG. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:1837021 In a wild-type strain approximately half of the cellular SecA content was found to be associated with the inner membrane, while the remainder was soluble. |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: SecA acts at the plasma membrane by binding the inner-membrane SecYEG channel. Reason: The SecA motor is peripherally associated with the plasma membrane during preprotein delivery and translocation through SecYEG. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:1837021 In a wild-type strain approximately half of the cellular SecA content was found to be associated with the inner membrane, while the remainder was soluble. |
| GO:0006605 protein targeting | IEA GO_REF:0000120 | MODIFY | Summary: The row captures SecA-dependent targeting of precursor proteins but uses a broad parent term. Reason: SecA directly targets SecB-bound and some nascent precursors to the bacterial inner membrane. GO:0006612 protein targeting to membrane is the more specific biological-process term for this activity. Proposed replacements: protein targeting to membrane Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2170023 The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. |
| GO:0006605 protein targeting | IMP PMID:6279567 Identification of a new gene (secA) and gene product involve... | MODIFY | Summary: The row captures SecA-dependent targeting of precursor proteins but uses a broad parent term. Reason: SecA directly targets SecB-bound and some nascent precursors to the bacterial inner membrane. GO:0006612 protein targeting to membrane is the more specific biological-process term for this activity. Proposed replacements: protein targeting to membrane Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2170023 The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. |
| GO:0006612 protein targeting to membrane | IDA PMID:2170023 The binding cascade of SecB to SecA to SecY/E mediates prepr... | ACCEPT | Summary: SecA targets preproteins to the inner-membrane Sec translocase. Reason: SecA binds SecB-bound precursors and SecYEG, placing it directly in precursor targeting to the plasma membrane. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2170023 The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. |
| GO:0006612 protein targeting to membrane | IDA PMID:28928132 SecA mediates cotranslational targeting and translocation of... | ACCEPT | Summary: SecA targets preproteins to the inner-membrane Sec translocase. Reason: SecA binds SecB-bound precursors and SecYEG, placing it directly in precursor targeting to the plasma membrane. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2170023 The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. |
| GO:0006886 intracellular protein transport | IEA GO_REF:0000002 | MODIFY | Summary: The row captures SecA-dependent protein movement but is too broad for the Sec export motor. Reason: SecA acts specifically in Sec-complex protein transport, not generic intracellular protein transport. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0008270 zinc ion binding | IDA PMID:10213615 Zinc stabilizes the SecB binding site of SecA. | KEEP AS NON CORE | Summary: SecA binds a C-terminal zinc ion that stabilizes the SecB-binding site. Reason: The zinc site is biochemically real and supports SecB docking, but metal binding is accessory to the core ATPase translocation cycle. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md The C-terminal zinc site is real but supports SecB binding rather than defining a separate pathway. PMID:10213615 It is concluded that the SecB binding domain of SecA is stabilized by a zinc ion that promotes the functional binding of SecB to SecA. |
| GO:0008564 protein-exporting ATPase activity | EXP PMID:1825804 Delta mu H+ and ATP function at different steps of the catal... | ACCEPT | Summary: SecA is the Sec pathway ATPase motor. Reason: SecA hydrolyzes ATP and couples that hydrolysis to preprotein translocation through the SecYEG channel. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0008564 protein-exporting ATPase activity | EXP PMID:2542029 SecA protein hydrolyzes ATP and is an essential component of... | ACCEPT | Summary: SecA is the Sec pathway ATPase motor. Reason: SecA hydrolyzes ATP and couples that hydrolysis to preprotein translocation through the SecYEG channel. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0008564 protein-exporting ATPase activity | IEA GO_REF:0000003 | ACCEPT | Summary: SecA is the Sec pathway ATPase motor. Reason: SecA hydrolyzes ATP and couples that hydrolysis to preprotein translocation through the SecYEG channel. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0009306 protein secretion | IMP PMID:6279567 Identification of a new gene (secA) and gene product involve... | MODIFY | Summary: The row reports the original secretion defect of secA mutants but uses a broad secretion term. Reason: In E. coli, SecA acts in the Sec-dependent protein transport step across the inner membrane. GO:0043952 is the more precise process term. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0009898 cytoplasmic side of plasma membrane | IDA PMID:27613865 Lipids Activate SecA for High Affinity Binding to the SecYEG... | ACCEPT | Summary: SecA binds SecYEG at the cytoplasmic face of the plasma membrane. Reason: This location captures the active side from which SecA engages SecYEG and drives ATP-dependent preprotein movement. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:1837021 In a wild-type strain approximately half of the cellular SecA content was found to be associated with the inner membrane, while the remainder was soluble. |
| GO:0015031 protein transport | IMP PMID:6279567 Identification of a new gene (secA) and gene product involve... | MODIFY | Summary: The row is a broad parent for the Sec-specific protein-transport process. Reason: SecA acts in the Sec pathway; GO:0043952 is the specific child process. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0016020 membrane | IEA GO_REF:0000002 | MODIFY | Summary: SecA acts at the plasma membrane rather than an unspecified membrane. Reason: The active SecA translocase motor is associated with the bacterial plasma membrane SecYEG channel. Proposed replacements: plasma membrane Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:1837021 In a wild-type strain approximately half of the cellular SecA content was found to be associated with the inner membrane, while the remainder was soluble. |
| GO:0016887 ATP hydrolysis activity | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The IBA row captures ATP hydrolysis but is less specific than SecA protein-exporting ATPase activity. Reason: SecA hydrolyzes ATP during protein export. Keep this generic hydrolysis row as a true non-core biochemical activity while GO:0008564 records the specific coupled protein-exporting ATPase reaction. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000770123 · PANTHER:PTN000770123 SUPPORTS TRANSFER The PAINT node captures a real but generic SecA ATP hydrolysis activity; E. coli SecA is represented more specifically by GO:0008564 for its coupled protein-exporting ATPase reaction. UniProtKB:P9WGP3 · UniProtKB:P9WGP3 SUPPORTS TRANSFER The PAINT node captures a real but generic SecA ATP hydrolysis activity; E. coli SecA is represented more specifically by GO:0008564 for its coupled protein-exporting ATPase reaction. UniProtKB:P9WGP5 · UniProtKB:P9WGP5 SUPPORTS TRANSFER The PAINT node captures a real but generic SecA ATP hydrolysis activity; E. coli SecA is represented more specifically by GO:0008564 for its coupled protein-exporting ATPase reaction. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0017038 protein import | IEA GO_REF:0000002 | REMOVE | Summary: The InterPro-derived import annotation is the wrong direction for E. coli SecA. Reason: E. coli SecA exports proteins from the cytoplasmic side of the inner membrane to the periplasm or inner membrane, whereas protein import is not its bacterial pathway role. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0031522 cell envelope Sec protein transport complex | IBA GO_REF:0000033 | ACCEPT | Summary: SecA is the peripheral ATPase associated with the cell-envelope Sec transport complex. Reason: SecA interacts with SecYEG as the peripheral motor of the Sec translocase. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000770133 · PANTHER:PTN000770133 SUPPORTS TRANSFER The PAINT trace is consistent with the Sec-family placement; the review action reflects whether the GOA term and qualifier are at the right specificity for this E. coli subunit. UniProtKB:P10408 · UniProtKB:P10408 SUPPORTS TRANSFER The PAINT trace is consistent with the Sec-family placement; the review action reflects whether the GOA term and qualifier are at the right specificity for this E. coli subunit. UniProtKB:P9WGP5 · UniProtKB:P9WGP5 SUPPORTS TRANSFER The PAINT trace is consistent with the Sec-family placement; the review action reflects whether the GOA term and qualifier are at the right specificity for this E. coli subunit. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0031522 cell envelope Sec protein transport complex | IDA PMID:2139227 Solubilization and functional reconstitution of the protein-... | ACCEPT | Summary: SecA is the peripheral ATPase associated with the cell-envelope Sec transport complex. Reason: SecA interacts with SecYEG as the peripheral motor of the Sec translocase. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0031522 cell envelope Sec protein transport complex | IDA PMID:2167176 The purified E. coli integral membrane protein SecY/E is suf... | ACCEPT | Summary: SecA is the peripheral ATPase associated with the cell-envelope Sec transport complex. Reason: SecA interacts with SecYEG as the peripheral motor of the Sec translocase. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0031522 cell envelope Sec protein transport complex | IEA GO_REF:0000117 | ACCEPT | Summary: SecA is the peripheral ATPase associated with the cell-envelope Sec transport complex. Reason: SecA interacts with SecYEG as the peripheral motor of the Sec translocase. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0042802 identical protein binding | IPI PMID:16079137 Protein complexes of the Escherichia coli cell envelope. | KEEP AS NON CORE | Summary: SecA self-association has been observed but is secondary to its motor activity. Reason: SecA can dimerize, yet the quaternary state is an accessory property and should not be elevated over protein-exporting ATPase activity. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0042802 identical protein binding | IPI PMID:18022369 Structural basis for signal-sequence recognition by the tran... | KEEP AS NON CORE | Summary: SecA self-association has been observed but is secondary to its motor activity. Reason: SecA can dimerize, yet the quaternary state is an accessory property and should not be elevated over protein-exporting ATPase activity. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0042802 identical protein binding | IPI PMID:21037004 Orientation of SecA and SecB in complex, derived from disulf... | KEEP AS NON CORE | Summary: SecA self-association has been observed but is secondary to its motor activity. Reason: SecA can dimerize, yet the quaternary state is an accessory property and should not be elevated over protein-exporting ATPase activity. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0043021 ribonucleoprotein complex binding | IDA PMID:28928132 SecA mediates cotranslational targeting and translocation of... | KEEP AS NON CORE | Summary: SecA can bind ribosome-nascent-chain complexes. Reason: Ribosome binding supports an additional cotranslational route for some substrates, but the canonical core function remains the SecA ATPase cycle at SecYEG. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA can bind ribosomes and can support a cotranslational targeting route for at least the RodZ inner-membrane substrate, but these ribosome-binding activities are accessory to the canonical SecB/SecYEG export cycle. PMID:31409676 We have mapped the interaction of SecA with translating and nontranslating ribosomes and demonstrate that the N terminus and the helical linker domain of SecA bind to an acidic patch on the surface of the ribosomal protein uL23. |
| GO:0043022 ribosome binding | IPI PMID:21292166 SecA interacts with ribosomes in order to facilitate posttra... | KEEP AS NON CORE | Summary: SecA can bind near the ribosomal tunnel exit. Reason: Ribosome binding is valid but accessory relative to the core ATPase motor role. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA can bind ribosomes and can support a cotranslational targeting route for at least the RodZ inner-membrane substrate, but these ribosome-binding activities are accessory to the canonical SecB/SecYEG export cycle. PMID:31409676 We have mapped the interaction of SecA with translating and nontranslating ribosomes and demonstrate that the N terminus and the helical linker domain of SecA bind to an acidic patch on the surface of the ribosomal protein uL23. |
| GO:0043022 ribosome binding | IPI PMID:31409676 Molecular Mimicry of SecA and Signal Recognition Particle Bi... | KEEP AS NON CORE | Summary: SecA can bind near the ribosomal tunnel exit. Reason: Ribosome binding is valid but accessory relative to the core ATPase motor role. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA can bind ribosomes and can support a cotranslational targeting route for at least the RodZ inner-membrane substrate, but these ribosome-binding activities are accessory to the canonical SecB/SecYEG export cycle. PMID:31409676 We have mapped the interaction of SecA with translating and nontranslating ribosomes and demonstrate that the N terminus and the helical linker domain of SecA bind to an acidic patch on the surface of the ribosomal protein uL23. |
| GO:0043952 protein transport by the Sec complex | IBA GO_REF:0000033 | ACCEPT | Summary: SecA is a dedicated Sec-complex protein transport motor. Reason: SecA is the ATPase that engages the SecYEG channel and drives Sec-dependent preprotein movement. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000770133 · PANTHER:PTN000770133 SUPPORTS TRANSFER The PAINT trace is consistent with the Sec-family placement; the review action reflects whether the GOA term and qualifier are at the right specificity for this E. coli subunit. UniProtKB:P10408 · UniProtKB:P10408 SUPPORTS TRANSFER The PAINT trace is consistent with the Sec-family placement; the review action reflects whether the GOA term and qualifier are at the right specificity for this E. coli subunit. UniProtKB:P9WGP3 · UniProtKB:P9WGP3 SUPPORTS TRANSFER The PAINT trace is consistent with the Sec-family placement; the review action reflects whether the GOA term and qualifier are at the right specificity for this E. coli subunit. UniProtKB:P9WGP5 · UniProtKB:P9WGP5 SUPPORTS TRANSFER The PAINT trace is consistent with the Sec-family placement; the review action reflects whether the GOA term and qualifier are at the right specificity for this E. coli subunit. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0043952 protein transport by the Sec complex | IDA PMID:2139227 Solubilization and functional reconstitution of the protein-... | ACCEPT | Summary: SecA is a dedicated Sec-complex protein transport motor. Reason: SecA is the ATPase that engages the SecYEG channel and drives Sec-dependent preprotein movement. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0043952 protein transport by the Sec complex | IDA PMID:2167176 The purified E. coli integral membrane protein SecY/E is suf... | ACCEPT | Summary: SecA is a dedicated Sec-complex protein transport motor. Reason: SecA is the ATPase that engages the SecYEG channel and drives Sec-dependent preprotein movement. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0043952 protein transport by the Sec complex | IEA GO_REF:0000117 | ACCEPT | Summary: SecA is a dedicated Sec-complex protein transport motor. Reason: SecA is the ATPase that engages the SecYEG channel and drives Sec-dependent preprotein movement. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0043952 protein transport by the Sec complex | IMP PMID:6279567 Identification of a new gene (secA) and gene product involve... | ACCEPT | Summary: SecA is a dedicated Sec-complex protein transport motor. Reason: SecA is the ATPase that engages the SecYEG channel and drives Sec-dependent preprotein movement. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0065002 intracellular protein transmembrane transport | IEA GO_REF:0000104 | MODIFY | Summary: SecA drives transport of proteins across the bacterial inner membrane through SecYEG, but the Sec-specific term is more precise. Reason: GO:0043952 captures the same transport event with the correct Sec-complex specificity. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0065002 intracellular protein transmembrane transport | IMP PMID:2846186 SecA protein is required for secretory protein translocation... | MODIFY | Summary: SecA drives transport of proteins across the bacterial inner membrane through SecYEG, but the Sec-specific term is more precise. Reason: GO:0043952 captures the same transport event with the correct Sec-complex specificity. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0065002 intracellular protein transmembrane transport | IMP PMID:6279567 Identification of a new gene (secA) and gene product involve... | MODIFY | Summary: SecA drives transport of proteins across the bacterial inner membrane through SecYEG, but the Sec-specific term is more precise. Reason: GO:0043952 captures the same transport event with the correct Sec-complex specificity. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2542029 These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane. |
| GO:0070678 preprotein binding | IDA PMID:2170023 The binding cascade of SecB to SecA to SecY/E mediates prepr... | ACCEPT | Summary: SecA binds preproteins and signal peptides during targeting and translocation. Reason: Preprotein binding is intrinsic to the SecA targeting and translocation ATPase cycle. Supporting Evidence: file:ECOLI/SecA/SecA-notes.md SecA is the peripheral ATPase motor of the E. coli Sec translocase. PMID:2170023 The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. |
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Download this section (compressed HTML)Q: Which E. coli inner-membrane substrates use SecA-ribosome cotranslational targeting rather than SRP-mediated targeting or the canonical SecB/SecA post-translational route?
Experiment: Combine ribosome profiling, SecA pulldown of ribosome-nascent-chain complexes, and acute SecA ribosome-binding mutants to map native substrates of the SecA cotranslational route.
Hypothesis: Only a defined subset of inner-membrane proteins uses direct SecA-ribosome targeting in vivo.
Type: ribosome-nascent-chain complex profiling
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