SecY is the pore-forming subunit of the Escherichia coli SecYEG protein-conducting channel in the inner membrane. Its ten-transmembrane-helix core forms the gated aqueous pore and lateral gate used for post-translational SecA/SecB-dependent export of secretory preproteins and for cotranslational insertion of inner-membrane proteins delivered by SRP. SecY directly contacts signal peptides, SecA, SecE, SecG, ribosomes, and accessory translocon factors during Sec-dependent protein movement into or across the plasma membrane.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005048 signal sequence receptor activity | IBA GO_REF:0000033 | ACCEPT | Summary: SecY directly binds signal peptides in the SecYEG lateral-gate region. Reason: Signal-sequence binding is a mechanistic subactivity of the pore-forming SecY subunit. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000097337 · PANTHER:PTN000097337 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:P0AGA2 · UniProtKB:P0AGA2 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/SecY/SecY-notes.md SecY directly contributes the protein-conducting pore and signal-peptide-interacting lateral gate. PMID:15476412 The signal peptide was found to specifically bind SecY in a saturable manner and at levels comparable to those that stimulate SecA ATPase activity. |
| GO:0005048 signal sequence receptor activity | IDA PMID:15476412 Demonstration of a specific Escherichia coli SecY-signal pep... | ACCEPT | Summary: SecY directly binds signal peptides in the SecYEG lateral-gate region. Reason: Signal-sequence binding is a mechanistic subactivity of the pore-forming SecY subunit. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY directly contributes the protein-conducting pore and signal-peptide-interacting lateral gate. PMID:15476412 The signal peptide was found to specifically bind SecY in a saturable manner and at levels comparable to those that stimulate SecA ATPase activity. |
| GO:0005515 protein binding | IPI PMID:15815684 FtsY, the bacterial signal-recognition particle receptor, in... | 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/SecY/SecY-notes.md Generic GO:0005515 protein-binding rows for SecY should be removed as uninformative interaction records. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| 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/SecY/SecY-notes.md Generic GO:0005515 protein-binding rows for SecY should be removed as uninformative interaction records. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| 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/SecY/SecY-notes.md Generic GO:0005515 protein-binding rows for SecY should be removed as uninformative interaction records. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| 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/SecY/SecY-notes.md Generic GO:0005515 protein-binding rows for SecY should be removed as uninformative interaction records. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| 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/SecY/SecY-notes.md Generic GO:0005515 protein-binding rows for SecY should be removed as uninformative interaction records. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| 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/SecY/SecY-notes.md Generic GO:0005515 protein-binding rows for SecY should be removed as uninformative interaction records. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| 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/SecY/SecY-notes.md Generic GO:0005515 protein-binding rows for SecY should be removed as uninformative interaction records. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| 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/SecY/SecY-notes.md Generic GO:0005515 protein-binding rows for SecY should be removed as uninformative interaction records. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| 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/SecY/SecY-notes.md Generic GO:0005515 protein-binding rows for SecY should be removed as uninformative interaction records. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| 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/SecY/SecY-notes.md Generic GO:0005515 protein-binding rows for SecY should be removed as uninformative interaction records. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0005515 protein binding | IPI PMID:20855604 Lateral opening of a translocon upon entry of protein sugges... | 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/SecY/SecY-notes.md Generic GO:0005515 protein-binding rows for SecY should be removed as uninformative interaction records. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0005515 protein binding | IPI PMID:21255212 The bacterial SRP receptor, SecA and the ribosome use overla... | 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/SecY/SecY-notes.md Generic GO:0005515 protein-binding rows for SecY should be removed as uninformative interaction records. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0005515 protein binding | IPI PMID:31699901 Noncompetitive binding of PpiD and YidC to the SecYEG transl... | 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/SecY/SecY-notes.md Generic GO:0005515 protein-binding rows for SecY should be removed as uninformative interaction records. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| 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/SecY/SecY-notes.md Generic GO:0005515 protein-binding rows for SecY should be removed as uninformative interaction records. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0005515 protein binding | IPI PMID:9294424 In vivo cross-linking of the SecA and SecY subunits of the E... | 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/SecY/SecY-notes.md Generic GO:0005515 protein-binding rows for SecY should be removed as uninformative interaction records. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: SecY is an integral plasma-membrane channel subunit. Reason: The annotation correctly places SecY in the E. coli inner membrane where SecYEG acts. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000097337 · PANTHER:PTN000097337 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:P0AGA2 · UniProtKB:P0AGA2 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:P16336 · UniProtKB:P16336 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/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0005886 plasma membrane | IDA PMID:15919996 Global topology analysis of the Escherichia coli inner membr... | ACCEPT | Summary: SecY is an integral plasma-membrane channel subunit. Reason: The annotation correctly places SecY in the E. coli inner membrane where SecYEG acts. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0005886 plasma membrane | IDA PMID:17309111 Comparison of SDS- and methanol-assisted protein solubilizat... | ACCEPT | Summary: SecY is an integral plasma-membrane channel subunit. Reason: The annotation correctly places SecY in the E. coli inner membrane where SecYEG acts. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0005886 plasma membrane | IDA PMID:2538820 Site-specific antibodies against the PrlA (secY) protein of ... | ACCEPT | Summary: SecY is an integral plasma-membrane channel subunit. Reason: The annotation correctly places SecY in the E. coli inner membrane where SecYEG acts. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0005886 plasma membrane | IDA PMID:2538820 Site-specific antibodies against the PrlA (secY) protein of ... | ACCEPT | Summary: SecY is an integral plasma-membrane channel subunit. Reason: The annotation correctly places SecY in the E. coli inner membrane where SecYEG acts. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0005886 plasma membrane | IDA PMID:3004955 The SecY membrane component of the bacterial protein export ... | ACCEPT | Summary: SecY is an integral plasma-membrane channel subunit. Reason: The annotation correctly places SecY in the E. coli inner membrane where SecYEG acts. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0005886 plasma membrane | IDA PMID:7650029 SecYEG and SecA are the stoichiometric components of preprot... | ACCEPT | Summary: SecY is an integral plasma-membrane channel subunit. Reason: The annotation correctly places SecY in the E. coli inner membrane where SecYEG acts. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: SecY is an integral plasma-membrane channel subunit. Reason: The annotation correctly places SecY in the E. coli inner membrane where SecYEG acts. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0005886 plasma membrane | TAS PMID:2202723 Structure, function, and biogenesis of SecY, an integral mem... | ACCEPT | Summary: SecY is an integral plasma-membrane channel subunit. Reason: The annotation correctly places SecY in the E. coli inner membrane where SecYEG acts. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0006605 protein targeting | IEA GO_REF:0000104 | MODIFY | Summary: This generic targeting row should be replaced by the specific SecYEG-dependent processes. Reason: SecYEG acts as the membrane channel used by SRP-delivered nascent chains and SecA-delivered precursors; GO:0006616 and GO:0043952 capture those SecY roles more precisely than generic protein targeting. Proposed replacements: SRP-dependent cotranslational protein targeting to membrane, translocation protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:10397756 Both targeting pathways intersect at the translocation pore because they are equally affected by a blocked translocation channel. |
| GO:0006616 SRP-dependent cotranslational protein targeting to membrane, translocation | IBA GO_REF:0000033 | ACCEPT | Summary: SecYEG is the translocon pore used by the bacterial SRP cotranslational insertion route. Reason: The same SecYEG channel used for SecA-driven export is also the membrane pore for SRP-delivered inner-membrane-protein substrates. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000097217 · PANTHER:PTN000097217 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. SGD:S000004370 · SGD:S000004370 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:P0AGA2 · UniProtKB:P0AGA2 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:P61619 · UniProtKB:P61619 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/SecY/SecY-notes.md The SecYEG pore is used by both the post-translational SecA/SecB route for secretory proteins and the SRP route for cotranslational membrane-protein insertion. PMID:10397756 Both targeting pathways intersect at the translocation pore because they are equally affected by a blocked translocation channel. |
| GO:0006616 SRP-dependent cotranslational protein targeting to membrane, translocation | IDA PMID:10397756 In vitro studies with purified components reveal signal reco... | ACCEPT | Summary: SecYEG is the translocon pore used by the bacterial SRP cotranslational insertion route. Reason: The same SecYEG channel used for SecA-driven export is also the membrane pore for SRP-delivered inner-membrane-protein substrates. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md The SecYEG pore is used by both the post-translational SecA/SecB route for secretory proteins and the SRP route for cotranslational membrane-protein insertion. PMID:10397756 Both targeting pathways intersect at the translocation pore because they are equally affected by a blocked translocation channel. |
| GO:0006616 SRP-dependent cotranslational protein targeting to membrane, translocation | IDA PMID:9564033 The Escherichia coli SRP and SecB targeting pathways converg... | ACCEPT | Summary: SecYEG is the translocon pore used by the bacterial SRP cotranslational insertion route. Reason: The same SecYEG channel used for SecA-driven export is also the membrane pore for SRP-delivered inner-membrane-protein substrates. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md The SecYEG pore is used by both the post-translational SecA/SecB route for secretory proteins and the SRP route for cotranslational membrane-protein insertion. PMID:10397756 Both targeting pathways intersect at the translocation pore because they are equally affected by a blocked translocation channel. |
| GO:0006886 intracellular protein transport | IMP PMID:2254269 Characterization of cold-sensitive secY mutants of Escherich... | MODIFY | Summary: This transport term is true but less specific than Sec-complex transport. Reason: SecY acts as the pore of the Sec channel; GO:0043952 is the precise process term. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0008320 transmembrane protein transporter activity | IBA GO_REF:0000033 | ACCEPT | Summary: SecY is the pore-forming protein transmembrane transporter subunit of SecYEG. Reason: SecY forms the central channel and lateral gate of the SecYEG protein-conducting pore. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000097217 · PANTHER:PTN000097217 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. SGD:S000004370 · SGD:S000004370 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:P0AGA2 · UniProtKB:P0AGA2 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/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0008320 transmembrane protein transporter activity | IDA PMID:1531482 SecY, SecE, and band 1 form the membrane-embedded domain of ... | ACCEPT | Summary: SecY is the pore-forming protein transmembrane transporter subunit of SecYEG. Reason: SecY forms the central channel and lateral gate of the SecYEG protein-conducting pore. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0008320 transmembrane protein transporter activity | IDA PMID:2139227 Solubilization and functional reconstitution of the protein-... | ACCEPT | Summary: SecY is the pore-forming protein transmembrane transporter subunit of SecYEG. Reason: SecY forms the central channel and lateral gate of the SecYEG protein-conducting pore. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0008320 transmembrane protein transporter activity | IDA PMID:2167176 The purified E. coli integral membrane protein SecY/E is suf... | ACCEPT | Summary: SecY is the pore-forming protein transmembrane transporter subunit of SecYEG. Reason: SecY forms the central channel and lateral gate of the SecYEG protein-conducting pore. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0008320 transmembrane protein transporter activity | IDA PMID:3017993 The secY protein can act post-translationally to promote bac... | ACCEPT | Summary: SecY is the pore-forming protein transmembrane transporter subunit of SecYEG. Reason: SecY forms the central channel and lateral gate of the SecYEG protein-conducting pore. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0008320 transmembrane protein transporter activity | IDA PMID:7650029 SecYEG and SecA are the stoichiometric components of preprot... | ACCEPT | Summary: SecY is the pore-forming protein transmembrane transporter subunit of SecYEG. Reason: SecY forms the central channel and lateral gate of the SecYEG protein-conducting pore. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0015031 protein transport | IEA GO_REF:0000002 | MODIFY | Summary: This broad protein-transport row should be made Sec-specific. Reason: SecY mediates protein transport by the Sec complex. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0016020 membrane | IDA PMID:3004955 The SecY membrane component of the bacterial protein export ... | MODIFY | Summary: SecY is specifically an inner/plasma membrane protein. Reason: The generic membrane term should be replaced by GO:0005886 plasma membrane for E. coli SecY. Proposed replacements: plasma membrane Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0016020 membrane | IDA PMID:8253068 A novel membrane protein involved in protein translocation a... | MODIFY | Summary: SecY is specifically an inner/plasma membrane protein. Reason: The generic membrane term should be replaced by GO:0005886 plasma membrane for E. coli SecY. Proposed replacements: plasma membrane Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0016020 membrane | IEA GO_REF:0000120 | MODIFY | Summary: SecY is specifically an inner/plasma membrane protein. Reason: The generic membrane term should be replaced by GO:0005886 plasma membrane for E. coli SecY. Proposed replacements: plasma membrane Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0016020 membrane | NAS PMID:8253068 A novel membrane protein involved in protein translocation a... | MODIFY | Summary: SecY is specifically an inner/plasma membrane protein. Reason: The generic membrane term should be replaced by GO:0005886 plasma membrane for E. coli SecY. Proposed replacements: plasma membrane Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0031522 cell envelope Sec protein transport complex | IBA GO_REF:0000033 | ACCEPT | Summary: SecY is a core subunit of the SecYEG cell-envelope Sec transport complex. Reason: SecY, SecE, and SecG constitute the membrane-embedded domain of the preprotein translocase. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000097337 · PANTHER:PTN000097337 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:P0AGA2 · UniProtKB:P0AGA2 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/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:1531482 These data establish that the subunits of SecY/E are firmly associated and that it is the associated complex which is active for translocation. |
| GO:0031522 cell envelope Sec protein transport complex | IDA PMID:1531482 SecY, SecE, and band 1 form the membrane-embedded domain of ... | ACCEPT | Summary: SecY is a core subunit of the SecYEG cell-envelope Sec transport complex. Reason: SecY, SecE, and SecG constitute the membrane-embedded domain of the preprotein translocase. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:1531482 These data establish that the subunits of SecY/E are firmly associated and that it is the associated complex which is active for translocation. |
| GO:0031522 cell envelope Sec protein transport complex | IDA PMID:2167176 The purified E. coli integral membrane protein SecY/E is suf... | ACCEPT | Summary: SecY is a core subunit of the SecYEG cell-envelope Sec transport complex. Reason: SecY, SecE, and SecG constitute the membrane-embedded domain of the preprotein translocase. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:1531482 These data establish that the subunits of SecY/E are firmly associated and that it is the associated complex which is active for translocation. |
| GO:0031522 cell envelope Sec protein transport complex | IPI PMID:16292303 Structure of the E. coli protein-conducting channel bound to... | ACCEPT | Summary: SecY is a core subunit of the SecYEG cell-envelope Sec transport complex. Reason: SecY, SecE, and SecG constitute the membrane-embedded domain of the preprotein translocase. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:1531482 These data establish that the subunits of SecY/E are firmly associated and that it is the associated complex which is active for translocation. |
| GO:0031522 cell envelope Sec protein transport complex | IPI PMID:27924919 A central cavity within the holo-translocon suggests a mecha... | ACCEPT | Summary: SecY is a core subunit of the SecYEG cell-envelope Sec transport complex. Reason: SecY, SecE, and SecG constitute the membrane-embedded domain of the preprotein translocase. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:1531482 These data establish that the subunits of SecY/E are firmly associated and that it is the associated complex which is active for translocation. |
| GO:0043952 protein transport by the Sec complex | IDA PMID:11867527 The SecYEG preprotein translocation channel is a conformatio... | ACCEPT | Summary: SecY is a core protein transport by the Sec complex component. Reason: The SecY pore directly executes Sec-dependent movement of polypeptides into or across the membrane. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0043952 protein transport by the Sec complex | IDA PMID:1531482 SecY, SecE, and band 1 form the membrane-embedded domain of ... | ACCEPT | Summary: SecY is a core protein transport by the Sec complex component. Reason: The SecY pore directly executes Sec-dependent movement of polypeptides into or across the membrane. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0043952 protein transport by the Sec complex | IDA PMID:2167176 The purified E. coli integral membrane protein SecY/E is suf... | ACCEPT | Summary: SecY is a core protein transport by the Sec complex component. Reason: The SecY pore directly executes Sec-dependent movement of polypeptides into or across the membrane. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0043952 protein transport by the Sec complex | IDA PMID:24550475 Membrane protein insertion and proton-motive-force-dependent... | ACCEPT | Summary: SecY is a core protein transport by the Sec complex component. Reason: The SecY pore directly executes Sec-dependent movement of polypeptides into or across the membrane. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0043952 protein transport by the Sec complex | IDA PMID:7650029 SecYEG and SecA are the stoichiometric components of preprot... | ACCEPT | Summary: SecY is a core protein transport by the Sec complex component. Reason: The SecY pore directly executes Sec-dependent movement of polypeptides into or across the membrane. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0043952 protein transport by the Sec complex | IEA GO_REF:0000104 | ACCEPT | Summary: SecY is a core protein transport by the Sec complex component. Reason: The SecY pore directly executes Sec-dependent movement of polypeptides into or across the membrane. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0043952 protein transport by the Sec complex | IMP PMID:2254269 Characterization of cold-sensitive secY mutants of Escherich... | ACCEPT | Summary: SecY is a core protein transport by the Sec complex component. Reason: The SecY pore directly executes Sec-dependent movement of polypeptides into or across the membrane. Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0065002 intracellular protein transmembrane transport | EXP PMID:6297749 A previously unidentified gene in the spc operon of Escheric... | MODIFY | Summary: This is a correct but less specific parent of Sec-complex protein transmembrane transport. Reason: GO:0043952 records the same transport role with the appropriate Sec-complex specificity. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0065002 intracellular protein transmembrane transport | EXP PMID:6370688 A defined mutation in the protein export gene within the spc... | MODIFY | Summary: This is a correct but less specific parent of Sec-complex protein transmembrane transport. Reason: GO:0043952 records the same transport role with the appropriate Sec-complex specificity. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0065002 intracellular protein transmembrane transport | IDA PMID:2139227 Solubilization and functional reconstitution of the protein-... | MODIFY | Summary: This is a correct but less specific parent of Sec-complex protein transmembrane transport. Reason: GO:0043952 records the same transport role with the appropriate Sec-complex specificity. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0065002 intracellular protein transmembrane transport | IDA PMID:3017993 The secY protein can act post-translationally to promote bac... | MODIFY | Summary: This is a correct but less specific parent of Sec-complex protein transmembrane transport. Reason: GO:0043952 records the same transport role with the appropriate Sec-complex specificity. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0065002 intracellular protein transmembrane transport | IDA PMID:7650029 SecYEG and SecA are the stoichiometric components of preprot... | MODIFY | Summary: This is a correct but less specific parent of Sec-complex protein transmembrane transport. Reason: GO:0043952 records the same transport role with the appropriate Sec-complex specificity. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0065002 intracellular protein transmembrane transport | IEA GO_REF:0000104 | MODIFY | Summary: This is a correct but less specific parent of Sec-complex protein transmembrane transport. Reason: GO:0043952 records the same transport role with the appropriate Sec-complex specificity. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
| GO:0065002 intracellular protein transmembrane transport | IMP PMID:2254269 Characterization of cold-sensitive secY mutants of Escherich... | MODIFY | Summary: This is a correct but less specific parent of Sec-complex protein transmembrane transport. Reason: GO:0043952 records the same transport role with the appropriate Sec-complex specificity. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecY/SecY-notes.md SecY is the pore-forming alpha subunit of the SecYEG inner-membrane channel. PMID:7650029 These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase. |
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