SecG

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005515 protein binding	IPI PMID:12359079 Membrane topology inversion of SecG detected by labeling wit...	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/SecG/SecG-notes.md Generic GO:0005515 protein-binding rows for SecG 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/SecG/SecG-notes.md Generic GO:0005515 protein-binding rows for SecG 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/SecG/SecG-notes.md Generic GO:0005515 protein-binding rows for SecG 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/SecG/SecG-notes.md Generic GO:0005515 protein-binding rows for SecG 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/SecG/SecG-notes.md Generic GO:0005515 protein-binding rows for SecG 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/SecG/SecG-notes.md Generic GO:0005515 protein-binding rows for SecG 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: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/SecG/SecG-notes.md Generic GO:0005515 protein-binding rows for SecG 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: SecG is an integral plasma-membrane SecYEG channel subunit. Reason: SecG is localized to the bacterial inner membrane as a small SecYEG accessory subunit. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002149719 · PANTHER:PTN002149719 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:P0AG99 · UniProtKB:P0AG99 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/SecG/SecG-notes.md SecG is the small accessory 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: SecG is an integral plasma-membrane SecYEG channel subunit. Reason: SecG is localized to the bacterial inner membrane as a small SecYEG accessory subunit. Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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:8253068 A novel membrane protein involved in protein translocation a...	ACCEPT	Summary: SecG is an integral plasma-membrane SecYEG channel subunit. Reason: SecG is localized to the bacterial inner membrane as a small SecYEG accessory subunit. Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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:0000044	ACCEPT	Summary: SecG is an integral plasma-membrane SecYEG channel subunit. Reason: SecG is localized to the bacterial inner membrane as a small SecYEG accessory subunit. Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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:0006616 SRP-dependent cotranslational protein targeting to membrane, translocation	IDA PMID:10397756 In vitro studies with purified components reveal signal reco...	ACCEPT	Summary: SecG contributes to the SecYEG pore used by the SRP cotranslational insertion route. Reason: SecG is part of the SecYEG channel engaged by SRP-delivered nascent inner-membrane proteins. Supporting Evidence: file:ECOLI/SecG/SecG-notes.md Like SecY and SecE, SecG acts in the SecYEG pore used by both SecA/SecB post-translational export and SRP-dependent cotranslational 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: SecG contributes to the SecYEG pore used by the SRP cotranslational insertion route. Reason: SecG is part of the SecYEG channel engaged by SRP-delivered nascent inner-membrane proteins. Supporting Evidence: file:ECOLI/SecG/SecG-notes.md Like SecY and SecE, SecG acts in the SecYEG pore used by both SecA/SecB post-translational export and SRP-dependent cotranslational 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	IDA PMID:7650029 SecYEG and SecA are the stoichiometric components of preprot...	MODIFY	Summary: This broad protein-transport row should be made Sec-specific. Reason: SecG acts in protein transport by the Sec complex. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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: SecG contributes to SecYEG protein transmembrane transporter activity. Reason: The IBA contributes_to row is appropriately scoped for a small accessory channel subunit. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002149719 · PANTHER:PTN002149719 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:P0AG99 · UniProtKB:P0AG99 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/SecG/SecG-notes.md SecG is the small accessory 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: SecG contributes to SecYEG protein transmembrane transporter activity. Reason: The direct EcoCyc row captures SecG activity at the level of the SecYEG channel. SecG is an accessory subunit rather than the pore-forming transporter by itself, so the synthesized core function records this as contributes_to protein transmembrane transporter activity. Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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:0009306 protein secretion	IEA GO_REF:0000002	MODIFY	Summary: This secretion annotation is a broad proxy for Sec-dependent export. Reason: GO:0043952 is the precise process for the SecG channel role. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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:0015450 protein-transporting ATPase activity	IEA GO_REF:0000002	REMOVE	Summary: SecG is not a protein-transporting ATPase. Reason: This InterPro2GO transfer conflates the membrane SecG subunit with SecA, the ATPase motor of bacterial Sec export. Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is not the ATPase motor of protein transport. 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: SecG is specifically an inner/plasma membrane protein. Reason: The generic membrane term should be replaced by GO:0005886 plasma membrane for E. coli SecG. Proposed replacements: plasma membrane Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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:0000002	MODIFY	Summary: SecG is specifically an inner/plasma membrane protein. Reason: The generic membrane term should be replaced by GO:0005886 plasma membrane for E. coli SecG. Proposed replacements: plasma membrane Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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: SecG is specifically an inner/plasma membrane protein. Reason: The generic membrane term should be replaced by GO:0005886 plasma membrane for E. coli SecG. Proposed replacements: plasma membrane Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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	IDA PMID:7650029 SecYEG and SecA are the stoichiometric components of preprot...	ACCEPT	Summary: SecG is a SecYEG cell-envelope Sec transport complex subunit. Reason: SecG associates with SecY and SecE in the membrane-embedded translocase. Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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	IPI PMID:16292303 Structure of the E. coli protein-conducting channel bound to...	ACCEPT	Summary: SecG is a SecYEG cell-envelope Sec transport complex subunit. Reason: SecG associates with SecY and SecE in the membrane-embedded translocase. Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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	IPI PMID:27924919 A central cavity within the holo-translocon suggests a mecha...	ACCEPT	Summary: SecG is a SecYEG cell-envelope Sec transport complex subunit. Reason: SecG associates with SecY and SecE in the membrane-embedded translocase. Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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	IBA GO_REF:0000033	ACCEPT	Summary: SecG contributes to protein transport by the Sec complex. Reason: SecG stimulates the SecYEG channel during preprotein translocation. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002149719 · PANTHER:PTN002149719 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:P0AG99 · UniProtKB:P0AG99 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/SecG/SecG-notes.md SecG is the small accessory 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:11867527 The SecYEG preprotein translocation channel is a conformatio...	ACCEPT	Summary: SecG contributes to protein transport by the Sec complex. Reason: SecG stimulates the SecYEG channel during preprotein translocation. Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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: SecG contributes to protein transport by the Sec complex. Reason: SecG stimulates the SecYEG channel during preprotein translocation. Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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: SecG contributes to protein transport by the Sec complex. Reason: SecG stimulates the SecYEG channel during preprotein translocation. Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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: SecG contributes to protein transport by the Sec complex. Reason: SecG stimulates the SecYEG channel during preprotein translocation. Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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	IBA GO_REF:0000033	MODIFY	Summary: This transmembrane-transport row is correct but less specific than Sec-complex protein transport. Reason: GO:0043952 captures SecG function in the SecYEG channel more precisely. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN002149719 · PANTHER:PTN002149719 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:P0AG99 · UniProtKB:P0AG99 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. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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 transmembrane-transport row is correct but less specific than Sec-complex protein transport. Reason: GO:0043952 captures SecG function in the SecYEG channel more precisely. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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:8253068 A novel membrane protein involved in protein translocation a...	MODIFY	Summary: This transmembrane-transport row is correct but less specific than Sec-complex protein transport. Reason: GO:0043952 captures SecG function in the SecYEG channel more precisely. Proposed replacements: protein transport by the Sec complex Supporting Evidence: file:ECOLI/SecG/SecG-notes.md SecG is the small accessory 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.

Gene Description

Existing Annotations Review

Core Functions

SecG is the small SecYEG accessory subunit that stabilizes or stimulates channel-mediated preprotein translocation and contributes to, but does not independently provide, SecYEG protein transmembrane transporter activity.

References

Suggested Questions for Experts

Suggested Experiments

📚 Additional Documentation

Notes

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