UniProtKB - P76576 (YFGM_ECOLI)
Protein
Ancillary SecYEG translocon subunit
Gene
yfgM
Organism
Escherichia coli (strain K12)
Status
Functioni
May mediate protein transfer from the SecYEG translocon to the periplasmic chaperone network via its periplasmic C-terminal region (PubMed:24855643). In addition, at the cytosolic site, acts as a negative regulator of RcsB (PubMed:26092727). In stationary phase, the FtsH-dependent degradation of YfgM ensures the release of RcsB from YfgM and thereby permits cellular protection by the Rcs phosphorelay system (PubMed:26092727). May coordinate stress responses across the inner membrane via a dynamic protein-protein interaction network inside and outside of the membrane (PubMed:26092727).2 Publications
Activity regulationi
Is stable during exponential growth and degraded in stationary phase by the essential FtsH protease. Degradation is influenced by the alarmone (p)ppGpp, but not by inorganic polyphosphate (polyP), RpoS, RcsB or PpiD.1 Publication
GO - Molecular functioni
- protein-containing complex binding Source: EcoCyc
Keywordsi
Molecular function | Chaperone |
Enzyme and pathway databases
BioCyci | EcoCyc:G7321-MONOMER |
Names & Taxonomyi
Protein namesi | Recommended name: Ancillary SecYEG translocon subunitCuratedAlternative name(s): Periplasmic chaperone YfgM1 Publication |
Gene namesi | Name:yfgM Ordered Locus Names:b2513, JW2497 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Plasma membrane
- Cell inner membrane 1 Publication; Single-pass type II membrane protein 1 Publication; Periplasmic side 1 Publication
Plasma Membrane
- integral component of external side of plasma membrane Source: EcoCyc
Other locations
- protein-containing complex Source: EcoCyc
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 23 | Cytoplasmic1 PublicationAdd BLAST | 23 | |
Transmembranei | 24 – 43 | HelicalSequence analysisAdd BLAST | 20 | |
Topological domaini | 44 – 206 | Periplasmic1 PublicationAdd BLAST | 163 |
Keywords - Cellular componenti
Cell inner membrane, Cell membrane, MembranePathology & Biotechi
Disruption phenotypei
Deletion of the gene in combination with either surA or skp causes increased sensitivity to vancomycin and exacerbates the RpoE-dependent envelope stress response in a skp deletion strain (PubMed:24855643). Strains lacking the gene show a decreased survival rate at low pH (PubMed:25403562). Several cell envelope proteins are misfolded/mistargeted and turned-over in the absence of YfgM, including HdeB and AnsB (PubMed:25403562).2 Publications
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 2 – 3 | Missing : Is able to insert into the inner membrane but is no longer degraded in stationary growth phase. 1 Publication | 2 | |
Mutagenesisi | 2 | E → A, K or Q: Stable under all growth conditions. 1 Publication | 1 | |
Mutagenesisi | 2 | E → D: Decreases degradation by FtsH. 1 Publication | 1 | |
Mutagenesisi | 3 | I → A: Stable under all growth conditions. 1 Publication | 1 | |
Mutagenesisi | 4 | Y → A: Destabilizes the protein, which is prone to degradation in early or late exponential phase. 1 Publication | 1 | |
Mutagenesisi | 5 | E → A: Destabilizes the protein, which is prone to degradation in early or late exponential phase. 1 Publication | 1 | |
Mutagenesisi | 6 | N → A: Decreases degradation by FtsH. 1 Publication | 1 | |
Mutagenesisi | 7 | E → A: Decreases degradation by FtsH. 1 Publication | 1 | |
Mutagenesisi | 8 | N → A: Decreases degradation by FtsH. 1 Publication | 1 | |
Mutagenesisi | 9 | D → A: Decreases degradation by FtsH. 1 Publication | 1 | |
Mutagenesisi | 10 | Q → A: Decreases degradation by FtsH. 1 Publication | 1 | |
Mutagenesisi | 11 | V → D: Decreases degradation by FtsH. 1 Publication | 1 | |
Mutagenesisi | 12 | E → A: Decreases degradation by FtsH. 1 Publication | 1 | |
Mutagenesisi | 13 | A → D: Decreases degradation by FtsH. 1 Publication | 1 | |
Mutagenesisi | 14 | V → D: Decreases degradation by FtsH. 1 Publication | 1 | |
Mutagenesisi | 15 | K → A: Does not affect degradation by FtsH. 1 Publication | 1 | |
Mutagenesisi | 16 | R → A: Does not affect degradation by FtsH. 1 Publication | 1 | |
Mutagenesisi | 17 | F → A: Does not affect degradation by FtsH. 1 Publication | 1 | |
Mutagenesisi | 18 | F → A: Does not affect degradation by FtsH. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000214364 | 1 – 206 | Ancillary SecYEG translocon subunitAdd BLAST | 206 |
Proteomic databases
jPOSTi | P76576 |
PaxDbi | P76576 |
PRIDEi | P76576 |
Interactioni
Subunit structurei
Protein-protein interaction databases
BioGRIDi | 4260588, 38 interactors 851320, 1 interactor |
DIPi | DIP-12043N |
IntActi | P76576, 5 interactors |
STRINGi | 511145.b2513 |
Family & Domainsi
Domaini
The first 14 N-terminal residues form the YfgM degron, which directs the protein to FtsH for proteolysis.1 Publication
Sequence similaritiesi
Belongs to the YfgM family.Curated
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | COG2976, Bacteria |
HOGENOMi | CLU_084785_0_0_6 |
InParanoidi | P76576 |
Family and domain databases
Gene3Di | 1.25.40.10, 1 hit |
InterProi | View protein in InterPro IPR011990, TPR-like_helical_dom_sf IPR018704, TPR_21 IPR026039, UPF0070 |
PANTHERi | PTHR38035, PTHR38035, 1 hit |
Pfami | View protein in Pfam PF09976, TPR_21, 1 hit |
PIRSFi | PIRSF006170, YfgM, 1 hit |
SUPFAMi | SSF48452, SSF48452, 1 hit |
i Sequence
Sequence statusi: Complete.
P76576-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MEIYENENDQ VEAVKRFFAE NGKALAVGVI LGVGALIGWR YWNSHQVDSA
60 70 80 90 100
RSASLAYQNA VTAVSEGKPD SIPAAEKFAA ENKNTYGALA SLELAQQFVD
110 120 130 140 150
KNELEKAAAQ LQQGLADTSD ENLKAVINLR LARVQVQLKQ ADAALKTLDT
160 170 180 190 200
IKGEGWAAIV ADLRGEALLS KGDKQGARSA WEAGVKSDVT PALSEMMQMK
INNLSI
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00096 Genomic DNA Translation: AAC75566.1 AP009048 Genomic DNA Translation: BAA16399.2 |
PIRi | H65027 |
RefSeqi | NP_417008.1, NC_000913.3 WP_000409205.1, NZ_STEB01000011.1 |
Genome annotation databases
EnsemblBacteriai | AAC75566; AAC75566; b2513 BAA16399; BAA16399; BAA16399 |
GeneIDi | 57732385 946981 |
KEGGi | ecj:JW2497 eco:b2513 |
PATRICi | fig|511145.12.peg.2612 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00096 Genomic DNA Translation: AAC75566.1 AP009048 Genomic DNA Translation: BAA16399.2 |
PIRi | H65027 |
RefSeqi | NP_417008.1, NC_000913.3 WP_000409205.1, NZ_STEB01000011.1 |
3D structure databases
SMRi | P76576 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 4260588, 38 interactors 851320, 1 interactor |
DIPi | DIP-12043N |
IntActi | P76576, 5 interactors |
STRINGi | 511145.b2513 |
Proteomic databases
jPOSTi | P76576 |
PaxDbi | P76576 |
PRIDEi | P76576 |
Genome annotation databases
EnsemblBacteriai | AAC75566; AAC75566; b2513 BAA16399; BAA16399; BAA16399 |
GeneIDi | 57732385 946981 |
KEGGi | ecj:JW2497 eco:b2513 |
PATRICi | fig|511145.12.peg.2612 |
Organism-specific databases
EchoBASEi | EB3961 |
Phylogenomic databases
eggNOGi | COG2976, Bacteria |
HOGENOMi | CLU_084785_0_0_6 |
InParanoidi | P76576 |
Enzyme and pathway databases
BioCyci | EcoCyc:G7321-MONOMER |
Miscellaneous databases
PROi | PR:P76576 |
Family and domain databases
Gene3Di | 1.25.40.10, 1 hit |
InterProi | View protein in InterPro IPR011990, TPR-like_helical_dom_sf IPR018704, TPR_21 IPR026039, UPF0070 |
PANTHERi | PTHR38035, PTHR38035, 1 hit |
Pfami | View protein in Pfam PF09976, TPR_21, 1 hit |
PIRSFi | PIRSF006170, YfgM, 1 hit |
SUPFAMi | SSF48452, SSF48452, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | YFGM_ECOLI | |
Accessioni | P76576Primary (citable) accession number: P76576 Secondary accession number(s): P76982, P76983 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 15, 1998 |
Last sequence update: | February 1, 1997 | |
Last modified: | April 7, 2021 | |
This is version 137 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families