YFGM_ECOLI
ID YFGM_ECOLI Reviewed; 206 AA.
AC P76576; P76982; P76983;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Ancillary SecYEG translocon subunit {ECO:0000305};
DE AltName: Full=Periplasmic chaperone YfgM {ECO:0000303|PubMed:25403562};
GN Name=yfgM; OrderedLocusNames=b2513, JW2497;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 78-206.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH PPID.
RX PubMed=21210718; DOI=10.1021/pr101105c;
RA Maddalo G., Stenberg-Bruzell F., Gotzke H., Toddo S., Bjorkholm P.,
RA Eriksson H., Chovanec P., Genevaux P., Lehtio J., Ilag L.L., Daley D.O.;
RT "Systematic analysis of native membrane protein complexes in Escherichia
RT coli.";
RL J. Proteome Res. 10:1848-1859(2011).
RN [5]
RP FUNCTION, INTERACTION WITH PPID AND SECYEG TRANSLOCON, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24855643; DOI=10.1074/jbc.m113.541672;
RA Goetzke H., Palombo I., Muheim C., Perrody E., Genevaux P., Kudva R.,
RA Mueller M., Daley D.O.;
RT "YfgM is an ancillary subunit of the SecYEG translocon in Escherichia
RT coli.";
RL J. Biol. Chem. 289:19089-19097(2014).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=25403562; DOI=10.1074/mcp.m114.043216;
RA Goetzke H., Muheim C., Altelaar A.F., Heck A.J., Maddalo G., Daley D.O.;
RT "Identification of putative substrates for the periplasmic chaperone YfgM
RT in Escherichia coli using quantitative proteomics.";
RL Mol. Cell. Proteomics 14:216-226(2015).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH RCSB, DOMAIN, AND
RP MUTAGENESIS OF GLU-2; ILE-3; TYR-4; GLU-5; ASN-6; GLU-7; ASN-8; ASP-9;
RP GLN-10; VAL-11; GLU-12; ALA-13; VAL-14; LYS-15; ARG-16; PHE-17 AND PHE-18.
RX PubMed=26092727; DOI=10.1074/jbc.m115.648550;
RA Bittner L.M., Westphal K., Narberhaus F.;
RT "Conditional proteolysis of the membrane protein YfgM by the FtsH protease
RT depends on a novel N-terminal degron.";
RL J. Biol. Chem. 290:19367-19378(2015).
RN [8]
RP INTERACTION WITH THE SECYEG TRANSLOCON AND PPID.
RX PubMed=31699901; DOI=10.1074/jbc.ra119.010686;
RA Jauss B., Petriman N.A., Drepper F., Franz L., Sachelaru I., Welte T.,
RA Steinberg R., Warscheid B., Koch H.G.;
RT "Noncompetitive binding of PpiD and YidC to the SecYEG translocon expands
RT the global view on the SecYEG interactome in Escherichia coli.";
RL J. Biol. Chem. 294:19167-19183(2019).
CC -!- FUNCTION: May mediate protein transfer from the SecYEG translocon to
CC the periplasmic chaperone network via its periplasmic C-terminal region
CC (PubMed:24855643). In addition, at the cytosolic site, acts as a
CC negative regulator of RcsB (PubMed:26092727). In stationary phase, the
CC FtsH-dependent degradation of YfgM ensures the release of RcsB from
CC YfgM and thereby permits cellular protection by the Rcs phosphorelay
CC system (PubMed:26092727). May coordinate stress responses across the
CC inner membrane via a dynamic protein-protein interaction network inside
CC and outside of the membrane (PubMed:26092727).
CC {ECO:0000269|PubMed:24855643, ECO:0000269|PubMed:26092727}.
CC -!- ACTIVITY REGULATION: Is stable during exponential growth and degraded
CC in stationary phase by the essential FtsH protease. Degradation is
CC influenced by the alarmone (p)ppGpp, but not by inorganic polyphosphate
CC (polyP), RpoS, RcsB or PpiD. {ECO:0000269|PubMed:26092727}.
CC -!- SUBUNIT: Interacts with the SecYEG translocon (PubMed:24855643,
CC PubMed:31699901). Forms a complex with PpiD (PubMed:21210718,
CC PubMed:24855643, PubMed:31699901). Also interacts with RcsB
CC (PubMed:26092727). {ECO:0000269|PubMed:21210718,
CC ECO:0000269|PubMed:24855643, ECO:0000269|PubMed:26092727,
CC ECO:0000269|PubMed:31699901}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:21210718}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:21210718}; Periplasmic side
CC {ECO:0000269|PubMed:21210718}.
CC -!- DOMAIN: The first 14 N-terminal residues form the YfgM degron, which
CC directs the protein to FtsH for proteolysis.
CC {ECO:0000269|PubMed:26092727}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene in combination with either
CC surA or skp causes increased sensitivity to vancomycin and exacerbates
CC the RpoE-dependent envelope stress response in a skp deletion strain
CC (PubMed:24855643). Strains lacking the gene show a decreased survival
CC rate at low pH (PubMed:25403562). Several cell envelope proteins are
CC misfolded/mistargeted and turned-over in the absence of YfgM, including
CC HdeB and AnsB (PubMed:25403562). {ECO:0000269|PubMed:24855643,
CC ECO:0000269|PubMed:25403562}.
CC -!- SIMILARITY: Belongs to the YfgM family. {ECO:0000305}.
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DR EMBL; U00096; AAC75566.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16399.2; -; Genomic_DNA.
DR PIR; H65027; H65027.
DR RefSeq; NP_417008.1; NC_000913.3.
DR RefSeq; WP_000409205.1; NZ_STEB01000011.1.
DR AlphaFoldDB; P76576; -.
DR SMR; P76576; -.
DR BioGRID; 4260588; 38.
DR BioGRID; 851320; 1.
DR DIP; DIP-12043N; -.
DR IntAct; P76576; 5.
DR STRING; 511145.b2513; -.
DR TCDB; 3.A.5.1.1; the general secretory pathway (sec) family.
DR jPOST; P76576; -.
DR PaxDb; P76576; -.
DR PRIDE; P76576; -.
DR EnsemblBacteria; AAC75566; AAC75566; b2513.
DR EnsemblBacteria; BAA16399; BAA16399; BAA16399.
DR GeneID; 66673599; -.
DR GeneID; 946981; -.
DR KEGG; ecj:JW2497; -.
DR KEGG; eco:b2513; -.
DR PATRIC; fig|511145.12.peg.2612; -.
DR EchoBASE; EB3961; -.
DR eggNOG; COG2976; Bacteria.
DR HOGENOM; CLU_084785_0_0_6; -.
DR InParanoid; P76576; -.
DR OMA; RFFANNG; -.
DR PhylomeDB; P76576; -.
DR BioCyc; EcoCyc:G7321-MON; -.
DR PRO; PR:P76576; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0071575; C:integral component of external side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:EcoCyc.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR018704; TPR_21.
DR InterPro; IPR026039; YfgM.
DR PANTHER; PTHR38035; PTHR38035; 1.
DR Pfam; PF09976; TPR_21; 1.
DR PIRSF; PIRSF006170; YfgM; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Chaperone; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..206
FT /note="Ancillary SecYEG translocon subunit"
FT /id="PRO_0000214364"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21210718"
FT TRANSMEM 24..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..206
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:21210718"
FT MUTAGEN 2..3
FT /note="Missing: Is able to insert into the inner membrane
FT but is no longer degraded in stationary growth phase."
FT /evidence="ECO:0000269|PubMed:26092727"
FT MUTAGEN 2
FT /note="E->A,K,Q: Stable under all growth conditions."
FT /evidence="ECO:0000269|PubMed:26092727"
FT MUTAGEN 2
FT /note="E->D: Decreases degradation by FtsH."
FT /evidence="ECO:0000269|PubMed:26092727"
FT MUTAGEN 3
FT /note="I->A: Stable under all growth conditions."
FT /evidence="ECO:0000269|PubMed:26092727"
FT MUTAGEN 4
FT /note="Y->A: Destabilizes the protein, which is prone to
FT degradation in early or late exponential phase."
FT /evidence="ECO:0000269|PubMed:26092727"
FT MUTAGEN 5
FT /note="E->A: Destabilizes the protein, which is prone to
FT degradation in early or late exponential phase."
FT /evidence="ECO:0000269|PubMed:26092727"
FT MUTAGEN 6
FT /note="N->A: Decreases degradation by FtsH."
FT /evidence="ECO:0000269|PubMed:26092727"
FT MUTAGEN 7
FT /note="E->A: Decreases degradation by FtsH."
FT /evidence="ECO:0000269|PubMed:26092727"
FT MUTAGEN 8
FT /note="N->A: Decreases degradation by FtsH."
FT /evidence="ECO:0000269|PubMed:26092727"
FT MUTAGEN 9
FT /note="D->A: Decreases degradation by FtsH."
FT /evidence="ECO:0000269|PubMed:26092727"
FT MUTAGEN 10
FT /note="Q->A: Decreases degradation by FtsH."
FT /evidence="ECO:0000269|PubMed:26092727"
FT MUTAGEN 11
FT /note="V->D: Decreases degradation by FtsH."
FT /evidence="ECO:0000269|PubMed:26092727"
FT MUTAGEN 12
FT /note="E->A: Decreases degradation by FtsH."
FT /evidence="ECO:0000269|PubMed:26092727"
FT MUTAGEN 13
FT /note="A->D: Decreases degradation by FtsH."
FT /evidence="ECO:0000269|PubMed:26092727"
FT MUTAGEN 14
FT /note="V->D: Decreases degradation by FtsH."
FT /evidence="ECO:0000269|PubMed:26092727"
FT MUTAGEN 15
FT /note="K->A: Does not affect degradation by FtsH."
FT /evidence="ECO:0000269|PubMed:26092727"
FT MUTAGEN 16
FT /note="R->A: Does not affect degradation by FtsH."
FT /evidence="ECO:0000269|PubMed:26092727"
FT MUTAGEN 17
FT /note="F->A: Does not affect degradation by FtsH."
FT /evidence="ECO:0000269|PubMed:26092727"
FT MUTAGEN 18
FT /note="F->A: Does not affect degradation by FtsH."
FT /evidence="ECO:0000269|PubMed:26092727"
SQ SEQUENCE 206 AA; 22176 MW; 2DAFC595EBDC5EEB CRC64;
MEIYENENDQ VEAVKRFFAE NGKALAVGVI LGVGALIGWR YWNSHQVDSA RSASLAYQNA
VTAVSEGKPD SIPAAEKFAA ENKNTYGALA SLELAQQFVD KNELEKAAAQ LQQGLADTSD
ENLKAVINLR LARVQVQLKQ ADAALKTLDT IKGEGWAAIV ADLRGEALLS KGDKQGARSA
WEAGVKSDVT PALSEMMQMK INNLSI
