GSPM_VIBCH
ID GSPM_VIBCH Reviewed; 165 AA.
AC P41851; Q9KNK8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Type II secretion system protein M;
DE Short=T2SS protein M;
DE AltName: Full=Cholera toxin secretion protein EpsM;
DE AltName: Full=General secretion pathway protein M;
GN Name=epsM; OrderedLocusNames=VC_2724;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=El Tor TRH7000;
RX PubMed=8406031; DOI=10.1016/0378-1119(93)90520-d;
RA Overbye L.J., Sandkvist M., Bagdasarian M.;
RT "Genes required for extracellular secretion of enterotoxin are clustered in
RT Vibrio cholerae.";
RL Gene 132:101-106(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EPSL.
RX PubMed=10322014; DOI=10.1128/jb.181.10.3129-3135.1999;
RA Sandkvist M., Hough L.P., Bagdasarian M.M., Bagdasarian M.;
RT "Direct interaction of the EpsL and EpsM proteins of the general secretion
RT apparatus in Vibrio cholerae.";
RL J. Bacteriol. 181:3129-3135(1999).
RN [4]
RP FUNCTION, AND INTERACTION WITH EPSE AND EPSL.
RX PubMed=10633109; DOI=10.1128/jb.182.3.742-748.2000;
RA Sandkvist M., Keith J.M., Bagdasarian M., Howard S.P.;
RT "Two regions of EpsL involved in species-specific protein-protein
RT interactions with EpsE and EpsM of the general secretion pathway in Vibrio
RT cholerae.";
RL J. Bacteriol. 182:742-748(2000).
RN [5]
RP SUBUNIT, INTERACTION WITH EPSL, AND DOMAIN.
RX PubMed=17921296; DOI=10.1128/jb.01256-07;
RA Johnson T.L., Scott M.E., Sandkvist M.;
RT "Mapping critical interactive sites within the periplasmic domain of the
RT Vibrio cholerae type II secretion protein EpsM.";
RL J. Bacteriol. 189:9082-9089(2007).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19251862; DOI=10.1128/jb.01701-08;
RA Lybarger S.R., Johnson T.L., Gray M.D., Sikora A.E., Sandkvist M.;
RT "Docking and assembly of the type II secretion complex of Vibrio
RT cholerae.";
RL J. Bacteriol. 191:3149-3161(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 65-165, AND SUBUNIT.
RX PubMed=15081815; DOI=10.1016/j.jmb.2004.01.064;
RA Abendroth J., Rice A.E., McLuskey K., Bagdasarian M., Hol W.G.;
RT "The crystal structure of the periplasmic domain of the type II secretion
RT system protein EpsM from Vibrio cholerae: the simplest version of the
RT ferredoxin fold.";
RL J. Mol. Biol. 338:585-596(2004).
CC -!- FUNCTION: Inner membrane component of the type II secretion system
CC required for the energy-dependent secretion of extracellular factors
CC such as proteases and toxins from the periplasm. Plays a role in the
CC complex assembly and recruits EpsL resulting in a stable complex in the
CC inner membrane. Provides thus a link between the energy-providing EpsE
CC protein in the cytoplasm and the rest of the T2SS machinery.
CC {ECO:0000269|PubMed:10322014, ECO:0000269|PubMed:10633109,
CC ECO:0000269|PubMed:19251862}.
CC -!- SUBUNIT: Type II secretion system is composed of four main components:
CC the outer membrane complex, the inner membrane complex, the cytoplasmic
CC secretion ATPase and the periplasm-spanning pseudopilus (By
CC similarity). Forms homodimers (PubMed:15081815, PubMed:17921296).
CC Interacts with EpsL/GspL (PubMed:10322014, PubMed:10633109). Interacts
CC with EpsE/GspE (PubMed:10633109). Interacts with EpsF/GspF
CC (PubMed:10633109). {ECO:0000250|UniProtKB:Q00514,
CC ECO:0000269|PubMed:10322014, ECO:0000269|PubMed:10633109,
CC ECO:0000269|PubMed:15081815, ECO:0000269|PubMed:17921296}.
CC -!- INTERACTION:
CC P41851; P45782: epsL; NbExp=2; IntAct=EBI-6400843, EBI-6400836;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: The periplasmic region found in the proximity of the
CC transmembrane appears to be critical for a stable interaction with
CC EpsL. {ECO:0000269|PubMed:17921296}.
CC -!- DISRUPTION PHENOTYPE: Absence of EpsM results in a decreased amount of
CC EpsL in type II secretion system complexes.
CC {ECO:0000269|PubMed:19251862}.
CC -!- SIMILARITY: Belongs to the GSP M family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF95864.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L13660; AAA60935.1; -; Genomic_DNA.
DR EMBL; L33796; AAA58794.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF95864.1; ALT_INIT; Genomic_DNA.
DR PIR; F82040; F82040.
DR PIR; JN0847; JN0847.
DR RefSeq; NP_232351.1; NC_002505.1.
DR RefSeq; WP_000661339.1; NZ_LT906614.1.
DR PDB; 1UV7; X-ray; 1.70 A; A/B=65-165.
DR PDBsum; 1UV7; -.
DR AlphaFoldDB; P41851; -.
DR SMR; P41851; -.
DR IntAct; P41851; 1.
DR STRING; 243277.VC_2724; -.
DR DNASU; 2615552; -.
DR EnsemblBacteria; AAF95864; AAF95864; VC_2724.
DR GeneID; 57741316; -.
DR GeneID; 66938402; -.
DR KEGG; vch:VC_2724; -.
DR PATRIC; fig|243277.26.peg.2599; -.
DR eggNOG; COG3149; Bacteria.
DR HOGENOM; CLU_118900_3_0_6; -.
DR OMA; PQGNKIQ; -.
DR EvolutionaryTrace; P41851; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015627; C:type II protein secretion system complex; IEA:InterPro.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro.
DR DisProt; DP00725; -.
DR InterPro; IPR007690; T2SS_GspM.
DR InterPro; IPR023229; T2SS_M_periplasmic_sf.
DR Pfam; PF04612; T2SSM; 1.
DR PIRSF; PIRSF006291; GspM; 1.
DR SUPFAM; SSF103054; SSF103054; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..165
FT /note="Type II secretion system protein M"
FT /id="PRO_0000207328"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P25061"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..165
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P25061"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:1UV7"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:1UV7"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:1UV7"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:1UV7"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:1UV7"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:1UV7"
SQ SEQUENCE 165 AA; 18652 MW; 8456C7317CE6F515 CRC64;
MKELLAPVQA WWRSVTPREQ KMVMGMGALT VLAIAYWGIW QPLSERTAQA QARLQTEKQL
LSWVSENAND IVTLRAQGGS DAPSDQPLNQ VITNSTRQFN IELIRVQPRG EMMQVWIQPL
PFSQLVSWIA YLQERQGVSV DAIDIDRGKV NGVVEVKRLQ LKRGG
