GSPG_VIBCH
ID GSPG_VIBCH Reviewed; 146 AA.
AC P45773; Q9JPZ6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Type II secretion system core protein G;
DE Short=T2SS core protein G;
DE AltName: Full=Cholera toxin secretion protein EpsG;
DE AltName: Full=General secretion pathway protein G;
DE Flags: Precursor;
GN Name=epsG; OrderedLocusNames=VC_2730;
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;
RA Overbye L.J.;
RT "Organization of the general secretion pathway genes in Vibrio cholerae.";
RL Thesis (1994), Michigan State University, United States.
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, INTERACTION WITH ESPL, AND MUTAGENESIS OF ASP-100 AND THR-121.
RX PubMed=21255118; DOI=10.1111/j.1365-2958.2010.07487.x;
RA Gray M.D., Bagdasarian M., Hol W.G., Sandkvist M.;
RT "In vivo cross-linking of EpsG to EpsL suggests a role for EpsL as an
RT ATPase-pseudopilin coupling protein in the Type II secretion system of
RT Vibrio cholerae.";
RL Mol. Microbiol. 79:786-798(2011).
RN [4]
RP INDUCTION BY CYCLIC DI-GMP AND VPSR.
RX PubMed=28674069; DOI=10.1128/jb.00106-17;
RA Sloup R.E., Konal A.E., Severin G.B., Korir M.L., Bagdasarian M.M.,
RA Bagdasarian M., Waters C.M.;
RT "Cyclic Di-GMP and VpsR Induce the Expression of Type II Secretion in
RT Vibrio cholerae.";
RL J. Bacteriol. 199:0-0(2017).
CC -!- FUNCTION: Core component of the type II secretion system required for
CC the energy-dependent secretion of extracellular factors such as
CC proteases and toxins from the periplasm (PubMed:21255118). Pseudopilin
CC (pilin-like) protein that polymerizes to form the pseudopilus. Further
CC polymerization triggers pseudopilus growth (By similarity).
CC {ECO:0000250|UniProtKB:Q00514, ECO:0000269|PubMed:21255118}.
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. Forms
CC homomultimers (By similarity). Interacts with EspL (PubMed:21255118).
CC {ECO:0000250|UniProtKB:Q00514, ECO:0000269|PubMed:21255118}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q00514}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: By cyclic di-GMP and VpsR. {ECO:0000269|PubMed:28674069}.
CC -!- PTM: Cleaved by the prepilin peptidase. {ECO:0000250|UniProtKB:Q00514}.
CC -!- PTM: Methylated by prepilin peptidase at the amino group of the N-
CC terminal phenylalanine once the leader sequence is cleaved.
CC {ECO:0000250|UniProtKB:Q00514}.
CC -!- SIMILARITY: Belongs to the GSP G family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L33796; AAA58788.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF95870.1; -; Genomic_DNA.
DR PIR; D82041; D82041.
DR RefSeq; NP_232357.1; NC_002505.1.
DR RefSeq; WP_000738789.1; NZ_LT906614.1.
DR PDB; 3FU1; X-ray; 1.90 A; A/B=35-146.
DR PDB; 4LW9; X-ray; 1.90 A; A/B/C/D/E/F/I/J/K/L/Q/R=35-146.
DR PDBsum; 3FU1; -.
DR PDBsum; 4LW9; -.
DR AlphaFoldDB; P45773; -.
DR SMR; P45773; -.
DR STRING; 243277.VC_2730; -.
DR DNASU; 2614893; -.
DR EnsemblBacteria; AAF95870; AAF95870; VC_2730.
DR GeneID; 57741322; -.
DR KEGG; vch:VC_2730; -.
DR PATRIC; fig|243277.26.peg.2605; -.
DR eggNOG; COG2165; Bacteria.
DR HOGENOM; CLU_091705_2_1_6; -.
DR OMA; PWRNDYL; -.
DR BioCyc; VCHO:VC2730-MON; -.
DR EvolutionaryTrace; P45773; -.
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; IBA:GO_Central.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IBA:GO_Central.
DR InterPro; IPR000983; Bac_GSPG_pilin.
DR InterPro; IPR012902; N_methyl_site.
DR InterPro; IPR045584; Pilin-like.
DR InterPro; IPR013545; T2SS_protein-GspG_C.
DR InterPro; IPR010054; Type2_sec_GspG.
DR Pfam; PF07963; N_methyl; 1.
DR Pfam; PF08334; T2SSG; 1.
DR PRINTS; PR00813; BCTERIALGSPG.
DR SUPFAM; SSF54523; SSF54523; 1.
DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR TIGRFAMs; TIGR01710; typeII_sec_gspG; 1.
DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane; Methylation;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT PROPEP 1..9
FT /note="Leader sequence"
FT /evidence="ECO:0000250|UniProtKB:Q00514"
FT /id="PRO_0000449509"
FT CHAIN 10..146
FT /note="Type II secretion system core protein G"
FT /id="PRO_0000024211"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 10
FT /note="N-methylphenylalanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT MUTAGEN 100
FT /note="D->E: Complete loss of secretion."
FT /evidence="ECO:0000269|PubMed:21255118"
FT MUTAGEN 121
FT /note="T->L: Complete loss of secretion."
FT /evidence="ECO:0000269|PubMed:21255118"
FT HELIX 36..63
FT /evidence="ECO:0007829|PDB:3FU1"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:3FU1"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:3FU1"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:3FU1"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:3FU1"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:3FU1"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:3FU1"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3FU1"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:3FU1"
FT HELIX 139..145
FT /evidence="ECO:0007829|PDB:3FU1"
SQ SEQUENCE 146 AA; 16080 MW; 2B211AA994761E2A CRC64;
MKKMRKQTGF TLLEVMVVVV ILGILASFVV PNLLGNKEKA DQQKAVTDIV ALENALDMYK
LDNSVYPTTD QGLEALVTKP TNPEPRNYRE GGYIKRLPKD PWGNDYQYLS PGDKGTIDVF
TLGADGQEGG EGTGADIGNW NIQDFQ
