ID   GSPI_VIBCH              Reviewed;         117 AA.
AC   P45775; Q9JPZ8;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Type II secretion system protein I;
DE            Short=T2SS minor pseudopilin I;
DE   AltName: Full=Cholera toxin secretion protein EpsI;
DE   AltName: Full=General secretion pathway protein I;
DE   Flags: Precursor;
GN   Name=epsI; OrderedLocusNames=VC_2728;
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).
CC   -!- FUNCTION: Component of the type II secretion system required for the
CC       energy-dependent secretion of extracellular factors such as proteases
CC       and toxins from the periplasm. Part of the pseudopilus tip complex that
CC       is critical for the recognition and binding of secretion substrates.
CC       {ECO:0000250|UniProtKB:Q00516}.
CC   -!- SUBUNIT: Type II secretion is composed of four main components: the
CC       outer membrane complex, the inner membrane complex, the cytoplasmic
CC       secretion ATPase and the periplasm-spanning pseudopilus. Interacts with
CC       core component EpsG. {ECO:0000250|UniProtKB:Q00516}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:Q00516}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- PTM: Cleaved by prepilin peptidase. {ECO:0000250|UniProtKB:Q00516}.
CC   -!- PTM: Methylated by prepilin peptidase at the amino group of the N-
CC       terminal phenylalanine once the leader sequence is cleaved by prepilin
CC       peptidase. {ECO:0000250|UniProtKB:Q00516}.
CC   -!- SIMILARITY: Belongs to the GSP I family. {ECO:0000305}.
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DR   EMBL; L33796; AAA58790.1; -; Genomic_DNA.
DR   EMBL; AE003852; AAF95868.1; -; Genomic_DNA.
DR   PIR; B82041; B82041.
DR   RefSeq; NP_232355.1; NC_002505.1.
DR   RefSeq; WP_000837699.1; NZ_LT906614.1.
DR   AlphaFoldDB; P45775; -.
DR   SMR; P45775; -.
DR   STRING; 243277.VC_2728; -.
DR   DNASU; 2614891; -.
DR   EnsemblBacteria; AAF95868; AAF95868; VC_2728.
DR   GeneID; 57741320; -.
DR   GeneID; 66938398; -.
DR   KEGG; vch:VC_2728; -.
DR   PATRIC; fig|243277.26.peg.2603; -.
DR   eggNOG; COG2165; Bacteria.
DR   HOGENOM; CLU_121289_3_1_6; -.
DR   OMA; RTWYWQQ; -.
DR   BioCyc; VCHO:VC2728-MON; -.
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; IPR012902; N_methyl_site.
DR   InterPro; IPR045584; Pilin-like.
DR   InterPro; IPR003413; T2SS_GspI_C.
DR   InterPro; IPR010052; T2SS_protein-GspI.
DR   PANTHER; PTHR38779; PTHR38779; 1.
DR   Pfam; PF07963; N_methyl; 1.
DR   Pfam; PF02501; T2SSI; 1.
DR   SUPFAM; SSF54523; SSF54523; 1.
DR   TIGRFAMs; TIGR01707; gspI; 1.
DR   TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR   PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Methylation;
KW   Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   PROPEP          1..6
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000024242"
FT   CHAIN           7..117
FT                   /note="Type II secretion system protein I"
FT                   /id="PRO_0000024243"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         7
FT                   /note="N-methylphenylalanine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
SQ   SEQUENCE   117 AA;  12837 MW;  D26BB486C272BE8B CRC64;
     MKSKRGFTLL EVLVALAIFA TAAISVIRSV SQHINTVNYL EEKMFAAMVV DNQMAQVMLN
     PQSLAAREGS EQMAGRTWYW KLSPVKTADN LLKAFDVSVA TEKGATPVVT VRSYVAN