GSPJ_VIBCH
ID GSPJ_VIBCH Reviewed; 221 AA.
AC P45776; Q9KNK5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Type II secretion system protein J;
DE Short=T2SS protein J;
DE AltName: Full=Cholera toxin secretion protein EpsJ;
DE AltName: Full=General secretion pathway protein J;
DE Flags: Precursor;
GN Name=epsJ; OrderedLocusNames=VC_2727;
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:Q00517}.
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:Q00517}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:Q00517}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Cleaved by prepilin peptidase. {ECO:0000250|UniProtKB:Q00517}.
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:Q00517}.
CC -!- SIMILARITY: Belongs to the GSP J family. {ECO:0000305}.
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DR EMBL; L33796; AAA58791.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF95867.1; -; Genomic_DNA.
DR PIR; A82041; A82041.
DR RefSeq; NP_232354.1; NC_002505.1.
DR RefSeq; WP_000269343.1; NZ_LT906614.1.
DR AlphaFoldDB; P45776; -.
DR SMR; P45776; -.
DR STRING; 243277.VC_2727; -.
DR DNASU; 2614890; -.
DR EnsemblBacteria; AAF95867; AAF95867; VC_2727.
DR KEGG; vch:VC_2727; -.
DR PATRIC; fig|243277.26.peg.2602; -.
DR eggNOG; COG4795; Bacteria.
DR HOGENOM; CLU_093850_0_0_6; -.
DR OMA; WYYPYPE; -.
DR BioCyc; VCHO:VC2727-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; IEA:InterPro.
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; IPR010055; T2SS_protein-GspJ.
DR Pfam; PF07963; N_methyl; 1.
DR Pfam; PF11612; T2SSJ; 1.
DR SUPFAM; SSF54523; SSF54523; 1.
DR TIGRFAMs; TIGR01711; gspJ; 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..15
FT /note="Leader sequence"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT /id="PRO_0000024258"
FT CHAIN 16..221
FT /note="Type II secretion system protein J"
FT /id="PRO_0000024259"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000305"
FT MOD_RES 16
FT /note="N-methylphenylalanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT CONFLICT 188..190
FT /note="KVT -> ESD (in Ref. 1; AAA58791)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 221 AA; 25260 MW; AF3F4B943A1CC366 CRC64;
MWRTNQVSSR QNMAGFTLIE VLVAIAIFAS LSVGAYQVLN QVQRSNEISA ERTARLAELQ
RAMVIMDADF RQMALRQFRT DGEAPSEQIL QWKESLLDSD QHGLLFVRLG WHNPQQQFPR
GEVAKVGYRL FENRLERVWW RYPDTPAGQQ GLISPLLTGV EDWAVQFYLQ GEWSKEWVPT
NALPEAVKVT LRLKDYGEIE RIYLTGGGSL NMTQESVENA G
