ID   GSPH_VIBCH              Reviewed;         194 AA.
AC   P45774; Q9JPZ7;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Type II secretion system protein H;
DE            Short=T2SS minor pseudopilin H;
DE   AltName: Full=Cholera toxin secretion protein EpsH;
DE   AltName: Full=General secretion pathway protein H;
DE   Flags: Precursor;
GN   Name=epsH; OrderedLocusNames=VC_2729;
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   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 36-194, AND FUNCTION.
RX   PubMed=18241884; DOI=10.1016/j.jmb.2007.08.041;
RA   Yanez M.E., Korotkov K.V., Abendroth J., Hol W.G.;
RT   "Structure of the minor pseudopilin EpsH from the Type 2 secretion system
RT   of Vibrio cholerae.";
RL   J. Mol. Biol. 377:91-103(2008).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 33-194, AND FUNCTION.
RX   PubMed=24316251; DOI=10.1016/j.bbapap.2013.11.013;
RA   Raghunathan K., Vago F.S., Grindem D., Ball T., Wedemeyer W.J.,
RA   Bagdasarian M., Arvidson D.N.;
RT   "The 1.59Aa resolution structure of the minor pseudopilin EpsH of Vibrio
RT   cholerae reveals a long flexible loop.";
RL   Biochim. Biophys. Acta 1844:406-415(2014).
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 (By similarity). Part of the pseudopilus
CC       tip complex that is critical for the recognition and binding of
CC       secretion substrates (PubMed:18241884, PubMed:24316251).
CC       {ECO:0000250|UniProtKB:Q00515, ECO:0000269|PubMed:18241884,
CC       ECO:0000269|PubMed:24316251}.
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:Q00515}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:Q00515}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- PTM: Cleaved by prepilin peptidase. {ECO:0000250|UniProtKB:Q00515}.
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:Q00515}.
CC   -!- SIMILARITY: Belongs to the GSP H family. {ECO:0000305}.
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DR   EMBL; L33796; AAA58789.1; -; Genomic_DNA.
DR   EMBL; AE003852; AAF95869.1; -; Genomic_DNA.
DR   PIR; C82041; C82041.
DR   RefSeq; NP_232356.1; NC_002505.1.
DR   RefSeq; WP_000127537.1; NZ_LT906614.1.
DR   PDB; 2QV8; X-ray; 2.00 A; A/B=36-194.
DR   PDB; 4DQ9; X-ray; 1.59 A; A/B=33-194.
DR   PDBsum; 2QV8; -.
DR   PDBsum; 4DQ9; -.
DR   AlphaFoldDB; P45774; -.
DR   SMR; P45774; -.
DR   STRING; 243277.VC_2729; -.
DR   DNASU; 2614892; -.
DR   EnsemblBacteria; AAF95869; AAF95869; VC_2729.
DR   KEGG; vch:VC_2729; -.
DR   PATRIC; fig|243277.26.peg.2604; -.
DR   eggNOG; COG2165; Bacteria.
DR   HOGENOM; CLU_111963_0_1_6; -.
DR   OMA; YVMFNAF; -.
DR   BioCyc; VCHO:VC2729-MON; -.
DR   EvolutionaryTrace; P45774; -.
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; IPR022346; T2SS_GspH.
DR   InterPro; IPR002416; T2SS_protein-GspH.
DR   Pfam; PF12019; GspH; 1.
DR   PRINTS; PR00885; BCTERIALGSPH.
DR   SUPFAM; SSF54523; SSF54523; 1.
DR   TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 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..6
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT                   /id="PRO_0000024226"
FT   CHAIN           7..194
FT                   /note="Type II secretion system protein H"
FT                   /id="PRO_0000024227"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         7
FT                   /note="N-methylphenylalanine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT   HELIX           34..59
FT                   /evidence="ECO:0007829|PDB:4DQ9"
FT   STRAND          63..68
FT                   /evidence="ECO:0007829|PDB:4DQ9"
FT   TURN            69..72
FT                   /evidence="ECO:0007829|PDB:4DQ9"
FT   STRAND          73..80
FT                   /evidence="ECO:0007829|PDB:4DQ9"
FT   TURN            81..83
FT                   /evidence="ECO:0007829|PDB:4DQ9"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:4DQ9"
FT   STRAND          91..93
FT                   /evidence="ECO:0007829|PDB:4DQ9"
FT   STRAND          95..98
FT                   /evidence="ECO:0007829|PDB:4DQ9"
FT   STRAND          103..109
FT                   /evidence="ECO:0007829|PDB:4DQ9"
FT   HELIX           123..125
FT                   /evidence="ECO:0007829|PDB:4DQ9"
FT   STRAND          146..149
FT                   /evidence="ECO:0007829|PDB:4DQ9"
FT   STRAND          158..164
FT                   /evidence="ECO:0007829|PDB:4DQ9"
FT   STRAND          172..177
FT                   /evidence="ECO:0007829|PDB:4DQ9"
FT   STRAND          183..186
FT                   /evidence="ECO:0007829|PDB:4DQ9"
SQ   SEQUENCE   194 AA;  21756 MW;  BF24460CE323BD30 CRC64;
     MTATRGFTLL EILLVLVLVS ASAVAVIATF PVSVKDEAKI SAQSFYQRLL LLNEEAILSG
     QDFGVRIDVD TRRLTFLQLT ADKGWQKWQN DKMTNQTTLK EGLQLDFELG GGAWQKDDRL
     FNPGSLFDEE MFADEKKEQK QEPAPQLFVL SSGEVTPFTL SIFPKGQEPD EQWRVTAQEN
     GTLRLLAPGE SDEE