ID   EPSK_VIBCH              Reviewed;         336 AA.
AC   P45781; Q9KNK6;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Type II secretion system protein K;
DE            Short=T2SS protein K;
DE   AltName: Full=Cholera toxin secretion protein EpsK;
DE   AltName: Full=General secretion pathway protein K;
DE   Flags: Precursor;
GN   Name=epsK; OrderedLocusNames=VC_2726;
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. Plays a role in pseudopilus assembly and
CC       seems to control its length. Interacts with the pseudopilus tip complex
CC       that is critical for the recognition and binding of secretion
CC       substrates. {ECO:0000250|UniProtKB:Q00518}.
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:Q00518}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:Q00518}.
CC   -!- PTM: Cleaved by prepilin peptidase. {ECO:0000250|UniProtKB:Q00518}.
CC   -!- SIMILARITY: Belongs to the GSP K 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; AAA58792.1; -; Genomic_DNA.
DR   EMBL; AE003852; AAF95866.1; -; Genomic_DNA.
DR   PIR; H82040; H82040.
DR   RefSeq; NP_232353.1; NC_002505.1.
DR   RefSeq; WP_001201881.1; NZ_LT906614.1.
DR   AlphaFoldDB; P45781; -.
DR   SMR; P45781; -.
DR   STRING; 243277.VC_2726; -.
DR   DNASU; 2614889; -.
DR   EnsemblBacteria; AAF95866; AAF95866; VC_2726.
DR   GeneID; 57741318; -.
DR   KEGG; vch:VC_2726; -.
DR   PATRIC; fig|243277.26.peg.2601; -.
DR   eggNOG; COG3156; Bacteria.
DR   HOGENOM; CLU_057294_0_0_6; -.
DR   OMA; AYWYSIG; -.
DR   BioCyc; VCHO:VC2726-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:0009306; P:protein secretion; IEA:InterPro.
DR   Gene3D; 1.10.40.60; -; 2.
DR   InterPro; IPR005628; GspK.
DR   InterPro; IPR038072; GspK_central_sf.
DR   InterPro; IPR045584; Pilin-like.
DR   PANTHER; PTHR38831; PTHR38831; 1.
DR   Pfam; PF03934; T2SSK; 1.
DR   PIRSF; PIRSF002786; XcpX; 1.
DR   SUPFAM; SSF158544; SSF158544; 2.
DR   SUPFAM; SSF54523; SSF54523; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   PROPEP          1..7
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000269|PubMed:10952301"
FT                   /id="PRO_0000449564"
FT   CHAIN           8..336
FT                   /note="Type II secretion system protein K"
FT                   /id="PRO_0000449565"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..336
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        179
FT                   /note="A -> G (in Ref. 1; AAA58792)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   336 AA;  37602 MW;  B217E623D6093045 CRC64;
     MRAKQRGVAL IVILLLLAVM VSIAATMAER LFSQFQRATH QLNYQQAYWY SLGVEALAKK
     GIEQSYQDSE TINLSQPWAL KEQTYPLDYG QVRGKIRDMQ ACFNLNALAG VKLTPDSVKK
     PYLLTVLQAL LEGLEVESYQ AEVIADSTLE FIDKDDSVRT AYGVEDSYYE SMIPAYMAAD
     TWLADASEWR AVQQVGGETM NKALPYVCAL PTDQWRLNVN TLPAEQAALL AAMFSPTLSP
     ESAKTLLEGR PFDGWASVDD FLAQSALTGV DNAVREEAKK YLSVDSHYFE LDAQVLVDTS
     RVRIRSLFYS NDKKTATVIR RRFGGISERV SDRSTE