ID   GSPK_AERHY              Reviewed;         331 AA.
AC   P31760;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Type II secretion system protein K;
DE            Short=T2SS protein K;
DE   AltName: Full=General secretion pathway protein K;
DE   Flags: Precursor;
GN   Name=exeK;
OS   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ah65;
RX   PubMed=8407845; DOI=10.1128/jb.175.20.6695-6703.1993;
RA   Howard S.P., Critch J., Bedi A.;
RT   "Isolation and analysis of eight exe genes and their involvement in
RT   extracellular protein secretion and outer membrane assembly in Aeromonas
RT   hydrophila.";
RL   J. Bacteriol. 175:6695-6703(1993).
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 ExeG. {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}.
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DR   EMBL; X66504; CAA47132.1; -; Genomic_DNA.
DR   PIR; D49905; D49905.
DR   AlphaFoldDB; P31760; -.
DR   SMR; P31760; -.
DR   STRING; 1448139.AI20_16495; -.
DR   eggNOG; COG3156; Bacteria.
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   Transmembrane; Transmembrane helix; Transport.
FT   PROPEP          1..9
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000250|UniProtKB:Q00518"
FT                   /id="PRO_0000449553"
FT   CHAIN           10..331
FT                   /note="Type II secretion system protein K"
FT                   /id="PRO_0000449554"
FT   TRANSMEM        8..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..331
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   331 AA;  36693 MW;  8F7B1C0A0C03D2E6 CRC64;
     MPSCRRQGGM ALLVVLLILS VMVIIASNMS GRLQLELRRT GNLTAGKQAW WYAMSAEALV
     SKVLVQDFKD DPNVVNLGQN WARQDAVFPV DDGKLTGRVR DLQSCFNLNS LSVPLKDGIS
     GDDLEKQPYP VKAFRALLKQ LEVEDYEAVQ LTDAIRDWTD KDTALVSSYG AEDAYYEGLT
     PPYLTANQWM LSTDELRAVR GVSARLYARL APYVCALPSD KLLVNINTIK PEQAALLVAL
     YLDKVGLDDA KRVLTSRPQK GWKEKKAMTD QMPAPLSTIP GLDAVLDVKS SYFEARLIAE
     VGDTRARLES VFVRGKDNKL VMLRRLNGGA E