ID   GSPK_KLEPN              Reviewed;         326 AA.
AC   P15750;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Type II secretion system protein K;
DE            Short=T2SS protein K;
DE   AltName: Full=General secretion pathway protein K;
DE   AltName: Full=Pullulanase secretion protein PulK;
DE   Flags: Precursor;
GN   Name=pulK;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UNF 5023;
RX   PubMed=2129543; DOI=10.1007/bf00633815;
RA   Reyss I., Pugsley A.P.;
RT   "Five additional genes in the pulC-O operon of the Gram-negative bacterium
RT   Klebsiella oxytoca UNF5023 which are required for pullulanase secretion.";
RL   Mol. Gen. Genet. 222:176-184(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 126-326.
RC   STRAIN=UNF 5023;
RX   PubMed=2162463; DOI=10.1111/j.1365-2958.1990.tb00604.x;
RA   Pugsley A.P., Reyss I.;
RT   "Five genes at the 3' end of the Klebsiella pneumoniae pulC operon are
RT   required for pullulanase secretion.";
RL   Mol. Microbiol. 4:365-379(1990).
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 PulG. {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; M32613; AAA25133.1; -; Genomic_DNA.
DR   EMBL; X52462; CAA36696.1; -; Genomic_DNA.
DR   PIR; S11799; S11799.
DR   AlphaFoldDB; P15750; -.
DR   SMR; P15750; -.
DR   TCDB; 3.A.15.1.1; the outer membrane protein secreting main terminal branch (mtb) family.
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..7
FT                   /note="Leader sequence"
FT                   /evidence="ECO:0000250|UniProtKB:Q00518"
FT                   /id="PRO_0000449560"
FT   CHAIN           8..326
FT                   /note="Type II secretion system protein K"
FT                   /id="PRO_0000449561"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..326
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   326 AA;  36153 MW;  5EF626A744C490B9 CRC64;
     MNHRQRGIAL LMVLLILALM MVLASAMTER SARMYQQTAT TLDNLQAKWY ALGAETLAAA
     LLQRDALDSP NQTHLAQNWA QQGRRFTVND GEIYATITDA QACFNLNAIN QRGDDESAAV
     PYPAQIFTRL LENLGSEPLR ALQLTAALRD WVDDDRQPLL NGAEDEVYMA QSPGYLTGNQ
     PLQDVSELRL LAGMDAALYQ RLLPYVCALA DETLQVNVNT LQPDRAALLA ALFPAELTLV
     EARQLLQARA ATGWSSVAAF LSQPALQKTD TAAARPWLAV HSERFIATFS VVMGNARYQQ
     RSLLQKQGRT FGVVQRRYGI YWVADE