ID   GSPK_DICCH              Reviewed;         354 AA.
AC   P24690;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   25-MAY-2022, entry version 84.
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=Pectic enzymes secretion protein OutK;
DE   Flags: Precursor;
GN   Name=outK;
OS   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EC16;
RX   PubMed=1429461; DOI=10.1128/jb.174.22.7385-7397.1992;
RA   Lindeberg M., Collmer A.;
RT   "Analysis of eight out genes in a cluster required for pectic enzyme
RT   secretion by Erwinia chrysanthemi: sequence comparison with secretion genes
RT   from other Gram-negative bacteria.";
RL   J. Bacteriol. 174:7385-7397(1992).
RN   [2]
RP   PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-324.
RC   STRAIN=EC16;
RX   PubMed=1992458; DOI=10.1073/pnas.88.3.1079;
RA   He S.Y., Lindeberg M., Chatterjee A.K., Collmer A.;
RT   "Cloned Erwinia chrysanthemi out genes enable Escherichia coli to
RT   selectively secrete a diverse family of heterologous proteins to its
RT   milieu.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:1079-1083(1991).
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 OutG. {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; L02214; AAA24838.1; -; Genomic_DNA.
DR   EMBL; M37886; AAA24829.2; -; Genomic_DNA.
DR   PIR; D37874; D37874.
DR   PIR; I47021; I47021.
DR   AlphaFoldDB; P24690; -.
DR   SMR; P24690; -.
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; 2.
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_0000449558"
FT   CHAIN           8..354
FT                   /note="Type II secretion system protein K"
FT                   /id="PRO_0000449559"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..354
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          114..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        54..73
FT                   /note="Missing (in Ref. 2; AAA24829)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   354 AA;  39155 MW;  4420ADFA2E25912F CRC64;
     MSRRQRGVAL LIVMLMLSLM VTIAASITER SGKAWQRTSN LLNRTQARWY ALGAEALISN
     VLQRDAQASP ESTFIGQPWS KVDHQMMADG TEIRAQALDG QACLNLNALS PARNVTPNNA
     SGNNTSGNNN AANGSSGNGN SPQPPKVGTS EQVPYAAQVF RQLMIVLGED PKQAERITDA
     LRDWLDEDSE PLMNGAEDDS YVNFHPGNQR MTDVTELRAV MGMDAALYRR LLPYVCVLPV
     DKLAINVNTL MPGSAPLLSA LFMGDISLDM AERILQQRPP QGWRNLNDFM GMSALPESGK
     NGARQVLVIK SDWFFADIQI RVDDSEFYQR SLFHRGKQIE VVQRQYGGYR TVNP