ID   GSPF_DICCH              Reviewed;         404 AA.
AC   P31704;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Type II secretion system protein F;
DE            Short=T2SS protein F;
DE   AltName: Full=General secretion pathway protein F;
DE   AltName: Full=Pectic enzymes secretion protein OutF;
GN   Name=outF;
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   INTERACTION WITH GSPE/OUTE AND GSPL/OUTL.
RX   PubMed=11266368; DOI=10.1093/embo-reports/kve042;
RA   Py B., Loiseau L., Barras F.;
RT   "An inner membrane platform in the type II secretion machinery of Gram-
RT   negative bacteria.";
RL   EMBO Rep. 2:244-248(2001).
CC   -!- FUNCTION: Component of the type II secretion system inner membrane
CC       complex required for the energy-dependent secretion of extracellular
CC       factors such as proteases and toxins from the periplasm.
CC       {ECO:0000250|UniProtKB:Q00514}.
CC   -!- SUBUNIT: Type II secretion system is composed of four main components:
CC       the outer membrane complex, the inner membrane complex, the cytoplasmic
CC       secretion ATPase and the periplasm-spanning pseudopilus (By
CC       similarity). Homodimer (By similarity). Interacts with OutE and OutL
CC       components (By similarity). {ECO:0000250|UniProtKB:P45780,
CC       ECO:0000250|UniProtKB:Q00513, ECO:0000250|UniProtKB:Q00514}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GSP F family. {ECO:0000305}.
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DR   EMBL; L02214; AAA24833.1; -; Genomic_DNA.
DR   PIR; D47021; D47021.
DR   AlphaFoldDB; P31704; -.
DR   SMR; P31704; -.
DR   IntAct; P31704; 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; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro.
DR   Gene3D; 1.20.81.30; -; 2.
DR   InterPro; IPR003004; GspF/PilC.
DR   InterPro; IPR011850; T2SS_GspF.
DR   InterPro; IPR001992; T2SS_GspF/T4SS_PilC_CS.
DR   InterPro; IPR018076; T2SS_GspF_dom.
DR   InterPro; IPR042094; T2SS_GspF_sf.
DR   PANTHER; PTHR30012; PTHR30012; 1.
DR   Pfam; PF00482; T2SSF; 2.
DR   PRINTS; PR00812; BCTERIALGSPF.
DR   TIGRFAMs; TIGR02120; GspF; 1.
DR   PROSITE; PS00874; T2SP_F; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell inner membrane; Cell membrane; Membrane; Metal-binding;
KW   Protein transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..404
FT                   /note="Type II secretion system protein F"
FT                   /id="PRO_0000207832"
FT   TOPO_DOM        1..171
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00513"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        193..222
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00513"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..374
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00513"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        396..404
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P41441"
FT   BINDING         97
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P45780"
FT   BINDING         151
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P45780"
FT   BINDING         155
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P45780"
SQ   SEQUENCE   404 AA;  44752 MW;  AB45B7D04B9B6FAE CRC64;
     MALFQYQALN AQGKKSQGMQ EADSARHARQ LLREKGLVPV KIEEQRGEAA PRSGFSLSFG
     RSHRIASDLA LLTRQLATLV AALPLEEALD AVAKQSEKPK LSALMAAVRA KVVEGHSLAE
     AMGNFPGSFE RLYCAMVAAG EASGHLDAVL NRLADYTEQR HEMRSRIQQA MIYPCVLTLV
     AISVVSILLS AVVPKVVEQF IHMKQALPLS TRLLMSASDA VRTYGPWVVL LLVLAIMGFR
     VLLRQEKHRL VFHRRLLFLP VVGRVARGLN TARYARTLSI LNSSAVPLLQ AMRISGDVLT
     NDYARFRLGQ ATDAVREGVT LHKALEQTAL FPPMMRHMIA SERRRARRHV NPRGDNQDRE
     FSAQMTLVLG LFEPLLVVSM AGIVLFIVLA ILQPILQLNT LMSM