ID   GSPF_PECCC              Reviewed;         408 AA.
AC   P31705;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 87.
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   Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS   carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SCRI 193;
RX   PubMed=8326859; DOI=10.1111/j.1365-2958.1993.tb01589.x;
RA   Reeves P.J., Whitcombe D., Wharam S., Gibson M., Allison G., Bunce N.,
RA   Barallon R., Douglas P., Mulholland V., Stevens S., Walker S.,
RA   Salmond G.P.C.;
RT   "Molecular cloning and characterization of 13 out genes from Erwinia
RT   carotovora subspecies carotovora: genes encoding members of a general
RT   secretion pathway (GSP) widespread in Gram-negative bacteria.";
RL   Mol. Microbiol. 8:443-456(1993).
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; X70049; CAA49647.1; -; Genomic_DNA.
DR   PIR; S32860; S32860.
DR   AlphaFoldDB; P31705; -.
DR   SMR; P31705; -.
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   3: Inferred from homology;
KW   Calcium; Cell inner membrane; Cell membrane; Membrane; Metal-binding;
KW   Protein transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..408
FT                   /note="Type II secretion system protein F"
FT                   /id="PRO_0000207833"
FT   TOPO_DOM        1..173
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00513"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        195..224
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00513"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        246..379
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00513"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        401..408
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P41441"
FT   REGION          38..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         99
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P45780"
FT   BINDING         153
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P45780"
FT   BINDING         157
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P45780"
SQ   SEQUENCE   408 AA;  45162 MW;  0B58B58E51FDEE4A CRC64;
     MAQYHYQALD AQGKKCRGTQ EADSARQARQ LLRERGLVPL SVDENRGDQQ KSGSTGLSLR
     RKIRLSTSDL ALLTRQLATL VAASMPLEEA LDAVAKQSEK PHLSQLMAAV RSKVMEGHSL
     ADAMKCFPGS FERLYCAMVA AGETSGHLDA VLNRLADYTE QRQQMRSRIQ QAMIYPCVLT
     VVAIAVVSIL LSVVVPKVVE QFIHMKQALP LSTRVLMGMS DAVRTFGPWM LLALLAGFMA
     FRVMLRQEKR RVSFHRRLLH LPLIGRIARG LNTARYARTL SILNASAVPL LQAMRISGDV
     MSNDYARHRL SLATDAVREG VSLHKALEQT ALFPPMMRHM IASGERSGEL DSMLERAADN
     QDREFSSQMT LALGLFEPLL VVSMAAVVLF IVLAILQPIL QLNTLMSS