ID   GSPF_AERHY              Reviewed;         388 AA.
AC   P31743;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Type II secretion system protein F;
DE            Short=T2SS protein F;
DE   AltName: Full=General secretion pathway protein F;
GN   Name=exeF;
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=1640836; DOI=10.1111/j.1365-2958.1992.tb00856.x;
RA   Jiang B., Howard S.P.;
RT   "The Aeromonas hydrophila exeE gene, required both for protein secretion
RT   and normal outer membrane biogenesis, is a member of a general secretion
RT   pathway.";
RL   Mol. Microbiol. 6:1351-1361(1992).
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 ExeE and ExeL
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; X66504; CAA47127.1; -; Genomic_DNA.
DR   PIR; S22670; S22670.
DR   AlphaFoldDB; P31743; -.
DR   SMR; P31743; -.
DR   STRING; 1448139.AI20_16520; -.
DR   eggNOG; COG1459; 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: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..388
FT                   /note="Type II secretion system protein F"
FT                   /id="PRO_0000207830"
FT   TOPO_DOM        1..153
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00513"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        175..205
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00513"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        227..350
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00513"
FT   TRANSMEM        351..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        372..388
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P41441"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         79
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P45780"
FT   BINDING         133
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P45780"
FT   BINDING         137
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P45780"
SQ   SEQUENCE   388 AA;  43464 MW;  D47B1628F977ED50 CRC64;
     MTEGDSARQV RQQLREQGLT PLEVNETTEK AKREANRFVL FRRGASTSEL ALITRQLATL
     VGAGLTIEEA LRAVAEQCEK AHLRSLVATV RSKVVEGYSL ADSLGAFPHV FDQLFRSMVA
     AGEKSGHLEK VLNRLADYTE QRQHMRTKLL QAMIYPIVLT LVAVGVISIL LTAVVPKVVA
     QFEHMGQQLP ATTRFLIGTS ELMQHYGLWF LLLLFIGGFV WRWWLTDEKR RRHWHQVVLR
     LPVIGRVSRG LNTARFARTL SILNASAVPL LEGMKIAGEV LSNDFARTRI GEATERVREG
     TSLRKALDET KIFPPMMLHM IASGEQSGEL DSMLERAADN QDREFETQVN IALGVFEPLL
     VVSMAGVVLF IVMSILQPIL ELNNMVNL