GSPF_VIBCH
ID GSPF_VIBCH Reviewed; 406 AA.
AC P45780; Q9JPZ5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Type II secretion system protein F;
DE Short=T2SS protein F;
DE AltName: Full=Cholera toxin secretion protein EpsF;
DE AltName: Full=General secretion pathway protein F;
GN Name=epsF; OrderedLocusNames=VC_2731;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=El Tor TRH7000;
RA Overbye L.J.;
RT "Organization of the general secretion pathway genes in Vibrio cholerae.";
RL Thesis (1994), Michigan State University, United States.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 56-170 IN COMPLEX WITH CALCIUM,
RP AND SUBUNIT.
RX PubMed=19324092; DOI=10.1016/j.jsb.2009.03.009;
RA Abendroth J., Mitchell D.D., Korotkov K.V., Johnson T.L., Kreger A.,
RA Sandkvist M., Hol W.G.;
RT "The three-dimensional structure of the cytoplasmic domains of EpsF from
RT the type 2 secretion system of Vibrio cholerae.";
RL J. Struct. Biol. 166:303-315(2009).
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 (PubMed:19324092). Interacts with EpsE/GspE and
CC EpsL/GspL components (By similarity). {ECO:0000250|UniProtKB:Q00513,
CC ECO:0000250|UniProtKB:Q00514, ECO:0000269|PubMed:19324092}.
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; L33796; AAA58787.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF95871.1; -; Genomic_DNA.
DR PIR; E82041; E82041.
DR RefSeq; NP_232358.1; NC_002505.1.
DR RefSeq; WP_000718700.1; NZ_LT906614.1.
DR PDB; 2VMA; X-ray; 1.90 A; A/B=56-170.
DR PDB; 2VMB; X-ray; 1.95 A; A/B=56-170.
DR PDB; 3C1Q; X-ray; 1.70 A; A/B=56-170.
DR PDBsum; 2VMA; -.
DR PDBsum; 2VMB; -.
DR PDBsum; 3C1Q; -.
DR AlphaFoldDB; P45780; -.
DR SMR; P45780; -.
DR STRING; 243277.VC_2731; -.
DR DNASU; 2614894; -.
DR EnsemblBacteria; AAF95871; AAF95871; VC_2731.
DR GeneID; 57741323; -.
DR KEGG; vch:VC_2731; -.
DR PATRIC; fig|243277.26.peg.2606; -.
DR eggNOG; COG1459; Bacteria.
DR HOGENOM; CLU_035032_0_1_6; -.
DR OMA; FEPLMIL; -.
DR BioCyc; VCHO:VC2731-MON; -.
DR EvolutionaryTrace; P45780; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
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 3D-structure; Calcium; Cell inner membrane; Cell membrane; Membrane;
KW Metal-binding; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..406
FT /note="Type II secretion system protein F"
FT /id="PRO_0000207836"
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..223
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00513"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00513"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..406
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:0007744|PDB:2VMA, ECO:0007744|PDB:2VMB"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:2VMA, ECO:0007744|PDB:2VMB"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:2VMA, ECO:0007744|PDB:2VMB"
FT HELIX 65..80
FT /evidence="ECO:0007829|PDB:3C1Q"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:3C1Q"
FT HELIX 99..113
FT /evidence="ECO:0007829|PDB:3C1Q"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:3C1Q"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:3C1Q"
FT HELIX 131..143
FT /evidence="ECO:0007829|PDB:3C1Q"
FT HELIX 146..168
FT /evidence="ECO:0007829|PDB:3C1Q"
SQ SEQUENCE 406 AA; 44931 MW; E3131EA383FDE83E CRC64;
MAAFEYKALD AKGRHKKGVI EGDNARQVRQ RLKEQSLVPM EVVETQVKAA RSRSQGFAFK
RGISTPDLAL ITRQLATLVQ SGMPLEECLR AVAEQSEKPR IRTMLVAVRA KVTEGYTLSD
SLGDYPHVFD ELFRSMVAAG EKSGHLDSVL ERLADYAENR QKMRSKLQQA MIYPVVLVVF
AVGIVAFLLA AVVPKIVGQF VQMGQALPAS TQFLLDASDF LQHWGISLLV GLLMLIYLVR
WLLTKPDIRL RWDRRVISLP VIGKIARGLN TARFARTLSI CTSSAIPILD GMRVAVDVMT
NQFVKQQVLA AAENVREGSS LRKALEQTKL FPPMMLHMIA SGEQSGELEG MLTRAADNQD
NSFESTVNIA LGIFTPALIA LMAGMVLFIV MATLMPILEM NNLMSR
