GSPF_PSEAE
ID GSPF_PSEAE Reviewed; 405 AA.
AC Q00513;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Type II secretion system protein F;
DE Short=T2SS protein F;
DE AltName: Full=General secretion pathway protein F;
GN Name=xcpS; OrderedLocusNames=PA3102;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=1588814; DOI=10.1111/j.1365-2958.1992.tb01550.x;
RA Bally M., Filloux A., Akrim M., Ball G., Lazdunski A., Tommassen J.;
RT "Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp
RT genes and processing of secretory apparatus components by prepilin
RT peptidase.";
RL Mol. Microbiol. 6:1121-1131(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP TOPOLOGY, AND INTERACTION WITH XCPR AND XCPY.
RX PubMed=17464073; DOI=10.1099/mic.0.2006/002840-0;
RA Arts J., de Groot A., Ball G., Durand E., Khattabi M.E., Filloux A.,
RA Tommassen J., Koster M.;
RT "Interaction domains in the Pseudomonas aeruginosa type II secretory
RT apparatus component XcpS (GspF).";
RL Microbiology 153:1582-1592(2007).
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 XcpR/GspE and
CC XcpY/GspL components (PubMed:17464073). {ECO:0000250|UniProtKB:P45780,
CC ECO:0000250|UniProtKB:Q00514, ECO:0000269|PubMed:17464073}.
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; X62666; CAA44534.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06490.1; -; Genomic_DNA.
DR PIR; S25385; SKPSXS.
DR RefSeq; NP_251792.1; NC_002516.2.
DR RefSeq; WP_003091376.1; NZ_QZGE01000009.1.
DR AlphaFoldDB; Q00513; -.
DR SMR; Q00513; -.
DR STRING; 287.DR97_4831; -.
DR PaxDb; Q00513; -.
DR PRIDE; Q00513; -.
DR EnsemblBacteria; AAG06490; AAG06490; PA3102.
DR GeneID; 878732; -.
DR KEGG; pae:PA3102; -.
DR PATRIC; fig|208964.12.peg.3254; -.
DR PseudoCAP; PA3102; -.
DR HOGENOM; CLU_035032_0_1_6; -.
DR InParanoid; Q00513; -.
DR OMA; FEPLMIL; -.
DR PhylomeDB; Q00513; -.
DR BioCyc; PAER208964:G1FZ6-3158-MON; -.
DR Proteomes; UP000002438; Chromosome.
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; IDA:PseudoCAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IDA:PseudoCAP.
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; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..405
FT /note="Type II secretion system protein F"
FT /id="PRO_0000207835"
FT TOPO_DOM 1..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:17464073"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..219
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:17464073"
FT TRANSMEM 220..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:17464073"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..405
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:17464073"
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 405 AA; 44062 MW; BEE59B58724C167E CRC64;
MAAFEYLALD PSGRQQKGVL EADSARQVRQ LLRERQLAPL DVKPTRTREQ SGQGGRLTFA
RGLSARDLAL VTRQLATLVQ AALPIEEALR AAAAQSTSQR IQSMLLAVRA KVLEGHSLAG
SLREFPTAFP ELYRATVAAG EHAGHLGPVL EQLADYTEQR QQSRQKIQLA LLYPVILMVA
SLAIVGFLLG YVVPDVVRVF IDSGQTLPLL TRVLIGVSDW VKAWGALAFV AAIGGVIGFR
YALRKDAFRE RWHGFLLRVP LVGRLVRSTD TARFASTLAI LTRSGVPLVE ALAIAAEVIA
NRIIRNEVVK AAQKVREGAS LTRSLEATGQ FPPMMLHMIA SGERSGELDQ MLARTARNQE
NDLAAQIGLM VGLFEPFMLI FMGAVVLVIV LAILLPILSL NQLVG
