位置:首页 > 蛋白库 > GSPF_XANCP
GSPF_XANCP
ID   GSPF_XANCP              Reviewed;         405 AA.
AC   P31744;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 3.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Type II secretion system protein F;
DE            Short=T2SS protein F;
DE   AltName: Full=General secretion pathway protein F;
GN   Name=xpsF; Synonyms=pefF; OrderedLocusNames=XCC0661;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=8000 NCPPB 1145;
RX   PubMed=1944223; DOI=10.1007/bf00267456;
RA   Dums F., Dow J.M., Daniels M.J.;
RT   "Structural characterization of protein secretion genes of the bacterial
RT   phytopathogen Xanthomonas campestris pathovar campestris: relatedness to
RT   secretion systems of other Gram-negative bacteria.";
RL   Mol. Gen. Genet. 229:357-364(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Xc1701;
RA   Hu N.-T.T., Hung M.-N., Wang K.C.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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 XpsE and XpsL
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA41804.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X59079; CAA41804.1; ALT_INIT; Genomic_DNA.
DR   EMBL; L02630; AAC27376.3; -; Genomic_DNA.
DR   EMBL; AE008922; AAM39977.1; -; Genomic_DNA.
DR   PIR; S17938; S17938.
DR   PIR; T12057; T12057.
DR   RefSeq; NP_636053.1; NC_003902.1.
DR   RefSeq; WP_011035901.1; NC_003902.1.
DR   AlphaFoldDB; P31744; -.
DR   SMR; P31744; -.
DR   STRING; 340.xcc-b100_3694; -.
DR   EnsemblBacteria; AAM39977; AAM39977; XCC0661.
DR   KEGG; xcc:XCC0661; -.
DR   PATRIC; fig|190485.4.peg.725; -.
DR   eggNOG; COG1459; Bacteria.
DR   HOGENOM; CLU_035032_2_1_6; -.
DR   OMA; YVVPQFV; -.
DR   Proteomes; UP000001010; 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: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; 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   PROSITE; PS00874; T2SP_F; 1.
PE   3: Inferred from homology;
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_0000207837"
FT   TOPO_DOM        1..169
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00513"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        191..218
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00513"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        240..370
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00513"
FT   TRANSMEM        371..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        392..405
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P41441"
FT   BINDING         98
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"
FT   CONFLICT        67
FT                   /note="A -> S (in Ref. 2; AAC27376)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        114..115
FT                   /note="GG -> A (in Ref. 1; CAA41804)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        346
FT                   /note="G -> A (in Ref. 1; CAA41804)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   405 AA;  44024 MW;  B5623E53CD137E23 CRC64;
     MPLYRYKALD AHGEMLDGQM EAANDAEVAL RLQEQGHLPV ETRLATGENG SPSLRMLLRK
     KPFDNAALVQ FTQQLATLIG AGQPLDRALS ILMDLPEDDK SRRVIADIRD TVRGGAPLSV
     ALERQHGLFS KLYINMVRAG EAGGSMQDTL QRLADYLERS RALKGKVINA LIYPAILLAV
     VGCALLFLLG YVVPQFAQMY ESLDVALPWF TQAVLSVGLL VRDWWLVLVV IPGVLGLWLD
     RKRRNAAFRA ALDAWLLRQK VIGSLIARLE TARLTRTLGT LLRNGVPLLA AIGIARNVMS
     NTALVEDVAA AADDVKNGHG LSMSLARGKR FPRLALQMIQ VGEESGALDT MLLKTADTFE
     LETAQAIDRA LAALVPLITL VLASVVGLVI ISVLVPLYDL TNAIG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024