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PSTB_BURPS
ID   PSTB_BURPS              Reviewed;         282 AA.
AC   Q63V79;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Phosphate import ATP-binding protein PstB {ECO:0000255|HAMAP-Rule:MF_01702};
DE            EC=7.3.2.1 {ECO:0000255|HAMAP-Rule:MF_01702};
DE   AltName: Full=ABC phosphate transporter {ECO:0000255|HAMAP-Rule:MF_01702};
DE   AltName: Full=Phosphate-transporting ATPase {ECO:0000255|HAMAP-Rule:MF_01702};
GN   Name=pstB {ECO:0000255|HAMAP-Rule:MF_01702}; Synonyms=phoT;
GN   OrderedLocusNames=BPSL1362;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC   -!- FUNCTION: Part of the ABC transporter complex PstSACB involved in
CC       phosphate import. Responsible for energy coupling to the transport
CC       system. {ECO:0000255|HAMAP-Rule:MF_01702}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in);
CC         Xref=Rhea:RHEA:24440, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01702};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (PstB),
CC       two transmembrane proteins (PstC and PstA) and a solute-binding protein
CC       (PstS). {ECO:0000255|HAMAP-Rule:MF_01702}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01702}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01702}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Phosphate
CC       importer (TC 3.A.1.7) family. {ECO:0000255|HAMAP-Rule:MF_01702}.
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DR   EMBL; BX571965; CAH35360.1; -; Genomic_DNA.
DR   RefSeq; WP_004193614.1; NZ_CP009538.1.
DR   RefSeq; YP_107987.1; NC_006350.1.
DR   AlphaFoldDB; Q63V79; -.
DR   SMR; Q63V79; -.
DR   STRING; 272560.BPSL1362; -.
DR   EnsemblBacteria; CAH35360; CAH35360; BPSL1362.
DR   GeneID; 56595289; -.
DR   KEGG; bps:BPSL1362; -.
DR   PATRIC; fig|272560.51.peg.118; -.
DR   eggNOG; COG1117; Bacteria.
DR   OMA; TIDICRV; -.
DR   Proteomes; UP000000605; Chromosome 1.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015415; F:ATPase-coupled phosphate ion transmembrane transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd03260; ABC_PstB_phosphate_transporter; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR015850; ABC_transpr_PstB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005670; Phosp_transpt1.
DR   PANTHER; PTHR43423; PTHR43423; 1.
DR   PANTHER; PTHR43423:SF3; PTHR43423:SF3; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00972; 3a0107s01c2; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51238; PSTB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Phosphate transport; Reference proteome; Translocase;
KW   Transport.
FT   CHAIN           1..282
FT                   /note="Phosphate import ATP-binding protein PstB"
FT                   /id="PRO_0000092796"
FT   DOMAIN          36..277
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
FT   BINDING         68..75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
SQ   SEQUENCE   282 AA;  31429 MW;  205CA8168A734F0D CRC64;
     MNMAESHLDP SKLATGPAGF GAAAGQRPLA PLNAKIEVKN LNFFYNQFHA LKNINLSIPE
     GKVTAFIGPS GCGKSTLLRT FNKMYALYPE QRAEGEIVMD GENLLQSKLD ISLLRARIGM
     VFQKPTPFPM SIYDNIAFGV KMFERLTRSE MDDRVEWALT KAALWNEVKD KLSQSGYGLS
     GGQQQRLCIA RGIAIRPEVL LLDEPCSALD PISTGRIEEL IAELKSDYTV VIVTHNMQQA
     ARCSDYTAYM YLGELIEFGE TEKIFIKPAR KETEDYITGR FG
 
 
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