PSTB_CAUVN
ID PSTB_CAUVN Reviewed; 274 AA.
AC B8GYG4; Q9ABD6; Q9RFA8;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 2.
DT 03-AUG-2022, entry version 82.
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}; OrderedLocusNames=CCNA_00294;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-274, AND CHARACTERIZATION.
RX PubMed=10629178; DOI=10.1128/jb.182.2.337-347.2000;
RA Gonin M., Quardokus E.M., O'Donnol D., Maddock J.R., Brun Y.V.;
RT "Regulation of stalk elongation by phosphate in Caulobacter crescentus.";
RL J. Bacteriol. 182:337-347(2000).
CC -!- FUNCTION: Part of the ABC transporter complex PstSACB involved in
CC phosphate import. Responsible for energy coupling to the transport
CC system.
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}.
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; CP001340; ACL93761.2; -; Genomic_DNA.
DR EMBL; AF196490; AAF15531.1; -; Genomic_DNA.
DR RefSeq; WP_010918181.1; NC_011916.1.
DR RefSeq; YP_002515669.2; NC_011916.1.
DR AlphaFoldDB; B8GYG4; -.
DR SMR; B8GYG4; -.
DR PRIDE; B8GYG4; -.
DR EnsemblBacteria; ACL93761; ACL93761; CCNA_00294.
DR GeneID; 7330747; -.
DR KEGG; ccs:CCNA_00294; -.
DR PATRIC; fig|565050.3.peg.291; -.
DR HOGENOM; CLU_000604_1_22_5; -.
DR OrthoDB; 1416748at2; -.
DR Proteomes; UP000001364; Chromosome.
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 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Phosphate transport; Reference proteome; Translocase;
KW Transport.
FT CHAIN 1..274
FT /note="Phosphate import ATP-binding protein PstB"
FT /id="PRO_0000378277"
FT DOMAIN 27..269
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
FT CONFLICT 125
FT /note="E -> D (in Ref. 2; AAF15531)"
FT /evidence="ECO:0000305"
FT CONFLICT 209..210
FT /note="IE -> MD (in Ref. 2; AAF15531)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 274 AA; 29510 MW; F5405E39AFE5BB12 CRC64;
MTVQSPDDST RAPATSTAAP ATADPKIKAR GVKVFYGDKQ ALFDVDLDIP AKSVTAFIGP
SGCGKSTFLR CINRMNDTIP SARVEGSILI DGADVNAKSV DPVVLRSRVG MVFQKPNPFP
KTIFENVAYG PRIHGLATGK AELEAIVESS LKKAGLWNEV ADRLHQPGTG LSGGQQQRLV
IARAIAVSPE VILMDEPCSA LDPIATAKIE ELIDELRSQF CIVIVTHSMA QAARVSQRTA
FFHLGKLVES GPTEEMFTNP RDSRTQDYIT GRFG
