ID A0A3S3PWG3_XANMN Unreviewed; 276 AA. AC A0A3S3PWG3; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 11-DEC-2019, entry version 6. DE RecName: Full=Phosphate import ATP-binding protein PstB {ECO:0000256|HAMAP-Rule:MF_01702}; DE EC=7.3.2.1 {ECO:0000256|HAMAP-Rule:MF_01702}; DE AltName: Full=ABC phosphate transporter {ECO:0000256|HAMAP-Rule:MF_01702}; DE AltName: Full=Phosphate-transporting ATPase {ECO:0000256|HAMAP-Rule:MF_01702}; GN Name=pstB {ECO:0000256|HAMAP-Rule:MF_01702, GN ECO:0000313|EMBL:RWU18576.1}; GN ORFNames=XANMN_07955 {ECO:0000313|EMBL:RWU18576.1}; OS Xanthomonas axonopodis pv. manihotis str. CIO151. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=1185660 {ECO:0000313|EMBL:RWU18576.1, ECO:0000313|Proteomes:UP000284211}; RN [1] {ECO:0000313|EMBL:RWU18576.1, ECO:0000313|Proteomes:UP000284211} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIO151 {ECO:0000313|EMBL:RWU18576.1, RC ECO:0000313|Proteomes:UP000284211}; RX PubMed=24278159; DOI=10.1371/journal.pone.0079704; RA Arrieta-Ortiz M.L., Rodriguez-R L.M., Perez-Quintero A., Poulin L., RA Diaz A.C., Arias Rojas N., Trujillo C., Restrepo Benavides M., Bart R., RA Boch J., Boureau T., Darrasse A., David P., Duge de Bernonville T., RA Fontanilla P., Gagnevin L., Guerin F., Jacques M.A., Lauber E., RA Lefeuvre P., Medina C., Medina E., Montenegro N., Munoz Bodnar A., RA Noel L.D., Ortiz Quinones J.F., Osorio D., Pardo C., Patil P.B., RA Poussier S., Pruvost O., Robene-Soustrade I., Ryan R.P., Tabima J., RA Urrego Morales O.G., Verniere C., Carrere S., Verdier V., Szurek B., RA Restrepo S., Lopez C., Koebnik R., Bernal A.; RT "Genomic survey of pathogenicity determinants and VNTR markers in the RT cassava bacterial pathogen Xanthomonas axonopodis pv. Manihotis strain RT CIO151."; RL PLoS ONE 8:e79704-e79704(2013). CC -!- FUNCTION: Part of the ABC transporter complex PstSACB involved in CC phosphate import. Responsible for energy coupling to the transport CC system. {ECO:0000256|HAMAP-Rule:MF_01702, CC ECO:0000256|SAAS:SAAS00742467}. 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:0000256|HAMAP-Rule:MF_01702, CC ECO:0000256|SAAS:SAAS01120720}; 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:0000256|HAMAP-Rule:MF_01702, CC ECO:0000256|SAAS:SAAS00742506}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01702}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01702}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Phosphate CC importer (TC 3.A.1.7) family. {ECO:0000256|HAMAP-Rule:MF_01702, CC ECO:0000256|SAAS:SAAS00742482}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RWU18576.1}. 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; SAZB01000004; RWU18576.1; -; Genomic_DNA. DR RefSeq; WP_017155847.1; NZ_SAZB01000004.1. DR Proteomes; UP000284211; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015415; F:ATPase-coupled phosphate ion transmembrane transporter activity; IEA:UniProtKB-UniRule. DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro. DR CDD; cd03260; ABC_PstB_phosphate_transporter; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR015850; ABC_transpr_PstB. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005670; Phosp_transpt1. 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 {ECO:0000256|HAMAP-Rule:MF_01702, ECO:0000256|PROSITE- KW ProRule:PRU00434, ECO:0000256|SAAS:SAAS00767138, KW ECO:0000313|EMBL:RWU18576.1}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01702, KW ECO:0000256|SAAS:SAAS00742451}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01702, ECO:0000256|SAAS:SAAS00742434}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01702, ECO:0000256|PROSITE- KW ProRule:PRU00434, ECO:0000256|SAAS:SAAS00767115}; KW Phosphate transport {ECO:0000256|HAMAP-Rule:MF_01702, KW ECO:0000256|SAAS:SAAS00742454}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01702, KW ECO:0000256|SAAS:SAAS01104977}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01702, ECO:0000256|SAAS:SAAS00767203}. FT DOMAIN 30..271 FT /note="ABC transporter" FT /evidence="ECO:0000259|PROSITE:PS50893" FT DOMAIN 230..276 FT /note="PSTB" FT /evidence="ECO:0000259|PROSITE:PS51238" FT NP_BIND 62..69 FT /note="ATP" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00434" SQ SEQUENCE 276 AA; 31110 MW; E06BFD87D7B020A8 CRC64; MNDLHNAKPM HRIAVPAATG APTAQAPVKV AARNLDFYYD KYHALKSINI EIPEKRVTAL IGPSGCGKST LLRIFNRIYA LYPKMEARGE VLLDNENILS PKYPMNRLRS KVGMVFQKPV PFPMTIFENV AYGIRHHEKL SKADMQNRVE QALRQGALWD EVKDKLGQSA LGLSGGQQQR LCIARAVALR PDVLLLDEPT SALDPISTSR IEQLVEELKR DYTIVIVTHN MQQAARVSDY TAFMYLGDLI EHDRTETIFS QPSKQQTEDY ITGRFG //