ID Q3EX50_BACTI Unreviewed; 290 AA. AC Q3EX50; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 01-OCT-2014, entry version 56. DE RecName: Full=Phosphate import ATP-binding protein PstB {ECO:0000256|HAMAP-Rule:MF_01702}; DE EC=3.6.3.27 {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 ORFNames=RBTH_05093 {ECO:0000313|EMBL:EAO55895.1}; OS Bacillus thuringiensis serovar israelensis ATCC 35646. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=339854 {ECO:0000313|EMBL:EAO55895.1}; RN [1] {ECO:0000313|EMBL:EAO55895.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 35646 {ECO:0000313|EMBL:EAO55895.1}; RA Anderson I., Sorokin A., Kapatral V., Reznik G., Bhattacharya A., RA Mikhailova N., Burd H., Joukov V., Kaznadzey D., Walunas T., RA D'Souza M., Larsen N., Pusch G., Liolios K., Grechkin Y., Lapidus A., RA Goltsman E., Chu L., Fonstein M., Ehrlich D., Overbeek R., RA Kyrpides N., Ivanova N.; RT "Comparative genome analysis of Bacillus cereus group genomes with RT Bacillus subtilis."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. 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:SAAS00042467}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + phosphate(Out) = ADP + phosphate CC + phosphate(In). {ECO:0000256|HAMAP-Rule:MF_01702, CC ECO:0000256|SAAS:SAAS00042511}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (PstB), two transmembrane proteins (PstC and PstA) and a solute- CC binding protein (PstS). {ECO:0000256|HAMAP-Rule:MF_01702, CC ECO:0000256|SAAS:SAAS00042475}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_01702}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01702}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|RuleBase:RU000684}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Phosphate CC importer (TC 3.A.1.7) family. {ECO:0000256|HAMAP-Rule:MF_01702}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000256|HAMAP- CC Rule:MF_01702}. CC -!- SIMILARITY: Contains ABC transporter domain. CC {ECO:0000256|SAAS:SAAS00042493}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EAO55895.1}. 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; AAJM01000047; EAO55895.1; -; Genomic_DNA. DR ProteinModelPortal; Q3EX50; -. DR EnsemblBacteria; EAO55895; EAO55895; RBTH_05093. DR PATRIC; 38346833; VBIBacThu7829_1728. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0015415; F:phosphate ion transmembrane-transporting ATPase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 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, KW ECO:0000256|RuleBase:RU000684, ECO:0000256|SAAS:SAAS00042476, KW ECO:0000313|EMBL:EAO55895.1}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01702, KW ECO:0000256|SAAS:SAAS00042474}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01702, KW ECO:0000256|SAAS:SAAS00042361}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01702, KW ECO:0000256|SAAS:SAAS00042480}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01702, KW ECO:0000256|RuleBase:RU000684, ECO:0000256|SAAS:SAAS00042403}; KW Phosphate transport {ECO:0000256|HAMAP-Rule:MF_01702, KW ECO:0000256|SAAS:SAAS00042543}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01702, KW ECO:0000256|SAAS:SAAS00042439}. FT DOMAIN 44 285 ABC transporter. {ECO:0000256|HAMAP-Rule: FT MF_01702}. FT NP_BIND 76 83 ATP. {ECO:0000256|HAMAP-Rule:MF_01702}. SQ SEQUENCE 290 AA; 33002 MW; 79AEEFF32E9B1649 CRC64; MFYGYEIENK LEVDERGIQM VATVVNVQVK NEEKIETAPK KVVFDTKNLN LWYGEDHALK DINLSIHENE VTAIIGPSGC GKSTYLKTLN RMVELVPIVR TTGVIEYRER NIFDKSYPVE ELRTHVGMVF QKPNPFPKSI YENVAYGPKI HGIRDKKTLD EIVEKSLRGA AIWDELKDRL HDNAYGLSGG QQQRLCIARC LAIEPDVILM DEPTSALDPI STLKVEELIQ ELKKDFSIVI VTHNMQQAAR ISDKTAFFLS GEVVEYTDTN KLFTTPSDKR TEDYITGRFG //