ID Q3EX50_BACTI Unreviewed; 290 AA. AC Q3EX50; DT 08-NOV-2005, integrated into UniProtKB/TrEMBL. DT 08-NOV-2005, sequence version 1. DT 07-APR-2021, entry version 91. 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 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, ECO:0000313|Proteomes:UP000005383}; RN [1] {ECO:0000313|EMBL:EAO55895.1, ECO:0000313|Proteomes:UP000005383} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC35646 {ECO:0000313|Proteomes:UP000005383}; RA Anderson I., Sorokin A., Kapatral V., Reznik G., Bhattacharya A., RA Mikhailova N., Burd H., Joukov V., Kaznadzey D., Walunas T., D'Souza M., RA Larsen N., Pusch G., Liolios K., Grechkin Y., Lapidus A., Goltsman E., RA Chu L., Fonstein M., Ehrlich D., Overbeek R., Kyrpides N., Ivanova N.; RT "Comparative genome analysis of Bacillus cereus group genomes with Bacillus RT 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 -!- 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 -!- 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 -!- 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 -!- 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: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 PATRIC; fig|339854.8.peg.5474; -. DR Proteomes; UP000005383; 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 PANTHER; PTHR43423; PTHR43423; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01702, ECO:0000256|PROSITE-ProRule:PRU00434, KW ECO:0000313|EMBL:EAO55895.1}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_01702}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01702}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01702, ECO:0000256|PROSITE-ProRule:PRU00434}; KW Phosphate transport {ECO:0000256|ARBA:ARBA00022592, ECO:0000256|HAMAP- KW Rule:MF_01702}; Translocase {ECO:0000256|HAMAP-Rule:MF_01702}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01702}. FT DOMAIN 44..285 FT /note="ABC transporter" FT /evidence="ECO:0000259|PROSITE:PS50893" FT DOMAIN 244..290 FT /note="PSTB" FT /evidence="ECO:0000259|PROSITE:PS51238" FT NP_BIND 76..83 FT /note="ATP" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00434" 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 //