PSTB2_MAGSA
ID PSTB2_MAGSA Reviewed; 259 AA.
AC Q2W7J9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Phosphate import ATP-binding protein PstB 2 {ECO:0000255|HAMAP-Rule:MF_01702};
DE EC=7.3.2.1 {ECO:0000255|HAMAP-Rule:MF_01702};
DE AltName: Full=ABC phosphate transporter 2 {ECO:0000255|HAMAP-Rule:MF_01702};
DE AltName: Full=Phosphate-transporting ATPase 2 {ECO:0000255|HAMAP-Rule:MF_01702};
GN Name=pstB2 {ECO:0000255|HAMAP-Rule:MF_01702}; OrderedLocusNames=amb1372;
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=342108;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
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; AP007255; BAE50176.1; -; Genomic_DNA.
DR RefSeq; WP_011383782.1; NC_007626.1.
DR AlphaFoldDB; Q2W7J9; -.
DR SMR; Q2W7J9; -.
DR STRING; 342108.amb1372; -.
DR EnsemblBacteria; BAE50176; BAE50176; amb1372.
DR KEGG; mag:amb1372; -.
DR HOGENOM; CLU_000604_1_22_5; -.
DR OMA; TIDICRV; -.
DR OrthoDB; 1416748at2; -.
DR Proteomes; UP000007058; 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 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..259
FT /note="Phosphate import ATP-binding protein PstB 2"
FT /id="PRO_0000272473"
FT DOMAIN 12..254
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
SQ SEQUENCE 259 AA; 28158 MW; C458DA9CFD91A376 CRC64;
MNQFIPRGTS KISARGLNVH YGEKQALHDI DLDIPAGEVT ALIGPSGCGK STFLRCINRM
NDMVDGAKVT GSLTLDGSDV YDRSLDVVQL RARVGMVFQK PNPFPKSIYD NVAYGPRIHG
LARDQAELDE IVMNSLEKAG LLAEVESRLS ESGTGLSGGQ QQRLCIARAI AVAPEVILMD
EPCSALDPIA TAKVEELIDE LRDNYTIVIV THSMQQAARV SQRTAFFHLG KLIEVGGTEE
IFTNPKEPLT QGYITGRFG