(data stored in SCRATCH zone)

SWISSPROT: PSTB1_BACSU

ID   PSTB1_BACSU             Reviewed;         260 AA.
AC   P46342;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   11-DEC-2019, entry version 137.
DE   RecName: Full=Phosphate import ATP-binding protein PstB 1 {ECO:0000255|HAMAP-Rule:MF_01702};
DE            EC=7.3.2.1 {ECO:0000255|HAMAP-Rule:MF_01702};
DE   AltName: Full=ABC phosphate transporter 1 {ECO:0000255|HAMAP-Rule:MF_01702};
DE   AltName: Full=Phosphate-transporting ATPase 1 {ECO:0000255|HAMAP-Rule:MF_01702};
GN   Name=pstB1 {ECO:0000255|HAMAP-Rule:MF_01702}; Synonyms=pstBB, yqgK, yzmF;
GN   OrderedLocusNames=BSU24950;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8760913; DOI=10.1099/13500872-142-8-2017;
RA   Takemaru K., Mizuno M., Kobayashi Y.;
RT   "A Bacillus subtilis gene cluster similar to the Escherichia coli
RT   phosphate-specific transport (pst) operon: evidence for a tandemly arranged
RT   pstB gene.";
RL   Microbiology 142:2017-2020(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01702};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-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}.
DR   EMBL; D58414; BAA09585.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12514.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14425.1; -; Genomic_DNA.
DR   PIR; E69956; E69956.
DR   RefSeq; NP_390374.1; NC_000964.3.
DR   RefSeq; WP_004399074.1; NZ_JNCM01000036.1.
DR   SMR; P46342; -.
DR   STRING; 224308.BSU24950; -.
DR   PaxDb; P46342; -.
DR   PRIDE; P46342; -.
DR   EnsemblBacteria; CAB14425; CAB14425; BSU24950.
DR   GeneID; 938205; -.
DR   KEGG; bsu:BSU24950; -.
DR   PATRIC; fig|224308.179.peg.2714; -.
DR   eggNOG; ENOG4105BZY; Bacteria.
DR   eggNOG; COG1117; LUCA.
DR   InParanoid; P46342; -.
DR   KO; K02036; -.
DR   OMA; IEDISMT; -.
DR   PhylomeDB; P46342; -.
DR   BioCyc; BSUB:BSU24950-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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;
DR   PRODOM; P46342.
DR   SWISS-2DPAGE; P46342.
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Phosphate transport; Reference proteome; Translocase; Transport.
FT   CHAIN           1..260
FT                   /note="Phosphate import ATP-binding protein PstB 1"
FT                   /id="PRO_0000092780"
FT   DOMAIN          8..255
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
FT   NP_BIND         46..53
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
SQ   SEQUENCE   260 AA;  29199 MW;  F90323CE2E015BC9 CRC64;
     MSIATEAVMK QEVYQVNGMN LWYGQHHALK NINLSIYENE VTAIIGPSGC GKSTFIKTLN
     LMIQMTPNVK LAGELNYNGS NILKDKVDIV DLRKNIGMVF QKGNPFPQSI FDNVAYGPRV
     HGTKNKKKLQ EIVEKSLKDV ALWDEVKDRL HTSALSLSGG QQQRLCIARA LATNPDILLM
     DEPTSALDPI STRKIEELIL ELKDKYTIVI VTHNMQQAAR VSDQTAFFYM GELVECDNTN
     KMFSNPKDQR TLDYISGKFG
//

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