(data stored in SCRATCH zone)

SWISSPROT: C3MFB2_SINFN

ID   C3MFB2_SINFN            Unreviewed;       271 AA.
AC   C3MFB2;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   08-MAY-2019, entry version 76.
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   OrderedLocusNames=NGR_c01470 {ECO:0000313|EMBL:ACP23949.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23949.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23949.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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
CC         phosphate(in); Xref=Rhea:RHEA:24440, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.3.2.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01702, ECO:0000256|SAAS:SAAS01120720};
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:SAAS00742506}.
CC   -!- SUBCELLULAR LOCATION: Cell inner 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. Phosphate
CC       importer (TC 3.A.1.7) family. {ECO:0000256|HAMAP-Rule:MF_01702,
CC       ECO:0000256|SAAS:SAAS00742482}.
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DR   EMBL; CP001389; ACP23949.1; -; Genomic_DNA.
DR   RefSeq; WP_012706734.1; NC_012587.1.
DR   RefSeq; YP_002824702.1; NC_012587.1.
DR   STRING; 394.NGR_c01470; -.
DR   EnsemblBacteria; ACP23949; ACP23949; NGR_c01470.
DR   GeneID; 32139538; -.
DR   GeneID; 7790726; -.
DR   KEGG; rhi:NGR_c01470; -.
DR   PATRIC; fig|394.7.peg.2941; -.
DR   eggNOG; ENOG4105BZY; Bacteria.
DR   eggNOG; COG1117; LUCA.
DR   KO; K02036; -.
DR   OMA; IEDISMT; -.
DR   OrthoDB; 1416748at2; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; C3MFB2.
DR   SWISS-2DPAGE; C3MFB2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01702, ECO:0000256|PROSITE-
KW   ProRule:PRU00434, ECO:0000256|SAAS:SAAS00767138,
KW   ECO:0000313|EMBL:ACP23949.1};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01702};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01702,
KW   ECO:0000256|SAAS:SAAS00742451};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01702,
KW   ECO:0000256|SAAS:SAAS00742434};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01702,
KW   ECO:0000256|PROSITE-ProRule:PRU00434, ECO:0000256|SAAS:SAAS00767115};
KW   Phosphate transport {ECO:0000256|HAMAP-Rule:MF_01702,
KW   ECO:0000256|SAAS:SAAS00742454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_01702,
KW   ECO:0000256|SAAS:SAAS01104977};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01702,
KW   ECO:0000256|SAAS:SAAS00767203}.
FT   DOMAIN       24    266       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   DOMAIN      225    271       PSTB. {ECO:0000259|PROSITE:PS51238}.
FT   NP_BIND      56     63       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00434}.
SQ   SEQUENCE   271 AA;  30311 MW;  9C9F4EFC9C697FF1 CRC64;
     MNIMSEAAVE KALDQKMNTV PLKMIGKDVS VYYGEKRALF DVNLNIRENT VTALIGPSGC
     GKSTFLRTLN RMNDTIENCR VTGRITLDED DIYDPSIDVV ELRARVGMVF QKPNPFPKSI
     YENVSYGPRI HGLARTKADF DEIVETSLQK AGLWNEVKDR LQEPGTGLSG GQQQRLCIAR
     AVAVSPEVIL MDEPCSALDP IATAKVEELI HELRANFTIV IVTHSMQQAA RVSQRTAMFH
     LGNLVEENDT DKMFTNPDDQ RTQDYIMGRF G
//

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