(data stored in ACNUC7421 zone)

SWISSPROT: C7PX49_CATAD

ID   C7PX49_CATAD            Unreviewed;       282 AA.
AC   C7PX49;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 66.
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   OrderedLocusNames=Caci_0448 {ECO:0000313|EMBL:ACU69400.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69400.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69400.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(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: ATP + H(2)O + phosphate(Out) = ADP + phosphate
CC       + phosphate(In). {ECO:0000256|HAMAP-Rule:MF_01702,
CC       ECO:0000256|SAAS:SAAS00742471}.
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 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; CP001700; ACU69400.1; -; Genomic_DNA.
DR   STRING; 479433.Caci_0448; -.
DR   EnsemblBacteria; ACU69400; ACU69400; Caci_0448.
DR   KEGG; cai:Caci_0448; -.
DR   eggNOG; ENOG4105BZY; Bacteria.
DR   eggNOG; COG1117; LUCA.
DR   KO; K02036; -.
DR   OMA; AFMYMGD; -.
DR   OrthoDB; POG091H01HF; -.
DR   Proteomes; UP000000851; 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-HAMAP.
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; C7PX49.
DR   SWISS-2DPAGE; C7PX49.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01702, ECO:0000256|PROSITE-
KW   ProRule:PRU00434, ECO:0000256|SAAS:SAAS00767138};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01702,
KW   ECO:0000256|SAAS:SAAS00742451};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01702,
KW   ECO:0000256|SAAS:SAAS00742455};
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:UP000000851};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01702,
KW   ECO:0000256|SAAS:SAAS00767203}.
FT   DOMAIN       29    277       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   DOMAIN      231    282       PSTB. {ECO:0000259|PROSITE:PS51238}.
FT   NP_BIND      61     68       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00434}.
SQ   SEQUENCE   282 AA;  30390 MW;  095313A1EA3EAAF9 CRC64;
     MTDSDLSHAG AVAVDDRPDA AGPHLPGTLE ARAVSAWFGD RKVLDRVSLT MPGGQVTALI
     GPSGCGKSTF LRILNRMHEL VASAALAGEV LLDGGDIYDP RVRLTEARAR IGMVFQKPNP
     FPGMSIYDNV TAGLKLTGTR RSRSEQDDIV ESCLTRAGLW NEVSDRLKQP GGALSGGQQQ
     RLCIARSLAV RPEVLLMDEP CSALDPTSTN RIEETIRELA SDVTIVIVTH NMQQASRVSD
     RCAFFLASAG TPGRIVEHGQ TRAMFSSPQD QRTSDYVNGR FG
//

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