(data stored in SCRATCH zone)

SWISSPROT: Q500L7_PSEU2

ID   Q500L7_PSEU2            Unreviewed;       326 AA.
AC   Q500L7;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 117.
DE   RecName: Full=Sulfate/thiosulfate import ATP-binding protein CysA {ECO:0000256|HAMAP-Rule:MF_01701};
DE            EC=7.3.2.3 {ECO:0000256|HAMAP-Rule:MF_01701};
DE   AltName: Full=Sulfate-transporting ATPase {ECO:0000256|HAMAP-Rule:MF_01701};
GN   Name=cysA {ECO:0000256|HAMAP-Rule:MF_01701};
GN   OrderedLocusNames=Psyr_0081 {ECO:0000313|EMBL:AAY35155.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35155.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35155.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35155.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- FUNCTION: Part of the ABC transporter complex CysAWTP involved in
CC       sulfate/thiosulfate import. Responsible for energy coupling to the
CC       transport system. {ECO:0000256|HAMAP-Rule:MF_01701,
CC       ECO:0000256|SAAS:SAAS00360330}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + sulfate(out) = ADP + H(+) + phosphate +
CC         sulfate(in); Xref=Rhea:RHEA:10192, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.3;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01701,
CC         ECO:0000256|SAAS:SAAS01131877};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + thiosulfate(out) = ADP + H(+) + phosphate +
CC         thiosulfate(in); Xref=Rhea:RHEA:29871, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33542,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.3;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01701,
CC         ECO:0000256|SAAS:SAAS01131887};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins
CC       (CysA), two transmembrane proteins (CysT and CysW) and a solute-
CC       binding protein (CysP). {ECO:0000256|HAMAP-Rule:MF_01701,
CC       ECO:0000256|SAAS:SAAS00360324}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01701}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01701}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC       Sulfate/tungstate importer (TC 3.A.1.6) family.
CC       {ECO:0000256|HAMAP-Rule:MF_01701, ECO:0000256|SAAS:SAAS00552311}.
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DR   EMBL; CP000075; AAY35155.1; -; Genomic_DNA.
DR   RefSeq; WP_011266173.1; NC_007005.1.
DR   RefSeq; YP_233193.1; NC_007005.1.
DR   STRING; 205918.Psyr_0081; -.
DR   EnsemblBacteria; AAY35155; AAY35155; Psyr_0081.
DR   GeneID; 3365556; -.
DR   KEGG; psb:Psyr_0081; -.
DR   PATRIC; fig|205918.7.peg.80; -.
DR   eggNOG; ENOG4108IJ6; Bacteria.
DR   eggNOG; COG1118; LUCA.
DR   KO; K02045; -.
DR   OMA; MEVRVQN; -.
DR   BioCyc; PSYR205918:G1G4J-81-MONOMER; -.
DR   Proteomes; UP000000426; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0015419; F:ATPase-coupled sulfate transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   CDD; cd03296; ABC_CysA_sulfate_importer; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR014769; ABC_CysA_ATP-bd_C.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005666; Sulph_transpt1.
DR   InterPro; IPR024765; TOBE-like.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF12857; TOBE_3; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50331; SSF50331; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00968; 3a0106s01; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51237; CYSA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q500L7.
DR   SWISS-2DPAGE; Q500L7.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01701, ECO:0000256|PROSITE-
KW   ProRule:PRU00434, ECO:0000256|SAAS:SAAS00237035};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01701};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01701,
KW   ECO:0000256|SAAS:SAAS00437629};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01701,
KW   ECO:0000256|SAAS:SAAS00437643};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01701,
KW   ECO:0000256|PROSITE-ProRule:PRU00434, ECO:0000256|SAAS:SAAS00452314};
KW   Sulfate transport {ECO:0000256|HAMAP-Rule:MF_01701,
KW   ECO:0000256|SAAS:SAAS00437635};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_01701,
KW   ECO:0000256|SAAS:SAAS01131881};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01701,
KW   ECO:0000256|SAAS:SAAS00237071}.
FT   DOMAIN        3    237       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   DOMAIN      197    322       CYSA. {ECO:0000259|PROSITE:PS51237}.
FT   NP_BIND      35     42       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00434}.
SQ   SEQUENCE   326 AA;  36766 MW;  DB50097550038653 CRC64;
     MSIEVRNVSK NFNAFKALNN ISLDIQSGEL VALLGPSGCG KTTLLRIIAG LETPDDGSIV
     FHGEDVSGHD VRDRNVGFVF QHYALFRHMT VFDNVAFGLR MKPKRERPNE TRIAEKVHEL
     LNMVQLDWLA DRYPEQLSGG QRQRIALARA LAVEPKVLLL DEPFGALDAK VRKELRRWLA
     RLHEDINLTS VFVTHDQEEA MEVADRIVVM NKGVIEQIGS PGEVYENPSN DFVYHFLGDS
     NRLSLGAEGH LLFRPHEVSL SRQEIEDHHA AEVRDIRPLG ATTRVTLKVE GQDELIEAEV
     VKDHDSLVGL AKGETLFFKP KVWQKL
//

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