(data stored in ACNUC7421 zone)

SWISSPROT: E6S995_INTC7

ID   E6S995_INTC7            Unreviewed;       336 AA.
AC   E6S995;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 58.
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=Intca_0526 {ECO:0000313|EMBL:ADU47071.1};
OS   Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 /
OS   NBRC 12989 / 7 KIP).
OC   Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU47071.1, ECO:0000313|Proteomes:UP000008914};
RN   [1] {ECO:0000313|EMBL:ADU47071.1, ECO:0000313|Proteomes:UP000008914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC   {ECO:0000313|Proteomes:UP000008914};
RX   PubMed=21304734; DOI=10.4056/sigs.1263355;
RA   Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S.,
RA   Cheng J.F., Detter C., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Pukall R., Sikorski J., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Intrasporangium calvum type strain (7
RT   KIP).";
RL   Stand. Genomic Sci. 3:294-303(2010).
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 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002343; ADU47071.1; -; Genomic_DNA.
DR   RefSeq; WP_013491392.1; NC_014830.1.
DR   STRING; 710696.Intca_0526; -.
DR   EnsemblBacteria; ADU47071; ADU47071; Intca_0526.
DR   KEGG; ica:Intca_0526; -.
DR   eggNOG; ENOG4108IJ6; Bacteria.
DR   eggNOG; COG1118; LUCA.
DR   KO; K02045; -.
DR   OrthoDB; 1220708at2; -.
DR   Proteomes; UP000008914; 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   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; IPR005116; Transp-assoc_OB_typ1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF03459; TOBE; 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; E6S995.
DR   SWISS-2DPAGE; E6S995.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01701, ECO:0000256|PROSITE-
KW   ProRule:PRU00434, ECO:0000256|SAAS:SAAS00237035};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01701,
KW   ECO:0000256|SAAS:SAAS01133279};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008914};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01701,
KW   ECO:0000256|SAAS:SAAS01133289};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01701,
KW   ECO:0000256|PROSITE-ProRule:PRU00434, ECO:0000256|SAAS:SAAS00452314};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008914};
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        2    232       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   DOMAIN      192    323       CYSA. {ECO:0000259|PROSITE:PS51237}.
FT   NP_BIND      34     41       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00434}.
SQ   SEQUENCE   336 AA;  36410 MW;  6B2B969AA104DB33 CRC64;
     MITVTGARKE FGSFTALDDV SLDIPSGSLT ALLGPSGSGK STLLRAIAGL ESLDSGVVSI
     GGRDVTGEPP QRRGIGFVFQ HYAAFKHLTV RDNVAFGLTI RKRPKTETDA KVNELLTVVG
     LEGFAHRYPA QLSGGQRQRM ALARALAVDP EVLLLDEPFG ALDAKVRTDL RTWLRRLHDE
     VHVTTVLVTH DQEEALDVAD RIAVLNHGRI EQVGDPVTLY DRPANDFVMS FLGSVSKLGE
     QLVRPHDIIL ERDHALALAA DAQVPGSPGV IRAVVERVVR LGFEVRVDLR ADSGERFAAQ
     ITRRDADGLD LRDGEPITAR AAHRSSVVDH DPALAI
//

If you have problems or comments...

PBIL Back to PBIL home page