CYSA_BACC1
ID CYSA_BACC1 Reviewed; 357 AA.
AC O31339;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Sulfate/thiosulfate import ATP-binding protein CysA {ECO:0000255|HAMAP-Rule:MF_01701};
DE EC=7.3.2.3 {ECO:0000255|HAMAP-Rule:MF_01701};
DE AltName: Full=Sulfate-transporting ATPase {ECO:0000255|HAMAP-Rule:MF_01701};
GN Name=cysA {ECO:0000255|HAMAP-Rule:MF_01701}; OrderedLocusNames=BCE_1199;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 125-357.
RX PubMed=10217496; DOI=10.1099/13500872-145-3-621;
RA Oekstad O.A., Hegna I.K., Lindbaeck T., Rishovd A.-L., Kolstoe A.-B.;
RT "Genome organization is not conserved between Bacillus cereus and Bacillus
RT subtilis.";
RL Microbiology 145:621-631(1999).
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:0000255|HAMAP-Rule:MF_01701}.
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:0000255|HAMAP-Rule:MF_01701};
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:0000255|HAMAP-Rule:MF_01701};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (CysA),
CC two transmembrane proteins (CysT and CysW) and a solute-binding protein
CC (CysP). {ECO:0000255|HAMAP-Rule:MF_01701}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01701};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01701}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC Sulfate/tungstate importer (TC 3.A.1.6) family. {ECO:0000255|HAMAP-
CC Rule:MF_01701}.
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DR EMBL; AE017194; AAS40129.1; -; Genomic_DNA.
DR EMBL; Y10908; CAA71848.1; -; Genomic_DNA.
DR RefSeq; WP_000027090.1; NC_003909.8.
DR AlphaFoldDB; O31339; -.
DR SMR; O31339; -.
DR EnsemblBacteria; AAS40129; AAS40129; BCE_1199.
DR GeneID; 59157220; -.
DR KEGG; bca:BCE_1199; -.
DR HOGENOM; CLU_000604_1_1_9; -.
DR OMA; HLGWEIQ; -.
DR Proteomes; UP000002527; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0015419; F:ABC-type sulfate transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0102025; F:ABC-type thiosulfate transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd03296; ABC_CysA_sulfate_importer; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR041193; CysA_C.
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; PF17850; CysA_C_terminal; 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;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Sulfate transport; Translocase; Transport.
FT CHAIN 1..357
FT /note="Sulfate/thiosulfate import ATP-binding protein CysA"
FT /id="PRO_0000092250"
FT DOMAIN 3..237
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01701"
FT BINDING 35..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01701"
SQ SEQUENCE 357 AA; 40048 MW; 8418862117A23D8A CRC64;
MSIQIQGVSK QYGTFQALTD IHLDIPKGEL VALLGPSGSG KTTLLRIIAG LEEADEGSIS
FEGEDLTDIH VKNRQVGFVF QHYALFKHMN VFENVAFGLK VRKKSLRPSA EAIEEKVTEL
LKLVKMDGFA KRYPAQLSGG QRQRIALARA LAVEPKILLL DEPFGALDAK VRKELRRWLR
KLHDEFQITS VFVTHDQEEA LDVADRIVVM NEGRIEQMGT PEEVYENPAS PFVYDFLGNV
NLFHGRVHKG KLNVGSVELE APEHKHISNV DGVAYVRPHH LSISRTKQSV DAIPAKVSYS
HAVGPVVYVE LKRDGTDEYL EAEISKEQFR QLSIQAGDVV YVQPKEVKVF IPEDFVI
