CYSA_SHIFL
ID CYSA_SHIFL Reviewed; 365 AA.
AC Q7UC29;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 134.
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};
GN OrderedLocusNames=SF2476.1, S2623;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01701}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC 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; AE005674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE014073; AAP17796.1; -; Genomic_DNA.
DR RefSeq; WP_000021053.1; NZ_WPGW01000057.1.
DR AlphaFoldDB; Q7UC29; -.
DR SMR; Q7UC29; -.
DR EnsemblBacteria; AAP17796; AAP17796; S2623.
DR KEGG; sft:NCTC1_02723; -.
DR KEGG; sfx:S2623; -.
DR PATRIC; fig|623.156.peg.4354; -.
DR HOGENOM; CLU_000604_1_1_6; -.
DR OMA; HLGWEIQ; -.
DR OrthoDB; 1220708at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005666; Sulph_transpt1.
DR Pfam; PF00005; ABC_tran; 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 inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Sulfate transport; Translocase;
KW Transport.
FT CHAIN 1..365
FT /note="Sulfate/thiosulfate import ATP-binding protein CysA"
FT /id="PRO_0000092294"
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 365 AA; 41069 MW; 082048EA8ED61AA8 CRC64;
MSIEIANIKK SFGRTQVLND ISLDIPSGQM VALLGPSGSG KTTLLRIIAG LEHQTSGHIR
FHGTDVSRLH ARDRKVGFVF QHYALFRHMT VFDNITFGLT VLPRRERPNA AAIKAKVTKL
LEMVQLAHLA DRYPAQLSGG QKQRVALARA LAVEPQILLL DEPFGALDAQ VRKELRRWLR
QLHEELKFTS VFVTHDQEEA TEVADRVVVM SQGNIEQADA PNQVWREPAT RFVLEFMGEV
NRLQGTIRGG QFHVGAHRWP LGYTPAYQGP VDLFLRPWEV DISRRTSLDS PLPVQVLEAS
PKGHYTQLVV QPLGWYNEPL TVVMHGDDAP QHGERLFVGL QHARLYNGDE RIETRDEELA
LAQSA
