CYSA_SYNE7
ID CYSA_SYNE7 Reviewed; 344 AA.
AC P14788; Q31MK9;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
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};
GN OrderedLocusNames=Synpcc7942_1680;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2538823; DOI=10.1073/pnas.86.6.1949;
RA Green L.S., Laudenbach D.E., Grossman A.R.;
RT "A region of a cyanobacterial genome required for sulfate transport.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1949-1953(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RX PubMed=1708375; DOI=10.1128/jb.173.9.2739-2750.1991;
RA Laudenbach D.E., Grossman A.R.;
RT "Characterization and mutagenesis of sulfur-regulated genes in a
RT cyanobacterium: evidence for function in sulfate transport.";
RL J. Bacteriol. 173:2739-2750(1991).
CC -!- FUNCTION: Part of the ABC transporter complex CysAWTP involved in
CC sulfate/thiosulfate import. Responsible for energy coupling to the
CC transport system.
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; Peripheral membrane protein.
CC -!- INDUCTION: By sulfur deprivation.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB57710.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J04512; AAA22056.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57710.1; ALT_INIT; Genomic_DNA.
DR EMBL; M65247; AAA73042.2; -; Genomic_DNA.
DR PIR; A30301; GRYCS7.
DR AlphaFoldDB; P14788; -.
DR SMR; P14788; -.
DR STRING; 1140.Synpcc7942_1680; -.
DR PRIDE; P14788; -.
DR EnsemblBacteria; ABB57710; ABB57710; Synpcc7942_1680.
DR KEGG; syf:Synpcc7942_1680; -.
DR eggNOG; COG1118; Bacteria.
DR HOGENOM; CLU_000604_1_1_3; -.
DR BioCyc; SYNEL:SYNPCC7942_1680-MON; -.
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 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 2: Evidence at transcript level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Stress response; Sulfate transport; Translocase;
KW Transport.
FT CHAIN 1..344
FT /note="Sulfate/thiosulfate import ATP-binding protein CysA"
FT /id="PRO_0000092296"
FT DOMAIN 9..239
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01701"
FT BINDING 41..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01701"
SQ SEQUENCE 344 AA; 38476 MW; 1A77A81AD0ABAA55 CRC64;
MPKDKAVGIQ VSQVSKQFGS FQAVKDVDLT VETGSLVALL GPSGSGKSTL LRLIAGLEQP
DSGRIFLTGR DATNESVRDR QIGFVFQHYA LFKHLTVRKN IAFGLELRKH TKEKVRARVE
ELLELVQLTG LGDRYPSQLS GGQRQRVALA RALAVQPQVL LLDEPFGALD AKVRKDLRSW
LRKLHDEVHV TTVFVTHDQE EAMEVADQIV VMNHGKVEQI GSPAEIYDNP ATPFVMSFIG
PVNVLPNSSH IFQAGGLDTP HPEVFLRPHD IEIAIDPIPE TVPARIDRIV HLGWEVQAEV
RLEDGQVLVA HLPRDRYRDL QLEPEQQVFV RPKQARSFPL NYSI
