CYSA_ANTAG
ID CYSA_ANTAG Reviewed; 381 AA.
AC Q85A69;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 84.
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};
OS Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC Anthoceros.
OX NCBI_TaxID=48387;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX PubMed=12527781; DOI=10.1093/nar/gkg155;
RA Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT chloroplast genome: insight into the earliest land plants.";
RL Nucleic Acids Res. 31:716-721(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC TISSUE=Thallus;
RX PubMed=12711687; DOI=10.1093/nar/gkg327;
RA Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT "RNA editing in hornwort chloroplasts makes more than half the genes
RT functional.";
RL Nucleic Acids Res. 31:2417-2423(2003).
CC -!- FUNCTION: Part of the ABC transporter complex 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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- RNA EDITING: Modified_positions=1 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 4 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 18 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 33 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 34 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 72 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 80 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 86 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 95 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 121 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 123 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 154 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 155 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 156 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 163 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 169 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 193 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 196 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 233 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 295 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 346 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}; Note=The initiator methionine is created
CC by RNA editing. The nonsense codons at positions 72, 121, 169, 193 and
CC 346 are modified to sense codons.;
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 ---------------------------------------------------------------------------
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; AB086179; BAC55343.1; -; Genomic_DNA.
DR EMBL; AB087436; BAC55436.1; -; mRNA.
DR RefSeq; NP_777407.1; NC_004543.1.
DR AlphaFoldDB; Q85A69; -.
DR SMR; Q85A69; -.
DR PRIDE; Q85A69; -.
DR GeneID; 2553491; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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 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; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 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; Chloroplast; Nucleotide-binding; Plastid; RNA editing;
KW Sulfate transport; Translocase; Transport.
FT CHAIN 1..381
FT /note="Sulfate/thiosulfate import ATP-binding protein CysA"
FT /id="PRO_0000092306"
FT DOMAIN 3..233
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 381 AA; 43655 MW; E140215B6FF1BA0A CRC64;
MSILVYEVSK SLGNLKVLDR VSLYVRKVSL VALLGPSGSG KSSLLRIIAG LDSPDYGSVW
LHGTDMTNTS TQYRHMAFVF QHYALFKNMT VYENISFGLR LRGFSYQKIR NKVNDLLDCL
RISDIVSEYP GKLSGGQKQR VALARSLAIK SDFLLLDEPF GALDGELRRH LSKWLKRYLK
DNGITTIMVT HDQKEAISMA DEIVVLKQGR FLQQGRSKNL YDEPIDYFVG IFSGSFIEFP
QLEESLDAPL GSSSSSSSST KKSMEKDFTP FIPDLIWSQI FTNQSIHHYH FFLRPHELYL
ESQIDLKAIP VQIKKIIYKR TFVQLDLSIT PSSWNITIPI GYQAFRKLNI QSFVQKLYIK
PRNQVYLRAY PKKKNIISKQ I