CYSA_MYCTU
ID CYSA_MYCTU Reviewed; 351 AA.
AC P9WQM1; L0TC79; P0A4W2; P71747;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-NOV-2014, sequence version 2.
DT 03-AUG-2022, entry version 50.
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=Rv2397c;
GN ORFNames=MTCY253.24;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP CHARACTERIZATION.
RX PubMed=11929522; DOI=10.1046/j.1365-2958.2002.02771.x;
RA Wooff E., Michell S.L.I., Gordon S.V., Chambers M.A., Bardarov S.,
RA Jacobs W.R. Jr., Hewinson R.G., Wheeler P.R.;
RT "Functional genomics reveals the sole sulphate transporter of the
RT Mycobacterium tuberculosis complex and its relevance to the acquisition of
RT sulphur in vivo.";
RL Mol. Microbiol. 43:653-663(2002).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 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; AL123456; CCP45187.1; -; Genomic_DNA.
DR PIR; H70682; H70682.
DR RefSeq; WP_003412325.1; NZ_NVQJ01000054.1.
DR RefSeq; YP_177879.1; NC_000962.3.
DR AlphaFoldDB; P9WQM1; -.
DR SMR; P9WQM1; -.
DR STRING; 83332.Rv2397c; -.
DR iPTMnet; P9WQM1; -.
DR PaxDb; P9WQM1; -.
DR DNASU; 885663; -.
DR GeneID; 45426385; -.
DR GeneID; 885663; -.
DR KEGG; mtu:Rv2397c; -.
DR TubercuList; Rv2397c; -.
DR eggNOG; COG1118; Bacteria.
DR PhylomeDB; P9WQM1; -.
DR Reactome; R-MTU-936635; Sulfate assimilation.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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 GO; GO:0008272; P:sulfate transport; IMP:MTBBASE.
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; IPR024765; TOBE-like.
DR Pfam; PF00005; ABC_tran; 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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Sulfate transport; Translocase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..351
FT /note="Sulfate/thiosulfate import ATP-binding protein CysA"
FT /id="PRO_0000092276"
FT DOMAIN 5..235
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01701"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01701"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
SQ SEQUENCE 351 AA; 37444 MW; 63A55D9DE26D1BEA CRC64;
MTYAIVVADA TKRYGDFVAL DHVDFVVPTG SLTALLGPSG SGKSTLLRTI AGLDQPDTGT
ITINGRDVTR VPPQRRGIGF VFQHYAAFKH LTVRDNVAFG LKIRKRPKAE IKAKVDNLLQ
VVGLSGFQSR YPNQLSGGQR QRMALARALA VDPEVLLLDE PFGALDAKVR EELRAWLRRL
HDEVHVTTVL VTHDQAEALD VADRIAVLHK GRIEQVGSPT DVYDAPANAF VMSFLGAVST
LNGSLVRPHD IRVGRTPNMA VAAADGTAGS TGVLRAVVDR VVVLGFEVRV ELTSAATGGA
FTAQITRGDA EALALREGDT VYVRATRVPP IAGGVSGVDD AGVERVKVTS T
