ID   CTPA_MYCTO              Reviewed;         761 AA.
AC   P9WPU0; L0T5H9; Q10876;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Copper-exporting P-type ATPase {ECO:0000250|UniProtKB:P9WPU1};
DE            EC=7.2.2.8 {ECO:0000250|UniProtKB:P9WPU1};
DE   AltName: Full=Copper-exporting P-type ATPase A;
GN   Name=ctpA; OrderedLocusNames=MT0101;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Involved in copper export. Could be involved in the copper
CC       detoxification of mycobacterial cells. {ECO:0000250|UniProtKB:P9WPU1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC         ChEBI:CHEBI:456216; EC=7.2.2.8;
CC         Evidence={ECO:0000250|UniProtKB:P9WPU1};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P9WPU1};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000305}.
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DR   EMBL; AE000516; AAK44324.1; -; Genomic_DNA.
DR   PIR; D70750; D70750.
DR   RefSeq; WP_003899808.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPU0; -.
DR   SMR; P9WPU0; -.
DR   EnsemblBacteria; AAK44324; AAK44324; MT0101.
DR   KEGG; mtc:MT0101; -.
DR   PATRIC; fig|83331.31.peg.106; -.
DR   HOGENOM; CLU_001771_0_3_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR   CDD; cd00371; HMA; 1.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR000579; Cation-trans_P-type_ATPase_A/B.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   Pfam; PF00403; HMA; 1.
DR   PRINTS; PR00940; CATPATPASEA.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF55008; SSF55008; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Copper; Copper transport; Ion transport;
KW   Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..761
FT                   /note="Copper-exporting P-type ATPase"
FT                   /id="PRO_0000426888"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        361..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        387..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        695..714
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        718..735
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          14..78
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   ACT_SITE        443
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q59385"
FT   BINDING         25
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         28
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
SQ   SEQUENCE   761 AA;  78851 MW;  D397901EC5C513BE CRC64;
     MTTAVTGEHH ASVQRIQLRI SGMSCSACAH RVESTLNKLP GVRAAVNFGT RVATIDTSEA
     VDAAALCQAV RRAGYQADLC TDDGRSASDP DADHARQLLI RLAIAAVLFV PVADLSVMFG
     VVPATRFTGW QWVLSALALP VVTWAAWPFH RVAMRNARHH AASMETLISV GITAATIWSL
     YTVFGNHSPI ERSGIWQALL GSDAIYFEVA AGVTVFVLVG RYFEARAKSQ AGSALRALAA
     LSAKEVAVLL PDGSEMVIPA DELKEQQRFV VRPGQIVAAD GLAVDGSAAV DMSAMTGEAK
     PTRVRPGGQV IGGTTVLDGR LIVEAAAVGA DTQFAGMVRL VEQAQAQKAD AQRLADRISS
     VFVPAVLVIA ALTAAGWLIA GGQPDRAVSA ALAVLVIACP CALGLATPTA MMVASGRGAQ
     LGIFLKGYKS LEATRAVDTV VFDKTGTLTT GRLQVSAVTA APGWEADQVL ALAATVEAAS
     EHSVALAIAA ATTRRDAVTD FRAIPGRGVS GTVSGRAVRV GKPSWIGSSS CHPNMRAARR
     HAESLGETAV FVEVDGEPCG VIAVADAVKD SARDAVAALA DRGLRTMLLT GDNPESAAAV
     ATRVGIDEVI ADILPEGKVD VIEQLRDRGH VVAMVGDGIN DGPALARADL GMAIGRGTDV
     AIGAADIILV RDHLDVVPLA LDLARATMRT VKLNMVWAFG YNIAAIPVAA AGLLNPLVAG
     AAMAFSSFFV VSNSLRLRKF GRYPLGCGTV GGPQMTAPSS A