ID   CTPD_MYCTU              Reviewed;         657 AA.
AC   P9WPT3; L0T9Q3; O53160; P63685;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Probable cobalt/nickel-exporting P-type ATPase;
DE            EC=7.2.2.-;
DE   AltName: Full=Cation-transporting P-type ATPase CtpD;
GN   Name=ctpD; OrderedLocusNames=Rv1469; ORFNames=MTV007.16;
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).
CC   -!- FUNCTION: Involved in heavy metal homeostasis. Probably exports nickel
CC       and cobalt ions out of the cell (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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; AL123456; CCP44228.1; -; Genomic_DNA.
DR   PIR; H70872; H70872.
DR   RefSeq; NP_215985.1; NC_000962.3.
DR   RefSeq; WP_003900344.1; NZ_NVQJ01000004.1.
DR   AlphaFoldDB; P9WPT3; -.
DR   SMR; P9WPT3; -.
DR   STRING; 83332.Rv1469; -.
DR   PaxDb; P9WPT3; -.
DR   DNASU; 886578; -.
DR   GeneID; 886578; -.
DR   KEGG; mtu:Rv1469; -.
DR   TubercuList; Rv1469; -.
DR   eggNOG; COG2217; Bacteria.
DR   OMA; IIMIFGH; -.
DR   PhylomeDB; P9WPT3; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   PRINTS; PR00941; CDATPASE.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Cobalt; Magnesium; Membrane; Metal-binding;
KW   Nickel; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Translocase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..657
FT                   /note="Probable cobalt/nickel-exporting P-type ATPase"
FT                   /id="PRO_0000046339"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        299..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        596..618
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        347
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         543
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         547
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   657 AA;  67885 MW;  1AF5A7DD4BC697D5 CRC64;
     MTLTACEVTA AEAPFDRVSK TIPHPLSWGA ALWSVVSVRW ATVALLLFLA GLVAQLNGAP
     EAMWWTLYLA CYLAGGWGSA WAGAQALRNK ALDVDLLMIA AAVGAVAIGQ IFDGALLIVI
     FATSGALDDI ATRHTAESVK GLLDLAPDQA VVVQGDGSER VVAASELVVG DRVVVRPGDR
     IPADGAVLSG ASDVDQRSIT GESMPVAKAR GDEVFAGTVN GSGVLHLVVT RDPSQTVVAR
     IVELVADASA TKAKTQLFIE KIEQRYSLGM VAATLALIVI PLMFGADLRP VLLRAMTFMI
     VASPCAVVLA TMPPLLSAIA NAGRHGVLVK SAVVVERLAD TSIVALDKTG TLTRGIPRLA
     SVAPLDPNVV DARRLLQLAA AAEQSSEHPL GRAIVAEARR RGIAIPPAKD FRAVPGCGVH
     ALVGNDFVEI ASPQSYRGAP LAELAPLLSA GATAAIVLLD GVAIGVLGLT DQLRPDAVES
     VAAMAALTAA PPVLLTGDNG RAAWRVARNA GITDVRAALL PEQKVEVVRN LQAGGHQVLL
     VGDGVNDAPA MAAARAAVAM GAGADLTLQT ADGVTIRDEL HTIPTIIGLA RQARRVVTVN
     LAIAATFIAV LVLWDLFGQL PLPLGVVGHE GSTVLVALNG MRLLTNRSWR AAASAAR