CTPD_MYCTO
ID CTPD_MYCTO Reviewed; 657 AA.
AC P9WPT2; 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 45.
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=MT1515;
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 heavy metal homeostasis. Probably exports nickel
CC and cobalt ions out of the cell (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Ni(2+)(out) = ADP + H(+) + Ni(2+)(in) + phosphate;
CC Xref=Rhea:RHEA:15557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49786,
CC ChEBI:CHEBI:456216;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Co(2+)(out) + H2O = ADP + Co(2+)(in) + H(+) + phosphate;
CC Xref=Rhea:RHEA:32779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:48828,
CC ChEBI:CHEBI:456216;
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; AE000516; AAK45780.1; -; Genomic_DNA.
DR PIR; H70872; H70872.
DR RefSeq; WP_003900344.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WPT2; -.
DR SMR; P9WPT2; -.
DR EnsemblBacteria; AAK45780; AAK45780; MT1515.
DR KEGG; mtc:MT1515; -.
DR PATRIC; fig|83331.31.peg.1630; -.
DR HOGENOM; CLU_001771_6_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:0015413; F:ABC-type nickel transporter activity; IEA:RHEA.
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:0032778; F:P-type cobalt transporter activity; IEA:RHEA.
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; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..657
FT /note="Probable cobalt/nickel-exporting P-type ATPase"
FT /id="PRO_0000426892"
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
