ID   CTPD_MYCS2              Reviewed;         647 AA.
AC   A0R3A7;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 118.
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; Synonyms=cadA; OrderedLocusNames=MSMEG_5403, MSMEI_5256;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   FUNCTION IN COBALT AND NICKEL HOMEOSTASIS, INDUCTION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=22591178; DOI=10.1111/j.1365-2958.2012.08082.x;
RA   Raimunda D., Long J.E., Sassetti C.M., Arguello J.M.;
RT   "Role in metal homeostasis of CtpD, a Co(2)(+) transporting P(1B4)-ATPase
RT   of Mycobacterium smegmatis.";
RL   Mol. Microbiol. 84:1139-1149(2012).
CC   -!- FUNCTION: Involved in heavy metal homeostasis. Probably exports nickel
CC       and cobalt ions out of the cell. {ECO:0000269|PubMed:22591178}.
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; Multi-pass membrane protein.
CC   -!- INDUCTION: By both Co(2+) and superoxide stress.
CC       {ECO:0000269|PubMed:22591178}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are hypersensitive to
CC       Co(2+) and Ni(2+) and accumulate these metals in the cytoplasm.
CC       {ECO:0000269|PubMed:22591178}.
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; CP000480; ABK73642.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP41699.1; -; Genomic_DNA.
DR   RefSeq; WP_011730513.1; NZ_SIJM01000006.1.
DR   RefSeq; YP_889645.1; NC_008596.1.
DR   AlphaFoldDB; A0R3A7; -.
DR   SMR; A0R3A7; -.
DR   STRING; 246196.MSMEI_5256; -.
DR   EnsemblBacteria; ABK73642; ABK73642; MSMEG_5403.
DR   EnsemblBacteria; AFP41699; AFP41699; MSMEI_5256.
DR   GeneID; 66736708; -.
DR   KEGG; msg:MSMEI_5256; -.
DR   KEGG; msm:MSMEG_5403; -.
DR   PATRIC; fig|246196.19.peg.5268; -.
DR   eggNOG; COG2217; Bacteria.
DR   OMA; IIMIFGH; -.
DR   OrthoDB; 237367at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   PRINTS; PR00941; CDATPASE.
DR   SFLD; SFLDF00027; p-type_atpase; 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.
PE   1: Evidence at protein level;
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..647
FT                   /note="Probable cobalt/nickel-exporting P-type ATPase"
FT                   /id="PRO_0000422735"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        587..607
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        339
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         532
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         536
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   647 AA;  66686 MW;  A8F6168FA27F7308 CRC64;
     MTALYPAVEP APAARPARPR SGGWLWTVPS VRWAAAALAL FLTGLAAQLL GAPQAVVWTL
     YLACYVVGGW EPAWVGVRAL RNRTLDVDLL MIVAAIGAAT IGQVFDGALL IVIFATSGAL
     EDVATTRTER SVRGLLDLAP EHATLLGDGS QRVVAAADLR PGDVIVVRPG ERISADGTVI
     GGASEVDQSS ITGEPLPAAK DVGDDVFAGT VNGSGALRVE VTREPSQTVV ARIVAMVTEA
     SATKATTQLF IEKIEQRYSA GVVVATLALL TVPLMFGADL RSTLLRAMTF MIVASPCAVV
     LATMPPLLSA IANASRHGVL VKSAVAMERL ADTDVVVLDK TGTLTAGEPV ISRVTVLIDG
     ADVLGMAAAA EQFSEHPLGR AIVAAARGRV VPEAGDFTAL PGRGVRARVA GHVVEVVSPA
     AYAGENAAVR EHCAAIENDG GTAVVVLEDG LPVGVIGLAD RLRPDAPAAV MQLAQLTKHP
     PMLLTGDNRR AAGRLAEEAG IADVHAELLP DGKAAAVQKL QRDNTHVLVV GDGVNDAPAM
     AAAHTSIAMG RAGADLTVQT ADVVTIRDEL ATVPAVIALA RRARRVVIAN LVMAGAAITT
     LVLWDLFGQL PLPLGVAGHE GSTILVALNG LRLLSNRAWI SPGATPT