ID   CTPB_MYCTU              Reviewed;         752 AA.
AC   P9WPT9; L0T4B7; P77905; Q10877;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Cation-transporting P-type ATPase B;
DE            EC=7.2.2.-;
GN   Name=ctpB; OrderedLocusNames=Rv0103c; ORFNames=MTCY251.22c;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RA   Agranoff D.D., Krishna S.K., Griffin G.E., Mangan J.;
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, 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; Y07638; CAA68915.1; -; Genomic_DNA.
DR   EMBL; AL123456; CCP42828.1; -; Genomic_DNA.
DR   PIR; G70751; G70751.
DR   RefSeq; NP_214617.1; NC_000962.3.
DR   RefSeq; WP_009935939.1; NZ_NVQJ01000053.1.
DR   AlphaFoldDB; P9WPT9; -.
DR   SMR; P9WPT9; -.
DR   STRING; 83332.Rv0103c; -.
DR   PaxDb; P9WPT9; -.
DR   DNASU; 886928; -.
DR   GeneID; 886928; -.
DR   KEGG; mtu:Rv0103c; -.
DR   TubercuList; Rv0103c; -.
DR   eggNOG; COG2217; Bacteria.
DR   OMA; YPTYFGY; -.
DR   PhylomeDB; P9WPT9; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR   GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
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; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..752
FT                   /note="Cation-transporting P-type ATPase B"
FT                   /id="PRO_0000046168"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        361..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        390..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        491..511
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        714..734
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          15..78
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   ACT_SITE        446
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         26
FT                   /ligand="a metal cation"
FT                   /ligand_id="ChEBI:CHEBI:25213"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         29
FT                   /ligand="a metal cation"
FT                   /ligand_id="ChEBI:CHEBI:25213"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
SQ   SEQUENCE   752 AA;  77509 MW;  21563FE4B4407505 CRC64;
     MAAPVVGDAD LQSVRRIRLD VLGMSCAACA SRVETKLNKI PGVRASVNFA TRVATIDAVG
     MAADELCGVV EKAGYHAAPH TETTVLDKRT KDPDGAHARR LLRRLLVAAV LFVPLADLST
     LFAIVPSARV PGWGYILTAL AAPVVTWAAW PFHSVALRNA RHRTTSMETL ISVGIVAATA
     WSLSSVFGDQ PPREGSGIWR AILNSDSIYL EVAAGVTVFV LAGRYFEARA KSKAGSALRA
     LAELGAKNVA VLLPDGAELV IPASELKKRQ RFVTRPGETI AADGVVVDGS AAIDMSAMTG
     EAKPVRAYPA ASVVGGTVVM DGRLVIEATA VGADTQFAAM VRLVEQAQTQ KARAQRLADH
     IAGVFVPVVF VIAGLAGAAW LVSGAGADRA FSVTLGVLVI ACPCALGLAT PTAMMVASGR
     GAQLGIFIKG YRALETIRSI DTVVFDKTGT LTVGQLAVST VTMAGSGTSE RDREEVLGLA
     AAVESASEHA MAAAIVAASP DPGPVNGFVA VAGCGVSGEV GGHHVEVGKP SWITRTTPCH
     DAALVSARLD GESRGETVVF VSVDGVVRAA LTIADTLKDS AAAAVAALRS RGLRTILLTG
     DNRAAADAVA AQVGIDSAVA DMLPEGKVDV IQRLREEGHT VAMVGDGIND GPALVGADLG
     LAIGRGTDVA LGAADIILVR DDLNTVPQAL DLARATMRTI RMNMIWAFGY NVAAIPIAAA
     GLLNPLIAGA AMAFSSFFVV SNSLRLRNFG AQ