ID   CTPG_MYCTU              Reviewed;         771 AA.
AC   P9WPS7; L0TB69; P63689; Q10866;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Probable cation-transporting ATPase G;
DE            EC=7.2.2.-;
GN   Name=ctpG; OrderedLocusNames=Rv1992c; ORFNames=MTCY39.27;
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).
RN   [2]
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; AL123456; CCP44764.1; -; Genomic_DNA.
DR   PIR; F70757; F70757.
DR   RefSeq; NP_216508.1; NC_000962.3.
DR   RefSeq; WP_003899120.1; NZ_NVQJ01000043.1.
DR   AlphaFoldDB; P9WPS7; -.
DR   SMR; P9WPS7; -.
DR   STRING; 83332.Rv1992c; -.
DR   PaxDb; P9WPS7; -.
DR   DNASU; 888914; -.
DR   GeneID; 888914; -.
DR   KEGG; mtu:Rv1992c; -.
DR   TubercuList; Rv1992c; -.
DR   eggNOG; COG2217; Bacteria.
DR   OMA; HLHLMET; -.
DR   PhylomeDB; P9WPS7; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
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:0015086; F:cadmium ion transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0046688; P:response to copper ion; IDA:MTBBASE.
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   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.
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..771
FT                   /note="Probable cation-transporting ATPase G"
FT                   /id="PRO_0000046345"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        387..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        411..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        657..677
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        716..736
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          19..86
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   REGION          122..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        462
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         651
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         655
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   771 AA;  79309 MW;  31281C919CC116CA CRC64;
     MTTVVDAEVQ LTVVSDAAGR MRVQATGFQF DAGRAVAIED TVGKVAGVQA VHAYPRTASI
     VIWYSRAICD TAAILSAIID AETVPAAAVP AYASRSASNR KAGVVQKIID WSTRTLSGVR
     RDVAAQPSGE TSDACCDGED NEDREPEQLW QVAKLRRAAF SGVLLTASLV AAWAYPLWPV
     VLGLKALALA VGASTFVPSS LKRLAEGRVG VGTLMTIAAL GAVALGELGE AATLAFLFSI
     SEGLEEYATA RTRRGLRALL SLVPDQATVL REGTETIVAS TELHVGDQMI VKPGERLATD
     GIIRAGRTAL DVSAITGESV PVEVGPGDEV FAGSINGLGV LQVGVTATAA NNSLARIVHI
     VEAEQVRKGA SQRLADCIAR PLVPSIMIAA ALIAGTGSVL GNPLVWIERA LVVLVAAAPC
     ALAIAVPVTV VASIGAASRL GVLIKGGAAL ETLGTIRAVA LDKTGTLTAN RPVVIDVATT
     NGATREEVLA VAAALEARSE HPLAVAVLAA TQATTAASDV QAVPGAGLIG RLDGRVVRLG
     RPGWLDAAEL ADHVACMQQA GATAVLVERD QQLLGAIAVR DELRPEAAEV VAGLRTGGYQ
     VTMLTGDNHA TAAALAAQAG IEQVHAELRP EDKAHLVAQL RARQPTAMVG DGVNDAPALA
     AADLGIAMGA MGTDVAIETA DVALMGQDLR HLPQALDHAR RSRQIMVQNV GLSLSIITVL
     MPLALFGILG LAAVVLVHEF TEVIVIANGV RAGRIKPLAG PPKTPDRTIP G