ID   CTPE_MYCTU              Reviewed;         797 AA.
AC   P9WPT1; L0T595; O08365; P0A504;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Calcium-transporting ATPase CtpE {ECO:0000250|UniProtKB:A0R3Y2};
DE            EC=7.2.2.10 {ECO:0000250|UniProtKB:A0R3Y2};
GN   Name=ctpE; OrderedLocusNames=Rv0908; ORFNames=MTCY21C12.02;
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   -!- FUNCTION: P-type ATPase involved in specific uptake of calcium.
CC       {ECO:0000250|UniProtKB:A0R3Y2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.10;
CC         Evidence={ECO:0000250|UniProtKB:A0R3Y2};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL123456; CCP43656.1; -; Genomic_DNA.
DR   PIR; D70581; D70581.
DR   RefSeq; NP_215423.1; NC_000962.3.
DR   RefSeq; WP_003898639.1; NZ_NVQJ01000001.1.
DR   AlphaFoldDB; P9WPT1; -.
DR   SMR; P9WPT1; -.
DR   STRING; 83332.Rv0908; -.
DR   PaxDb; P9WPT1; -.
DR   DNASU; 885657; -.
DR   GeneID; 45424871; -.
DR   GeneID; 885657; -.
DR   KEGG; mtu:Rv0908; -.
DR   TubercuList; Rv0908; -.
DR   eggNOG; COG0474; Bacteria.
DR   OMA; RLGRKQC; -.
DR   PhylomeDB; P9WPT1; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
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; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Calcium transport; Cell membrane; Ion transport;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..797
FT                   /note="Calcium-transporting ATPase CtpE"
FT                   /id="PRO_0000046341"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        601..621
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        633..653
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        667..687
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        703..723
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        729..749
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        764..784
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        301
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT   BINDING         301
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT   BINDING         536
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
SQ   SEQUENCE   797 AA;  84973 MW;  4C5034FC6052FC7B CRC64;
     MTRSASATAG LTDAEVAQRV AEGKSNDIPE RVTRTVGQIV RANVFTRINA ILGVLLLIVL
     ATGSLINGMF GLLIIANSVI GMVQEIRAKQ TLDKLAIIGQ AKPLVRRQSG TRTRSTNEVV
     LDDIIELGPG DQVVVDGEVV EEENLEIDES LLTGEADPIA KDAGDTVMSG SFVVSGAGAY
     RATKVGSEAY AAKLAAEASK FTLVKSELRN GINRILQFIT YLLVPAGLLT IYTQLFTTHV
     GWRESVLRMV GALVPMVPEG LVLMTSIAFA VGVVRLGQRQ CLVQELPAIE GLARVDVVCA
     DKTGTLTESG MRVCEVEELD GAGRQESVAD VLAALAAADA RPNASMQAIA EAFHSPPGWV
     VAANAPFKSA TKWSGVSFRD HGNWVIGAPD VLLDPASVAA RQAERIGAQG LRVLLLAAGS
     VAVDHAQAPG QVTPVALVVL EQKVRPDARE TLDYFAVQNV SVKVISGDNA VSVGAVADRL
     GLHGEAMDAR ALPTGREELA DTLDSYTSFG RVRPDQKRAI VHALQSHGHT VAMTGDGVND
     VLALKDADIG VAMGSGSPAS RAVAQIVLLN NRFATLPHVV GEGRRVIGNI ERVANLFLTK
     TVYSVLLALL VGIECLIAIP LRRDPLLFPF QPIHVTIAAW FTIGIPAFIL SLAPNNERAY
     PGFVRRVMTS AVPFGLVIGV ATFVTYLAAY QGRYASWQEQ EQASTAALIT LLMTALWVLA
     VIARPYQWWR LALVLASGLA YVVIFSLPLA REKFLLDASN LATTSIALAV GVVGAATIEA
     MWWIRSRMLG VKPRVWR