CTPE_MYCTO
ID CTPE_MYCTO Reviewed; 797 AA.
AC P9WPT0; 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 48.
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=MT0931;
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: 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}.
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DR EMBL; AE000516; AAK45178.1; -; Genomic_DNA.
DR PIR; D70581; D70581.
DR RefSeq; WP_003917373.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WPT0; -.
DR SMR; P9WPT0; -.
DR EnsemblBacteria; AAK45178; AAK45178; MT0931.
DR KEGG; mtc:MT0931; -.
DR PATRIC; fig|83331.31.peg.1000; -.
DR HOGENOM; CLU_002360_5_1_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: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:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW ATP-binding; Calcium; Calcium transport; Cell membrane; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..797
FT /note="Calcium-transporting ATPase CtpE"
FT /id="PRO_0000426893"
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; 85000 MW; 56FA84FC6043ED7B 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 LALVLPSGLA YVVIFSLPLA REKFLLDASN LATTSIALAV GVVGAATIEA
MWWIRSRMLG VKPRVWR
