ID   CTPJ_MYCTO              Reviewed;         660 AA.
AC   P9WPT6; F2GFW6; L0TGM0; O69710; Q7D4Y4;
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=Probable cation-transporting P-type ATPase J;
DE            EC=7.2.2.-;
GN   Name=ctpJ; Synonyms=nmtA; OrderedLocusNames=MT3851;
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   -!- 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; AE000516; AAK48215.1; -; Genomic_DNA.
DR   PIR; H70798; H70798.
DR   RefSeq; WP_003899665.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPT6; -.
DR   SMR; P9WPT6; -.
DR   EnsemblBacteria; AAK48215; AAK48215; MT3851.
DR   KEGG; mtc:MT3851; -.
DR   PATRIC; fig|83331.31.peg.4144; -.
DR   HOGENOM; CLU_001771_6_3_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:0019829; F:ATPase-coupled cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; SSF81660; SSF81660; 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   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Translocase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..660
FT                   /note="Probable cation-transporting P-type ATPase J"
FT                   /id="PRO_0000426890"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        598..618
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        340
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         544
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         548
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   660 AA;  68645 MW;  AAF058332553A1B1 CRC64;
     MAVRELSPAR CTSASPLVLA RRTKLFALSE MRWAALALGL FSAGLLTQLC GAPQWVRWAL
     FLACYATGGW EPGLAGLQAL QRRTLDVDLL MVVAAIGAAA IGQIAEGALL IVIFATSGAL
     EALVTARTAD SVRGLMGLAP GTATRVGAGG GEETVNAADL RIGDIVLVRP GERISADATV
     LAGGSEVDQA TVTGEPLPVD KSIGDQVFAG TVNGTGALRI RVDRLARDSV VARIATLVEQ
     ASQTKARTQL FIEKVEQRYS IGMVAVTLAV FAVPPLWGET LQRALLRAMT FMIVASPCAV
     VLATMPPLLA AIANAGRHGV LAKSAIVMEQ LGTTTRIAFD KTGTLTRGTP ELAGIWVYER
     RFTDDELLRL AAAAEYPSEH PLGAAIVKAA QSRRIRLPTV GEFTAHPGCR VTARVDGHVI
     AVGSATALLG TAGAAALEAS MITAVDFLQG EGYTVVVVVC DSHPVGLLAI TDQLRPEAAA
     AISAATKLTG AKPVLLTGDN RATADRLGVQ VGIDDVRAGL LPDDKVAAVR QLQAGGARLT
     VVGDGINDAP ALAAAHVGIA MGSARSELTL QTADAVVVRD DLTTIPTVIA MSRRARRIVV
     ANLIVAVTFI AGLVVWDLAF TLPLPLGVAR HEGSTIIVGL NGLRLLRHTA WRRAAGTAHR