CTPJ_MYCTU
ID CTPJ_MYCTU Reviewed; 660 AA.
AC P9WPT7; 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 51.
DE RecName: Full=Probable cation-transporting P-type ATPase J;
DE EC=7.2.2.-;
GN Name=ctpJ; Synonyms=nmtA; OrderedLocusNames=Rv3743c;
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 INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12163508; DOI=10.1074/jbc.m207677200;
RA Cavet J.S., Meng W., Pennella M.A., Appelhoff R.J., Giedroc D.P.,
RA Robinson N.J.;
RT "A nickel-cobalt-sensing ArsR-SmtB family repressor. Contributions of
RT cytosol and effector binding sites to metal selectivity.";
RL J. Biol. Chem. 277:38441-38448(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 -!- INDUCTION: Transcription is repressed by NmtR. Induced by nickel and,
CC to some extent, cobalt. {ECO:0000269|PubMed:12163508}.
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; CCP46570.1; -; Genomic_DNA.
DR PIR; H70798; H70798.
DR RefSeq; NP_218260.1; NC_000962.3.
DR RefSeq; WP_003899665.1; NZ_NVQJ01000009.1.
DR AlphaFoldDB; P9WPT7; -.
DR SMR; P9WPT7; -.
DR STRING; 83332.Rv3743c; -.
DR PaxDb; P9WPT7; -.
DR DNASU; 885106; -.
DR GeneID; 885106; -.
DR KEGG; mtu:Rv3743c; -.
DR TubercuList; Rv3743c; -.
DR eggNOG; COG2217; Bacteria.
DR OMA; FAQPWET; -.
DR PhylomeDB; P9WPT7; -.
DR Proteomes; UP000001584; 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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..660
FT /note="Probable cation-transporting P-type ATPase J"
FT /id="PRO_0000419203"
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
