CTPG_MYCTO
ID CTPG_MYCTO Reviewed; 771 AA.
AC P9WPS6; 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 50.
DE RecName: Full=Probable cation-transporting ATPase G;
DE EC=7.2.2.-;
GN Name=ctpG; OrderedLocusNames=MT2048;
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; AAK46325.1; -; Genomic_DNA.
DR PIR; F70757; F70757.
DR RefSeq; WP_003899120.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WPS6; -.
DR SMR; P9WPS6; -.
DR EnsemblBacteria; AAK46325; AAK46325; MT2048.
DR KEGG; mtc:MT2048; -.
DR PATRIC; fig|83331.31.peg.2205; -.
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 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 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..771
FT /note="Probable cation-transporting ATPase G"
FT /id="PRO_0000426895"
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
