CTPB_MYCTO
ID CTPB_MYCTO Reviewed; 752 AA.
AC P9WPT8; L0T4B7; P77905; Q10877;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Cation-transporting P-type ATPase B;
DE EC=7.2.2.-;
GN Name=ctpB; OrderedLocusNames=MT0112;
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; AAK44334.1; -; Genomic_DNA.
DR PIR; G70751; G70751.
DR RefSeq; WP_003400797.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WPT8; -.
DR SMR; P9WPT8; -.
DR EnsemblBacteria; AAK44334; AAK44334; MT0112.
DR KEGG; mtc:MT0112; -.
DR PATRIC; fig|83331.31.peg.117; -.
DR HOGENOM; CLU_001771_0_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 CDD; cd00371; HMA; 1.
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; IPR000579; Cation-trans_P-type_ATPase_A/B.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00403; HMA; 1.
DR PRINTS; PR00940; CATPATPASEA.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 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..752
FT /note="Cation-transporting P-type ATPase B"
FT /id="PRO_0000426889"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 15..78
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 446
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 29
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
SQ SEQUENCE 752 AA; 77483 MW; D5247986C5132626 CRC64;
MAAPVVGDAD LQSVRRIRLD VSGMSCAACA SRVETKLNKI PGVRASVNFA TRVATIDAVG
MAADELCGVV EKAGYHAAPH TETTVLDKRT KDPDGAHARR LLRRLLVAAV LFVPLADLST
LFAIVPSARV PGWGYILTAL AAPVVTWAAW PFHSVALRNA RHRTTSMETL ISVGIVAATA
WSLSSVFGDQ PPREGSGIWR AILNSDSIYL EVAAGVTVFV LAGRYFEARA KSKAGSALRA
LAELGAKNVA VLLPDGAELV IPASELKKRQ RFVTRPGETI AADGVVVDGS AAIDMSAMTG
EAKPVRAYPA ASVVGGTVVM DGRLVIEATA VGADTQFAAM VRLVEQAQTQ KARAQRLADH
IAGVFVPVVF VIAGLAGAAW LVSGAGADRA FSVTLGVLVI ACPCALGLAT PTAMMVASGR
GAQLGIFIKG YRALETIRSI DTVVFDKTGT LTVGQLAVST VTMAGSGTSE RDREEVLGLA
AAVESASEHA MAAAIVAASP DPGPVNGFVA VAGCGVSGEV GGHHVEVGKP SWITRTTPCH
DAALVSARLD GESRGETVVF VSVDGVVRAA LTIADTLKDS AAAAVAALRS RGLRTILLTG
DNRAAADAVA AQVGIDSAVA DMLPEGKVDV IQRLREEGHT VAMVGDGIND GPALVGADLG
LAIGRGTDVA LGAADIILVR DDLNTVPQAL DLARATMRTI RMNMIWAFGY NVAAIPIAAA
GLLNPLIAGA AMAFSSFFVV SNSLRLRNFG AQ
