CTPB_MYCLE
ID CTPB_MYCLE Reviewed; 750 AA.
AC P46840;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cation-transporting P-type ATPase B;
DE EC=7.2.2.-;
GN Name=ctpB; OrderedLocusNames=ML2000;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7476188; DOI=10.1111/j.1365-2958.1995.tb02317.x;
RA Fsihi H., Cole S.T.;
RT "The Mycobacterium leprae genome: systematic sequence analysis identifies
RT key catabolic enzymes, ATP-dependent transport systems and a novel polA
RT locus associated with genomic variability.";
RL Mol. Microbiol. 16:909-919(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; Multi-pass membrane protein.
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; Z46257; CAA86363.1; -; Genomic_DNA.
DR EMBL; AL583924; CAC30955.1; -; Genomic_DNA.
DR PIR; C87159; C87159.
DR PIR; S77653; S77653.
DR RefSeq; NP_302350.1; NC_002677.1.
DR RefSeq; WP_010908670.1; NC_002677.1.
DR AlphaFoldDB; P46840; -.
DR SMR; P46840; -.
DR EnsemblBacteria; CAC30955; CAC30955; CAC30955.
DR KEGG; mle:ML2000; -.
DR PATRIC; fig|272631.5.peg.3760; -.
DR Leproma; ML2000; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_11; -.
DR OMA; YPTYFGY; -.
DR Proteomes; UP000000806; 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; 1.
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; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..750
FT /note="Cation-transporting P-type ATPase B"
FT /id="PRO_0000046167"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 663..683
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 693..713
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 715..735
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 17..80
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 445
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305"
FT BINDING 28
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 31
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT CONFLICT 544..548
FT /note="EGESR -> RRRIT (in Ref. 1; CAA86363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 750 AA; 78101 MW; 1D58477D4A69B00D CRC64;
MTASLVEDTN NNHESVRRIQ LDVAGMLCAA CASRVETKLN KIPGVRASVN FATRVATIDA
VDVAVDELRQ VIEQAGYRAT AHAESAVEEI DPDADYARNL LRRLIVAALL FVPLADLSTM
FAIVPTNRFP GWGYLLTALA APIVTWAAWP FHRVALRNAR YRAASMETLI SAGILAATGW
SLSTIFVDKE PRQTHGIWQA ILHSDSIYFE VAAGVTVFVL AGRFFEARAK SKAGSALRAL
AARGAKNVEV LLPNGAELTI PAGELKKQQH FLVRPGETIT ADGVVIDGTA TIDMSAITGE
ARPVHASPAS TVVGGTTVLD GRLVIEATAV GGDTQFAAMV RLVEDAQVQK ARVQHLADRI
AAVFVPMVFV IAGLAGASWL LAGASPDRAF SVVLGVLVIA CPCTLGLATP TAMMVASGRG
AQLGIFIKGY RALETINAID TVVFDKTGTL TLGQLSVSTV TSTGGWCSGE VLALASAVEA
ASEHSVATAI VAAYADPRPV ADFVAFAGCG VSGVVAEHHV KIGKPSWVTR NAPCDVVLES
ARREGESRGE TVVFVSVDGV ACGAVAIADT VKDSAADAIS ALCSRGLHTI LLTGDNQAAA
RAVAAQVGID TVIADMLPEA KVDVIQRLRD QGHTVAMVGD GINDGPALAC ADLGLAMGRG
TDVAIGAADL ILVRDSLGVV PVALDLARAT MRTIRINMIW AFGYNVAAIP IASSGLLNPL
IAGAAMAFSS FFVVSNSLRL SNFGLSQTSD
