CTPA_MYCLE
ID CTPA_MYCLE Reviewed; 780 AA.
AC P46839; Q9CBG9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Copper-exporting P-type ATPase {ECO:0000250|UniProtKB:P9WPU1};
DE EC=7.2.2.8 {ECO:0000250|UniProtKB:P9WPU1};
DE AltName: Full=Copper-exporting P-type ATPase A;
GN Name=ctpA; OrderedLocusNames=ML1987;
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 -!- FUNCTION: Involved in copper export. {ECO:0000250|UniProtKB:P9WPU1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC ChEBI:CHEBI:456216; EC=7.2.2.8;
CC Evidence={ECO:0000250|UniProtKB:P9WPU1};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P9WPU1};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA86358.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAC30942.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z46257; CAA86358.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL583924; CAC30942.1; ALT_FRAME; Genomic_DNA.
DR PIR; F87157; F87157.
DR PIR; S77652; S77652.
DR RefSeq; WP_010908658.1; NC_002677.1.
DR AlphaFoldDB; P46839; -.
DR SMR; P46839; -.
DR EnsemblBacteria; CAC30942; CAC30942; CAC30942.
DR KEGG; mle:ML1987; -.
DR Leproma; ML1987; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_11; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
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; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR PRINTS; PR00940; CATPATPASEA.
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; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Copper; Copper transport; Ion transport;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..780
FT /note="Copper-exporting P-type ATPase"
FT /id="PRO_0000046164"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 680..698
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 704..722
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 2..67
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 430
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q59385"
FT BINDING 13
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 16
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
SQ SEQUENCE 780 AA; 81791 MW; BCA853E957F15C78 CRC64;
MQRIQLNITG MSCSCCAPNG WNNLPNKLSD FSTLVNSATR VAAINLSEVT QTAEVCEAVR
RAALCTDGGE ALQRRQADAD NARYLLIRLA VAAALFVPLA HLSVMFAVLP STHFPGWEWM
LTALAIPVVT WAAWPFHRVA IHNARYHGAS METLISTGIT AATIWSLYTV FGHHQSTEHR
GVWRALLGSD AIYFEVAAGI TVFVLAGKYY TARAKSHASI ALLALAALSA KDAAVLQPDG
SEMVIPANEL NEQQRFVVRP GQTIAADGLV IDGSATVSMS PITGEAKPVR VNPGAQVIGG
TVVLNGRLIV EAAAVGDETQ LAGMVRLVEQ AQQQNANAQR LADRIASVFV PCVFAVAALT
AVGWLIAGSG PDRVFSAAIA VLVIACPCAL GLATPTAMMV ASGRGAQLGI LLKGHESFEA
TRAVDTVVFD KTGTLTTGQL KVSAVTAAPG WQANEVLQMA ATVESASEHA VALAIAASTT
HREPVANFRA VPGHGVSGTV AERAVRVGKP SWIASRCNST TLVTARRNAE LRGETAVFVE
IDGEQCGVIA VADAVKASAA DAVAALHDRG FRTALLTGDN PASAAAVASR IGIDEVIADI
LPEDKVDVIE QLRDRGHVVA MVGDGINDGP ALARADLGMA IGRGTDVAIG AADIILVRDN
LDVVPITLDL AAATMRTIKF NMVWAFGYNI AAIPIAAAGL LNPLVAGAAM AFSSFFVVSN
SLRLRNFGAI LSCGTSRHRT VKRWRCPPPT RLRSTACSPV DASPLRPVAH RTGVKPPTHR
