CTPA_MYCTU
ID CTPA_MYCTU Reviewed; 761 AA.
AC P9WPU1; L0T5H9; Q10876;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Copper-exporting P-type ATPase {ECO:0000305};
DE EC=7.2.2.8 {ECO:0000269|PubMed:25967101};
DE AltName: Full=Copper-exporting P-type ATPase A;
GN Name=ctpA; OrderedLocusNames=Rv0092; ORFNames=MTCY251.11;
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.
RX PubMed=21035536; DOI=10.1016/j.micpath.2010.10.003;
RA Kumar M., Khan F.G., Sharma S., Kumar R., Faujdar J., Sharma R.,
RA Chauhan D.S., Singh R., Magotra S.K., Khan I.A.;
RT "Identification of Mycobacterium tuberculosis genes preferentially
RT expressed during human infection.";
RL Microb. Pathog. 50:31-38(2011).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=H37Rv;
RX PubMed=25967101; DOI=10.1007/s10534-015-9860-x;
RA Leon-Torres A., Novoa-Aponte L., Soto C.Y.;
RT "CtpA, a putative Mycobacterium tuberculosis P-type ATPase, is stimulated
RT by copper (I) in the mycobacterial plasma membrane.";
RL BioMetals 28:713-724(2015).
CC -!- FUNCTION: Involved in copper export. Could be involved in the copper
CC detoxification of mycobacterial cells. {ECO:0000269|PubMed:25967101}.
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:0000269|PubMed:25967101};
CC -!- ACTIVITY REGULATION: ATPase activity is stimulated by Cu(+) ions.
CC {ECO:0000269|PubMed:25967101}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:25967101};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius. Active across a broad
CC temperature range. {ECO:0000269|PubMed:25967101};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25967101};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Up-regulated in pulmonary and extrapulmonary TB patients.
CC {ECO:0000269|PubMed:21035536}.
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; CCP42817.1; -; Genomic_DNA.
DR PIR; D70750; D70750.
DR RefSeq; NP_214606.1; NC_000962.3.
DR RefSeq; WP_003899808.1; NZ_NVQJ01000005.1.
DR AlphaFoldDB; P9WPU1; -.
DR SMR; P9WPU1; -.
DR STRING; 83332.Rv0092; -.
DR TCDB; 3.A.3.5.41; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; P9WPU1; -.
DR PaxDb; P9WPU1; -.
DR DNASU; 886946; -.
DR GeneID; 886946; -.
DR KEGG; mtu:Rv0092; -.
DR TubercuList; Rv0092; -.
DR eggNOG; COG2217; Bacteria.
DR OMA; NDGCTII; -.
DR PhylomeDB; P9WPU1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
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:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell membrane; Copper; Copper transport;
KW Ion transport; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..761
FT /note="Copper-exporting P-type ATPase"
FT /id="PRO_0000046165"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 695..714
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 718..735
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 14..78
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 443
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q59385"
FT BINDING 25
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 28
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
SQ SEQUENCE 761 AA; 78851 MW; D397901EC5C513BE CRC64;
MTTAVTGEHH ASVQRIQLRI SGMSCSACAH RVESTLNKLP GVRAAVNFGT RVATIDTSEA
VDAAALCQAV RRAGYQADLC TDDGRSASDP DADHARQLLI RLAIAAVLFV PVADLSVMFG
VVPATRFTGW QWVLSALALP VVTWAAWPFH RVAMRNARHH AASMETLISV GITAATIWSL
YTVFGNHSPI ERSGIWQALL GSDAIYFEVA AGVTVFVLVG RYFEARAKSQ AGSALRALAA
LSAKEVAVLL PDGSEMVIPA DELKEQQRFV VRPGQIVAAD GLAVDGSAAV DMSAMTGEAK
PTRVRPGGQV IGGTTVLDGR LIVEAAAVGA DTQFAGMVRL VEQAQAQKAD AQRLADRISS
VFVPAVLVIA ALTAAGWLIA GGQPDRAVSA ALAVLVIACP CALGLATPTA MMVASGRGAQ
LGIFLKGYKS LEATRAVDTV VFDKTGTLTT GRLQVSAVTA APGWEADQVL ALAATVEAAS
EHSVALAIAA ATTRRDAVTD FRAIPGRGVS GTVSGRAVRV GKPSWIGSSS CHPNMRAARR
HAESLGETAV FVEVDGEPCG VIAVADAVKD SARDAVAALA DRGLRTMLLT GDNPESAAAV
ATRVGIDEVI ADILPEGKVD VIEQLRDRGH VVAMVGDGIN DGPALARADL GMAIGRGTDV
AIGAADIILV RDHLDVVPLA LDLARATMRT VKLNMVWAFG YNIAAIPVAA AGLLNPLVAG
AAMAFSSFFV VSNSLRLRKF GRYPLGCGTV GGPQMTAPSS A
