CTPV_MYCTU
ID CTPV_MYCTU Reviewed; 770 AA.
AC P9WPS3; L0T821; P77894;
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 copper-exporting P-type ATPase V;
DE EC=7.2.2.8;
DE AltName: Full=Cu(+)-exporting ATPase;
GN Name=ctpV; OrderedLocusNames=Rv0969; ORFNames=MTCY10D7.05c;
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 SUBCELLULAR LOCATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15952732; DOI=10.1021/pr0500049;
RA Xiong Y., Chalmers M.J., Gao F.P., Cross T.A., Marshall A.G.;
RT "Identification of Mycobacterium tuberculosis H37Rv integral membrane
RT proteins by one-dimensional gel electrophoresis and liquid chromatography
RT electrospray ionization tandem mass spectrometry.";
RL J. Proteome Res. 4:855-861(2005).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17143269; DOI=10.1038/nchembio844;
RA Liu T., Ramesh A., Ma Z., Ward S.K., Zhang L., George G.N., Talaat A.M.,
RA Sacchettini J.C., Giedroc D.P.;
RT "CsoR is a novel Mycobacterium tuberculosis copper-sensing transcriptional
RT regulator.";
RL Nat. Chem. Biol. 3:60-68(2007).
RN [4]
RP FUNCTION IN COPPER HOMEOSTASIS AND IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20624225; DOI=10.1111/j.1365-2958.2010.07273.x;
RA Ward S.K., Abomoelak B., Hoye E.A., Steinberg H., Talaat A.M.;
RT "CtpV: a putative copper exporter required for full virulence of
RT Mycobacterium tuberculosis.";
RL Mol. Microbiol. 77:1096-1110(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
CC -!- FUNCTION: Necessary for copper homeostasis and likely functions as a
CC copper exporter. Also required for full virulence.
CC {ECO:0000269|PubMed:20624225}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15952732};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15952732}.
CC -!- INDUCTION: Induced by copper ions via CsoR.
CC {ECO:0000269|PubMed:17143269}.
CC -!- DISRUPTION PHENOTYPE: Mutants show increased copper sensitivity.
CC {ECO:0000269|PubMed:20624225}.
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; CCP43718.1; -; Genomic_DNA.
DR PIR; G70718; G70718.
DR RefSeq; NP_215484.3; NC_000962.3.
DR RefSeq; WP_009935691.1; NZ_NVQJ01000001.1.
DR AlphaFoldDB; P9WPS3; -.
DR SMR; P9WPS3; -.
DR STRING; 83332.Rv0969; -.
DR PaxDb; P9WPS3; -.
DR DNASU; 885254; -.
DR GeneID; 885254; -.
DR KEGG; mtu:Rv0969; -.
DR PATRIC; fig|83332.111.peg.1076; -.
DR TubercuList; Rv0969; -.
DR eggNOG; COG2217; Bacteria.
DR OMA; NAPLMHL; -.
DR PhylomeDB; P9WPS3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
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; HDA:MTBBASE.
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 GO; GO:0010273; P:detoxification of copper ion; IDA:MTBBASE.
DR GO; GO:0046688; P:response to copper ion; IDA:MTBBASE.
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 PRINTS; PR00120; HATPASE.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Copper; Copper transport; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..770
FT /note="Probable copper-exporting P-type ATPase V"
FT /id="PRO_0000046348"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 718..737
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 741..760
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..66
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 103..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 460
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 660
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 664
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 770 AA; 80103 MW; 08CE6D54EF4F9ECA CRC64;
MRVCVTGFNV DAVRAVAIEE TVSQVTGVHA VHAYPRTASV VIWYSPELGD TAAVLSAITK
AQHVPAELVP ARAPHSAGVR GVGVVRKITG GIRRMLSRPP GVDKPLKASR CGGRPRGPVR
GSASWPGEQN RRERRTWLPR VWLALPLGLL ALGSSMFFGA YPWAGWLAFA ATLPVQFVAG
WPILRGAVQQ ARALTSNMDT LIALGTLTAF VYSTYQLFAG GPLFFDTSAL IIAFVVLGRH
LEARATGKAS EAISKLLELG AKEATLLVDG QELLVPVDQV QVGDLVRVRP GEKIPVDGEV
TDGRAAVDES MLTGESVPVE KTAGDRVAGA TVNLDGLLTV RATAVGADTA LAQIVRLVEQ
AQGDKAPVQR LADRVSAVFV PAVIGVAVAT FAGWTLIAAN PVAGMTAAVA VLIIACPCAL
GLATPTAIMV GTGRGAELGI LVKGGEVLEA SKKIDTVVFD KTGTLTRARM RVTDVIAGQR
RQPDQVLRLA AAVESGSEHP IGAAIVAAAH ERGLAIPAAN AFTAVAGHGV RAQVNGGPVV
VGRRKLVDEQ HLVLPDHLAA AAVEQEERGR TAVFVGQDGQ VVGVLAVADT VKDDAADVVG
RLHAMGLQVA MITGDNARTA AAIAKQVGIE KVLAEVLPQD KVAEVRRLQD QGRVVAMVGD
GVNDAPALVQ ADLGIAIGTG TDVAIEASDI TLMSGRLDGV VRAIELSRQT LRTIYQNLGW
AFGYNTAAIP LAALGALNPV VAGAAMGFSS VSVVTNSLRL RRFGRDGRTA
