CTPV_MYCTO
ID CTPV_MYCTO Reviewed; 770 AA.
AC P9WPS2; L0T821; P77894;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 47.
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=MT0997;
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 -!- FUNCTION: Necessary for copper homeostasis and likely functions as a
CC copper exporter. Also required for full virulence (By similarity).
CC {ECO:0000250}.
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:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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=AAK45246.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK45246.1; ALT_INIT; Genomic_DNA.
DR PIR; G70718; G70718.
DR RefSeq; WP_009935691.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WPS2; -.
DR SMR; P9WPS2; -.
DR EnsemblBacteria; AAK45246; AAK45246; MT0997.
DR KEGG; mtc:MT0997; -.
DR PATRIC; fig|83331.31.peg.1069; -.
DR HOGENOM; CLU_001771_11_2_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: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; 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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Copper; Copper transport; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..770
FT /note="Probable copper-exporting P-type ATPase V"
FT /id="PRO_0000426897"
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
