ATCU_RHILV
ID ATCU_RHILV Reviewed; 841 AA.
AC Q9X5V3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Copper-transporting P-type ATPase;
DE EC=7.2.2.9;
GN Name=actP;
OS Rhizobium leguminosarum bv. viciae.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=387;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=WSM710;
RX PubMed=11936079; DOI=10.1046/j.1365-2958.2002.02791.x;
RA Reeve W.G., Tiwari R.P., Kale N.B., Dilworth M.J., Glenn A.R.;
RT "ActP controls copper homeostasis in Rhizobium leguminosarum bv. viciae and
RT Sinorhizobium meliloti preventing low pH-induced copper toxicity.";
RL Mol. Microbiol. 43:981-991(2002).
CC -!- FUNCTION: Involved in copper efflux.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(2+)(in) + H2O = ADP + Cu(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:10376, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29036, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.9;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Transcriptionally regulated by HmrR in response to Cu(+)
CC ions.
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; AF127795; AAD26860.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9X5V3; -.
DR SMR; Q9X5V3; -.
DR PRIDE; Q9X5V3; -.
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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.620.20; -; 2.
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; IPR009078; Ferritin-like_SF.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR045800; HMBD.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR011017; TRASH_dom.
DR InterPro; IPR007029; YHS_dom.
DR Pfam; PF19335; HMBD; 1.
DR Pfam; PF04945; YHS; 2.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00746; TRASH; 2.
DR SUPFAM; SSF47240; SSF47240; 2.
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.
PE 1: Evidence at protein level;
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..841
FT /note="Copper-transporting P-type ATPase"
FT /id="PRO_0000046326"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 602..622
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 638..658
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 742..762
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 800..820
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 530
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 729
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 733
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 841 AA; 88059 MW; F6BE9E88F4C7BD7D CRC64;
MNIKQEDDHH HSHAHGDNHC HCGHDQEKAA DAIVRDPICG MTVDPQAGKP SLGHGGRIYH
FCSEHCRTKF AAAPEDYLTA KDPVCGMSVD RSTARYFLKA EGEKFYFCSA ACQAKFEADP
AAYRDGQRPT AKPAPKGTLY TCPMHPEVVS DRPGDCPKCG MALEPMGIPP TDEGPNPELV
DFVRRLWVSA ILALPLLALG MGPMLGLPLR EAIGEPQATF IELLLATPVV LWAALPFFRR
AWASVVNRSP NMWTLIGLGV GTAYLYSVVA TLAPGIFPMS FRGHGAAVPV YFEAAAVIVA
LVFVGQVLEL KARERTGSAI RALLDLAPKT ARRIDAEGNE SDVPVDDINV ADRLRVRPGE
RVPVDGSVLE GQSTVDESMI SGEPLPVEKS KGDPLTGGTI NKNGTFVMSA EKVGADTVLS
RIVDMVAKAQ RSRAPIQGAV DRVSAVFVPA VVAVALLAFL AWAAIGPEPR MANGLLAAVA
VLIIACPCAL GLATPMSIMI ATGRGAGEGV LIKDAEALER FSKGDTLIVD KTGTLTEGKP
KLTDIAAFGR VGEDRLLSLA ASLERGSEHP LAEAIVSGAE ERGVPFVEVT GFEAKTGKGV
QGIADGTMVA LGNSAMLADL GIDPAALSEK TEALRGDGKT VMFVVFDGAL AGLVAVADRI
KPTTAAAIQA LHDSGLKIIM ATGDNERTAR AVAKSLGIDE VRADVLPEGK KALIDELRSK
GAIIAMAGDG VNDAPALAAA DVGIAMGTGA DVAMESAGIT LVKGDLTGIV RARRLAEATM
RNIRQNLGFA FGYNALGVPV AAGVLYPILG LLLSPMIAAA AMSLSSVSVI SNALRLRFAK
L
