ID G3A2S0_9RALS Unreviewed; 748 AA.
AC G3A2S0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 08-NOV-2023, entry version 58.
DE SubName: Full=Copper transporting P-type ATPase {ECO:0000313|EMBL:CCA85729.1};
DE EC=3.6.3.4 {ECO:0000313|EMBL:CCA85729.1};
GN Name=copA {ECO:0000313|EMBL:CCA85729.1};
GN ORFNames=RALSY_20338 {ECO:0000313|EMBL:CCA85729.1};
OS Ralstonia syzygii R24.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=907261 {ECO:0000313|EMBL:CCA85729.1};
RN [1] {ECO:0000313|EMBL:CCA85729.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R24 {ECO:0000313|EMBL:CCA85729.1};
RX PubMed=21931687; DOI=10.1371/journal.pone.0024356;
RA Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S.,
RA Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., Prior P.;
RT "Ralstonia syzygii, the Blood Disease Bacterium and some Asian R.
RT solanacearum strains form a single genomic species despite divergent
RT lifestyles.";
RL PLoS ONE 6:e24356-e24356(2011).
RN [2] {ECO:0000313|EMBL:CCA85729.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R24 {ECO:0000313|EMBL:CCA85729.1};
RA Genoscope - CEA;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
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DR EMBL; FR854087; CCA85729.1; -; Genomic_DNA.
DR AlphaFoldDB; G3A2S0; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd00371; HMA; 1.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; 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 NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00941; CDATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 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 {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Hydrolase {ECO:0000313|EMBL:CCA85729.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 99..120
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 126..145
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 189..207
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 342..364
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 689..708
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 714..731
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 10..75
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 748 AA; 77494 MW; 30AA4DCEF01202FF CRC64;
MTAASLADAA SLDLEIQGMT CAACAGRVER ALRAVPGVTQ ASVNLATERA RVQRANEVSG
DALVAAVVAA GYEARIASDG TAVAPPGAEP GFWDGPGPVW VSAALSLPLV APMLAGWLGA
GWMLPAWLQW LLATPVQCVI GARFYRAGWK ALRAGAGNMD LLVALGTSAA YGLSLWLWWR
ADAGDMPHLY FESAAVVITL VRLGKWLEAR VKRQTAQAIR ALQALWPDTA RVRGADGVLR
DVPVAQVRVD DAVSVRAGER IPVDGTVVEG ASHVDQSMLT GESLPVPTRT GDHVTAGAIA
TDGVLLVRTT AIGADTMLSR IIRLVEDAQA AKPPIQQLVD RVSAIFVPAV LVAALVTLTG
WMIAGAGWET AIVNAVAVLV IACPCALGLA TPSAIMAGTG AGARRGILIA DAQALERAQQ
VDFVVFDKTG TLTLGQPRVV AVEAAPGIDA DAVLDQLAAL QAEHTHPLAQ ATRDRASARG
RGIAPAQSPE VLAGRGVRGS VDGAVLSLGN ARWMDELHLD RTPLQARADV LEAQGNTVSW
LAQGGADGRA QLRGLIAFGD ALKPGAREAV AELRRRGIRT ALVTGDNAGA ARSVAEALGI
EATAAQVLPQ DKAARVTAWQ QGGHVVAMVG DGINDAPALA AADVGIAMAT GTDVAMQAAG
ITLMRGEPRL VSAALDLSQR TVAKIRQNLF WAFVYNVVGI PLAAFGLLSP TFAGAAMAFS
SVSVVTNALM LRRWRPGWET ATATGDRA
//
