ID A0A1H2VRR9_9GAMM Unreviewed; 861 AA.
AC A0A1H2VRR9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Copper-exporting P-type ATPase {ECO:0000256|ARBA:ARBA00015102};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
DE AltName: Full=Copper-exporting P-type ATPase A {ECO:0000256|ARBA:ARBA00029719};
DE AltName: Full=Cu(+)-exporting ATPase {ECO:0000256|ARBA:ARBA00033239};
GN ORFNames=SAMN05443545_102481 {ECO:0000313|EMBL:SDW71073.1};
OS Aidingimonas halophila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Aidingimonas.
OX NCBI_TaxID=574349 {ECO:0000313|EMBL:SDW71073.1, ECO:0000313|Proteomes:UP000198500};
RN [1] {ECO:0000313|EMBL:SDW71073.1, ECO:0000313|Proteomes:UP000198500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19219 {ECO:0000313|EMBL:SDW71073.1,
RC ECO:0000313|Proteomes:UP000198500};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNNI01000002; SDW71073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2VRR9; -.
DR STRING; 574349.SAMN05443545_102481; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000198500; Unassembled WGS sequence.
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; -; 2.
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; 1.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF6; COPPER-EXPORTING P-TYPE ATPASE; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
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; 2.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000198500};
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 198..216
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 222..241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 262..281
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 287..306
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 443..465
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 471..494
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 787..806
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 812..830
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 107..170
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 61..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 91731 MW; F8F36CEF82810D71 CRC64;
MNQPNLQHRH VPNIRCQGCI DNIRRAIQAH DNNADIVGSS DDKQLHVTTS LEPETLDRLL
ADAGYPPEGE GTGTDNGRQT PLSREQDGEV ESPRSLISEQ RPAKHGTTQR LAISGMTCAS
CVRTVEQALS STSGVTDADV NFGTHTAQVH GTASSEQLVA SVTAVGYGAE PMADLQEAEA
AREDNQTRDY RRHLRGSAMA LGLGVPLMAG MFIVHPDPSG SGQLFWIVIG LLSLGILAGP
GRHFFISAWQ AFTHHQANMD TLVALGTGTA WLYSMVVVLF AEFLPEAARG IYFEASAMII
GLILLGQAME LKARGRTSEA LKRLLDLQSK TARVIRNGDE IDIAVDAVRK GDHIRVRPGE
RLPVDGEVIE GRSHVDESML TGEPVPIAKQ PRDEVNAGTV NGKGSLVYQA TRVGADTRLG
QITEQVARAQ NSRPPIGELA DRVSSVFVPA VMIVAVLTAM VWFNIGAEPR VIHMLVTATT
VLIIACPCAL GLATPISTMI GVGKAAEQGV LIRSGDALQT ASRLTTLIVD KTGTLTEGKP
RVTEARCFGR GESEILADVA ALERGSEHPL ASALLSYAQS RGAAAGEVRD FGSLTGRGVM
ATKTNGDTLR LGNAALLEDA GISLADGSDW ASQLEQDART IIYFARNQRL EAVFGISDPL
RNDAIAAVKR LQDDGLRIVM LTGDNQHTAA AIAASVGIDE FQAGLMPEDK HADIERRQQR
GEVVGMVGDG INDAPALAQA DVGFAIGQGT DVAIESAGMT LIRNSLHGVA DAIEISRATL
INIKQNLWGA FGYNSLCIPI AAGIFYPFTD MLLSPMIAGA AMSLSSVTVV SNANRLRMFR
TSHQATPRQD NQMSRAEEVN A
//
