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Database: UniProt
Entry: A0A126V4R2_9RHOB
LinkDB: A0A126V4R2_9RHOB
Original site: A0A126V4R2_9RHOB 
ID   A0A126V4R2_9RHOB        Unreviewed;       835 AA.
AC   A0A126V4R2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=ATPase {ECO:0000313|EMBL:AML52866.1};
GN   ORFNames=RC74_17815 {ECO:0000313|EMBL:AML52866.1};
OS   Falsihalocynthiibacter arcticus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Falsihalocynthiibacter.
OX   NCBI_TaxID=1579316 {ECO:0000313|EMBL:AML52866.1, ECO:0000313|Proteomes:UP000070371};
RN   [1] {ECO:0000313|EMBL:AML52866.1, ECO:0000313|Proteomes:UP000070371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 20958 {ECO:0000313|EMBL:AML52866.1};
RA   Lee Y.M., Baek K., Lee H.K., Shin S.C.;
RT   "Complete genome sequence of Halocynthiibacter arcticus PAMC 20958t from
RT   arctic marine sediment.";
RL   Submitted (FEB-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; CP014327; AML52866.1; -; Genomic_DNA.
DR   RefSeq; WP_039000906.1; NZ_CP014327.1.
DR   AlphaFoldDB; A0A126V4R2; -.
DR   STRING; 1579316.RC74_17815; -.
DR   KEGG; hat:RC74_17815; -.
DR   OrthoDB; 9807843at2; -.
DR   Proteomes; UP000070371; Chromosome.
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:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR   GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR   CDD; cd00371; HMA; 2.
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; IPR006122; HMA_Cu_ion-bd.
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   NCBIfam; TIGR00003; copper ion binding protein; 1.
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; 2.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00943; CUATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 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; 2.
DR   PROSITE; PS50846; HMA_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Cell membrane {ECO:0000256|RuleBase:RU362081};
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
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:UP000070371};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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        161..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        200..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        231..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        264..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        416..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        444..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        759..778
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        784..802
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          5..70
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          72..138
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   835 AA;  86173 MW;  75414B0708B64861 CRC64;
     MADENIVTLS IEGMTCASCV GRVEKSLKAV SGVSSAAVNL ANETAQVQFS SPADLSVLTQ
     ALEGAGYPAV TAEVTLEVEG MTCASCVGRV ERGLKAATGA LDASVNLATE TATLRYIVGA
     TTPADLARVA TGLGYPAKVK AGVDAEKADR KAAEISRLGR LTLIAALLAL PVFILEMGSH
     VIPGMHMWVE RTIGLQTSRI VQFLLTTAVL LGPGLQFYTK GFPLLLKGKP DMNSLVALGT
     SAAYGFSLVS TFAPKLLPQG TANVYFEAAA VIVVLILLGR WLEARAKGRT GEAIRKLVGL
     QAKEARVERN GEVVELPIDE IAVGDVIHLR PGEKIAVDGE VLSGTSYVDE SMITGEPVPV
     EKSEGAMVVG ATVNGAGALT FRATKVGADT MLAQIIAMVE RAQGAKLPIQ GAVDKITAWF
     VPAVIAAAVV TIAVWLIFGP SPALSYAIVA GVAVLIIACP CAMGLATPTS IMVGTGRAAE
     MGVLFRKGDA LQSLQEVKVV ALDKTGTLTA GRPELTDLVI AASFVESEVL RLVAAVETQS
     EHPIAAAIVR AATTRKLDIP TVDTFASITG FGVSASVEGH NILVGADRLM RRDGIDMGDF
     ADTGAALGKK GRSPLYAAID GRIAAVIGVS DPIKPTTPAA IAALHDLGLT VAMITGDNQG
     TADVIARELG IDIVVAEVLP EGKVDALKAL QKQGKLAFVG DGINDAPALA QADVGIAIGT
     GTDVAIETAD VVLMSGELTG VVNAFDISGR VMRNIRQNLF WAFGYNTLLI PVAAGALYPA
     FGVMLSPVLA AGAMAFSSIF VLSNALRLRW VKPAVATTTP PQAAALAPRK TAQAA
//
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