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Database: UniProt
Entry: A0A0W7Z532_9BURK
LinkDB: A0A0W7Z532_9BURK
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ID   A0A0W7Z532_9BURK        Unreviewed;       824 AA.
AC   A0A0W7Z532; A0A1V3TM90;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=ATPase {ECO:0000313|EMBL:KUF42320.1};
GN   ORFNames=AS359_02345 {ECO:0000313|EMBL:KUF42320.1};
OS   Comamonas kerstersii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=225992 {ECO:0000313|EMBL:KUF42320.1, ECO:0000313|Proteomes:UP000053300};
RN   [1] {ECO:0000313|EMBL:KUF42320.1, ECO:0000313|Proteomes:UP000053300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12322-1 {ECO:0000313|EMBL:KUF42320.1,
RC   ECO:0000313|Proteomes:UP000053300};
RA   Ming D., Wang M., Hu S., Zhou Y., Jiang T.;
RT   "Complete genome sequence of a multi-drug resistant strain Acidovorax sp.
RT   12322-1.";
RL   Submitted (DEC-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUF42320.1}.
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DR   EMBL; LPXH01000015; KUF42320.1; -; Genomic_DNA.
DR   RefSeq; WP_058879547.1; NZ_MPOF01000007.1.
DR   AlphaFoldDB; A0A0W7Z532; -.
DR   STRING; 225992.B5M06_03950; -.
DR   Proteomes; UP000053300; 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:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
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; 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; 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   Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW   Ion transport {ECO:0000256|ARBA:ARBA00022796};
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:UP000053300};
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}; Transport {ECO:0000256|ARBA:ARBA00022796}.
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        196..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        272..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        424..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        452..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        768..787
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        793..815
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          10..75
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          77..142
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   824 AA;  86092 MW;  6CD95871AD7863BB CRC64;
     MATATPSSSL QVDLPVQGMS CASCVGRVER VLKKLPGVQD ASVNLATEQA RIHFAGAADV
     PAAIAAIEKA GYSVPQHSLE LQVQEMTCAS CVGRVERILR KQPGVLNATV NLATERATVQ
     VVDGVDVARL LAAVSKAGYP AQLLQADAPA ATGSTAQRHA EESQHLQREL WIAAALALPV
     FVMEMGGHLW PAFHHWVHAA IGQHSSWLLQ CVLTTLVLIG PGRRFYAKGI PALLRGGPDM
     NSLVAVGTLA AYGYSLVATF APQWLPAGST HVYYESAAVI VVLILLGRFM EARAKGNTSQ
     AIQQLVQLQA KTARVRRGGQ VMELDIAQVV AGDVLEVRPG ERIPVDGVVL EGRSFVDESM
     LSGEPVPVEK TDGAPLMGGT VNQQGALVMQ ATKVGADTLL AGIIRMVEQA QGAKLPIQAL
     VDKVTMWFVP AVMAVALLTF VGWMVWGPAP ALSLALVNAV AVLIIACPCA MGLATPTSIM
     VGTGRAAQLG VLLRKGEALQ LLKDAKVVAV DKTGTLTKGK PELTDVLLAP GLDRTTVLAQ
     IAAVEAKSEH PIARAIVEGA QAQGLALPAV DSFESLTGRG VRAQVAGVRV DIGADRWMAE
     LGCDVALFAA EAERLGREGK TPLYAAIDGQ LAAMIAVADP IKPSTPAAIA ALHQLGLKVA
     MITGDNRHTA QAIAQQLGID EVVAEVLPGG KVDAVQRLQA QYGTLAYVGD GINDAPALAQ
     ADVGVAIGTG TDIAIESADV VLMSGDLQGV PRAMALSQAT MANIRQNLFW AFAYNVALIP
     VAAGVLYPFN GTLLSPMFAA GAMAMSSVFV LSNALRLRRF MPSI
//
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