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Database: UniProt
Entry: A0A017HDW4_9RHOB
LinkDB: A0A017HDW4_9RHOB
Original site: A0A017HDW4_9RHOB 
ID   A0A017HDW4_9RHOB        Unreviewed;       820 AA.
AC   A0A017HDW4;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Lead, cadmium, zinc and mercury transporting ATPase/ Copper-translocating P-type ATPase {ECO:0000313|EMBL:EYD72358.1};
DE            EC=3.6.3.3 {ECO:0000313|EMBL:EYD72358.1};
DE            EC=3.6.3.4 {ECO:0000313|EMBL:EYD72358.1};
GN   ORFNames=Lokhon_01153 {ECO:0000313|EMBL:EYD72358.1};
OS   Limimaricola hongkongensis DSM 17492.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Limimaricola.
OX   NCBI_TaxID=1122180 {ECO:0000313|EMBL:EYD72358.1, ECO:0000313|Proteomes:UP000025047};
RN   [1] {ECO:0000313|EMBL:EYD72358.1, ECO:0000313|Proteomes:UP000025047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17492 {ECO:0000313|EMBL:EYD72358.1,
RC   ECO:0000313|Proteomes:UP000025047};
RA   Fiebig A., Goeker M., Klenk H.-P.P.;
RL   Submitted (MAR-2013) 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:EYD72358.1}.
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DR   EMBL; APGJ01000004; EYD72358.1; -; Genomic_DNA.
DR   RefSeq; WP_017928295.1; NZ_KK088650.1.
DR   AlphaFoldDB; A0A017HDW4; -.
DR   STRING; 1122180.Lokhon_01153; -.
DR   PATRIC; fig|1122180.6.peg.1144; -.
DR   eggNOG; COG2217; Bacteria.
DR   HOGENOM; CLU_001771_0_3_5; -.
DR   OrthoDB; 9807843at2; -.
DR   Proteomes; UP000025047; 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; 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; 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: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   Hydrolase {ECO:0000313|EMBL:EYD72358.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000025047};
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        165..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        197..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        236..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        264..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        417..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        445..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        760..780
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        786..807
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          4..66
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          68..134
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          134..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   820 AA;  82996 MW;  B4FA4339DE26AB25 CRC64;
     MTAQPTILRI DNMSCASCVG RVERALAAVP GVTEAQVNLA TEAATLRGGQ PGEIVAALDR
     AGYPARRDRV RLGIDGLSCA SCVGRVERAL AAVPGVIEAR VNLATATAEV DRLAGGAPVA
     ELIAAAQAAG YAARDADDRP SGNGAGATGD RKPAEAGQLM RRAGVAAVLT LPVVGLAMGA
     HAIPGVHAAI AQGIGHWTSW LIQFVLTTLV LAGPGRIFLM RGLPALWRGA PDMNSLVALG
     TLAAWGYSTV ATFAPGLLPE SARAVYFEAA GVIVTLILLG RALEARAKGR TGAAIRALVD
     LQAPVARIER GGETVEIDAG ALRPGDVMLV RPGDRIATDG EVISGESRVD EAMLTGEPVP
     VAKRAGDAVT GGTVNGNGAL RVRATAVGAE TRLAEIIRMV EAAQGAKLPI QGLVDRITAW
     FVPAVLGLAV LTVAAWLLLG PAPALTHALV AGVSVLIIAC PCAMGLAVPV SIMVGTGRAA
     SLGVLFRRGD ALQALDGVRV VAFDKTGTLT QGRPALTDLD ALAGQDEAAI LADVAALEAQ
     SEHPIAAAIV AAARARGLAP QGAEGVEAVP GRGLKGRVGG RAVLVGNARL LSEAGVDPAP
     LEDLARAQAG RGRTPVLVAI DGAPVAALAV ADPLRPEARA VVGTLRSMGV EVAMITGDSR
     VTARTIAAEL GIDLVEAEVL PEGKVAAVQA LRDRGPVAFV GDGINDAPAL AAADVGIAIG
     SGTEVAIESA EVVLSSGRIG AVADALSISR RVMRNIRQNL GWAFGYNIAL IPVAAGALYA
     VNGMMLSPVL AAAAMSVSSV LVLTNALRLR GMQRIVEEGS
//
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