ID E4NKW4_HALBP Unreviewed; 902 AA.
AC E4NKW4;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=heavy metal-translocating P-type ATPase, Cd/Co/Hg/Pb/Zn-transporting {ECO:0000313|EMBL:ADQ66010.1, ECO:0000313|EMBL:ELY27493.1};
GN OrderedLocusNames=Hbor_04060 {ECO:0000313|EMBL:ADQ66010.1};
GN ORFNames=C499_10529 {ECO:0000313|EMBL:ELY27493.1};
OS Halogeometricum borinquense (strain ATCC 700274 / DSM 11551 / JCM 10706 /
OS KCTC 4070 / PR3).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halogeometricum.
OX NCBI_TaxID=469382 {ECO:0000313|EMBL:ADQ66010.1, ECO:0000313|Proteomes:UP000006663};
RN [1] {ECO:0000313|EMBL:ADQ66010.1, ECO:0000313|Proteomes:UP000006663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700274 / DSM 11551 / JCM 10706 / KCTC 4070 / PR3
RC {ECO:0000313|Proteomes:UP000006663}, and PR 3
RC {ECO:0000313|EMBL:ADQ66010.1};
RX PubMed=21304651; DOI=10.4056/sigs.23264;
RA Malfatti S., Tindall B.J., Schneider S., Fahnrich R., Lapidus A.,
RA Labuttii K., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Anderson I.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Chain P.;
RT "Complete genome sequence of Halogeometricum borinquense type strain
RT (PR3).";
RL Stand. Genomic Sci. 1:150-159(2009).
RN [2] {ECO:0000313|EMBL:ELY27493.1, ECO:0000313|Proteomes:UP000011585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11551 {ECO:0000313|EMBL:ELY27493.1,
RC ECO:0000313|Proteomes:UP000011585};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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DR EMBL; CP001690; ADQ66010.1; -; Genomic_DNA.
DR EMBL; AOHT01000033; ELY27493.1; -; Genomic_DNA.
DR RefSeq; WP_006055422.1; NZ_AOHT01000033.1.
DR AlphaFoldDB; E4NKW4; -.
DR STRING; 469382.Hbor_04060; -.
DR GeneID; 9992226; -.
DR KEGG; hbo:Hbor_04060; -.
DR PATRIC; fig|469382.19.peg.2067; -.
DR eggNOG; arCOG01576; Archaea.
DR eggNOG; arCOG02764; Archaea.
DR HOGENOM; CLU_001771_6_4_2; -.
DR OrthoDB; 8588at2157; -.
DR Proteomes; UP000006663; Chromosome.
DR Proteomes; UP000011585; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:InterPro.
DR CDD; cd00371; HMA; 2.
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; 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; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR PANTHER; PTHR48085:SF5; CADMIUM_ZINC-TRANSPORTING ATPASE HMA2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
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; PS50846; HMA_2; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006663};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 211..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 479..498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 830..853
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 53..119
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 122..188
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 902 AA; 94585 MW; 2F6A96BA5DEACE3F CRC64;
MNRDSHDTEE AGHDHGRDHP PSSDDTEACG CDDGCDTDES STSVASGFDG DGQTLRLSVP
EMDCPSCAEK VTKSVRGDAG VRDVDAQPTT GTLYVQYDPT ATDDSAVRSR VESAGYAIAD
EETVTFSVPE MDCPSCAGKV ENSLDGVSGI VDFETQPTAG KVTIRYNPDE ASRGDFVAAI
EGAGYAVEDD GGADSPHDVW RSQRALKTWG GAAFLAVGLG LEFVVEGLDL VLAAPVGYEI
SVAWVSYTLA VLLAGIPILR NGYYSAKNLS LDIDLLMTAG IVGAMAVNMP FEAATLAVLF
SVAELLERFS MDRARNSLRE LMELSPDTAT VLRNSGSSKT SQAEREEVVV PVEDVAVGET
VIVRPGDRVP LDGTVTEGTS AVDESPITGE SVPVDKEPGL EVFAGSIVEE GYLEIETTTP
ASESTLSKVV DMVEDANREK TEAERFIDRF ARYYTPIIVV GAIATATVPP LLFEEPFRMW
FVRALTLLVV ACPCAFVIST PVSVVSGITS AARNGVLVKG GQHLEAMNDV DAVAVDKTGT
LTTGELGVTD VVALNGNDES DVLGCAAAIE SRSEHPIAQA IVEYAADRDV PERDIREFES
ITGKGVKAVL DDKVHYAGKP GLFESLGFDL EHTHVQADGG VRSDGGQAVE DARNCDHGRY
LDLANEVVPR LQAEGKSVVL VGTEDEIEGV VAVADTVRPE SAWAVSRLHD HGISQVVMLT
GDNERTAQVI GERVGVDEVR ADLLPEQKVE AVRELLAEHD SVAMVGDGVN DAPALAAATV
GVAMGAAGTD TALETADVAL LSDDLTRLPY LVDLSNGTSS VIRQNVWSSL VVKGALAVAA
PLGIISVATA IIVGDMGMSL GVTTNALRLA GVDPESAVAD AEADPGDAES SVDDSLADTS
AA
//
