ID A0AAJ3MHG8_PAEPO Unreviewed; 813 AA. AC A0AAJ3MHG8; DT 24-JUL-2024, integrated into UniProtKB/TrEMBL. DT 24-JUL-2024, sequence version 1. DT 02-OCT-2024, entry version 2. DE RecName: Full=Cd(2+)-exporting ATPase {ECO:0000256|ARBA:ARBA00039103}; DE EC=7.2.2.21 {ECO:0000256|ARBA:ARBA00039103}; GN ORFNames=A7312_19355 {ECO:0000313|EMBL:ODA11596.1}, QDS18_19890 GN {ECO:0000313|EMBL:MDH2333120.1}; OS Paenibacillus polymyxa (Bacillus polymyxa). OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus. OX NCBI_TaxID=1406 {ECO:0000313|EMBL:ODA11596.1, ECO:0000313|Proteomes:UP000094974}; RN [1] {ECO:0000313|Proteomes:UP000094974} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFSAN034343 {ECO:0000313|Proteomes:UP000094974}; RA Zheng J., Timme R., Allard M., Strain E., Luo Y., Brown E.; RT "Whole genome shotgun sequencing of cultured foodborne pathogen."; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ODA11596.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CFSAN034343 {ECO:0000313|EMBL:ODA11596.1}; RA Zheng J., Timme R., Allard M., Strain E., Luo Y., Brown E.; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:MDH2333120.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ANTI {ECO:0000313|EMBL:MDH2333120.1}; RA Goncalves O.S., Santana M.F.; RT "Uncovering the Secrets of Slow-Growing Bacteria in Tropical Savanna Soil RT through Cultivation and Genomic Analysis."; RL Submitted (APR-2023) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate; CC Xref=Rhea:RHEA:12132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:48775, CC ChEBI:CHEBI:456216; EC=7.2.2.21; CC Evidence={ECO:0000256|ARBA:ARBA00036510}; 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:ODA11596.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JARVWT010000009; MDH2333120.1; -; Genomic_DNA. DR EMBL; LYND01000011; ODA11596.1; -; Genomic_DNA. DR Proteomes; UP000094974; Unassembled WGS sequence. DR Proteomes; UP001229409; Unassembled WGS sequence. DR CDD; cd00371; HMA; 1. DR CDD; cd07548; P-type_ATPase-Cd_Zn_Co_like; 1. DR Gene3D; 3.30.70.100; -; 1. 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; IPR051014; Cation_Transport_ATPase_IB. 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; TIGR01512; ATPase-IB2_Cd; 1. DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1. DR NCBIfam; TIGR01494; ATPase_P-type; 1. 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; 1. DR Pfam; PF00702; Hydrolase; 1. DR PRINTS; PR00119; CATATPASE. DR PRINTS; PR00941; CDATPASE. 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; 1. 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 Cadmium {ECO:0000256|ARBA:ARBA00022539}; KW Cell membrane {ECO:0000256|RuleBase:RU362081}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065}; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; 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:ARBA00022448}. FT TRANSMEM 197..214 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362081" FT TRANSMEM 220..238 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362081" FT TRANSMEM 422..442 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362081" FT TRANSMEM 454..481 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362081" FT TRANSMEM 764..783 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362081" FT DOMAIN 8..76 FT /note="HMA" FT /evidence="ECO:0000259|PROSITE:PS50846" FT REGION 82..191 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 104..128 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 142..191 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 813 AA; 87582 MW; 6B8112A86F4CDC16 CRC64; MDALKRTERH EWILEGLDCA NCALKIENGV SKIEGVLDCS VNFVTKTLTM TTSSDQKEEV FRQTERKVHR LEPHVRMVVK NARGRLREDS RSNAGAVQSD STEDCACGHE HDGEGEGHTH EVGQHAAHSH AGHHHGAHGK QAHTHDGHNH GDHGHEHHNH HAEHEHGEAT HAHSHSHGDD GHAGHTHDHG TDGMRRMIAR LAIGAVVAAV AWWLPVEGVG KLALFLLAYI IVGGDVVLQA ARSLVRGMAF DEYFLMTLAT VGAFAIGEYP EGVAVMFFYQ IGELFQGIAV NRSRKSISDL MDIRPDYANL KTAESVRRVS PEDVRIGDLI VIKPGEKIPL DGKVIDGKSH VDTSALTGES VPRTVEPGSS VLSGFINTNG LLTVEVSKEF SESAVSKILE LVQNASAKKA PTEKFITKFS RYYTPVVVIV ALLLAVVPPL VVPGAQFADW VYRALVFLVI SCPCALVVSI PLGFFGGIGA ASRSGILIKG GNYLEALNHV KYAVFDKTGT LTKGVFRVTG IYPAGDFTNE SLLETAALAE LHSTHPIAAS LRESYGKELR ADRVQQYSEI SGHGIQAQID GRLVSAGNAK LMEREHVVFN AAQQAGTLDE GTVVHVAVDG TYAGCILISD EVKEDAAQTV ASLKKLGVVK TIMLTGDNRT VAEAVGRQLG LDEVRAELLP QHKAEAIEQL SASKKTSDKI LFVGDGINDT PVLALADVGV AMGGLGSDAA IEAADIVIMN DEPSRLVTAI HIAKRTRRIV WQNIIFALGV KAVFLTLGAF GIATMWEAVF SDVGVTLLAV LNVMRVLKVR SYE //