ID A0A433RGX4_9BACL Unreviewed; 725 AA.
AC A0A433RGX4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Cd(2+)-exporting ATPase {ECO:0000256|ARBA:ARBA00039103};
DE EC=7.2.2.21 {ECO:0000256|ARBA:ARBA00039103};
GN Name=cadA {ECO:0000313|EMBL:RUS46994.1};
GN ORFNames=ELR57_11355 {ECO:0000313|EMBL:RUS46994.1};
OS Cohnella sp. AR92.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=648716 {ECO:0000313|EMBL:RUS46994.1, ECO:0000313|Proteomes:UP000267180};
RN [1] {ECO:0000313|EMBL:RUS46994.1, ECO:0000313|Proteomes:UP000267180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR92 {ECO:0000313|EMBL:RUS46994.1,
RC ECO:0000313|Proteomes:UP000267180};
RX PubMed=29166641; DOI=10.1159/000480541;
RA Pisa J.H., Manfredi A.P., Perotti N.I., Romero H.G., Breccia J.D.,
RA Martinez M.A.;
RT "Agrowastes as Feedstock for the Production of Endo-?-Xylanase from
RT Cohnella sp. Strain AR92.";
RL J. Mol. Microbiol. Biotechnol. 27:277-288(2017).
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:RUS46994.1}.
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DR EMBL; RZJR01000006; RUS46994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433RGX4; -.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000267180; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008551; F:P-type cadmium transporter activity; IEA:RHEA.
DR CDD; cd00371; HMA; 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; 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; TIGR01511; ATPase-IB1_Cu; 1.
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; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00941; CDATPASE.
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; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01229; COF_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 Hydrolase {ECO:0000313|EMBL:RUS46994.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000267180};
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 112..133
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 139..158
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 338..359
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 365..390
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 669..689
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 695..718
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT REGION 68..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 78656 MW; 9D335EF0C2940D09 CRC64;
MELRVKGLSC PNCAAELEGE IRRLEHGQEA TLSYNSGKLI VNDKISLEQV SRILRSDGAY
LESPAYPQRK HDQHDHHHSH KHDHDHDHGH DHGHDHGHDH GHDHGADGMK RIIAILSLAT
ILYIGTILAS PYLADSTSIV LYLIASLLSG YSTFWRGLKN LARFKFNIDT LMTIALIGAA
AIGDWREATL VAILFGLNEL LEGLGMEKAR KSMETLLQVA PKTAIRVEDG FETVVPISQL
QVGDLVLVKP GEKIPSDGQV TSGKSSVNEA AITGESLPVE KAPGERVFGG SLNNEGVLRV
RIDKAYEDSS LAKILHLVQE AQETKTPTEL FINKFSRYYT PIIIAIAILV IAVPPLFLGG
DWSDWLYQGL AVLIVGCPCA LILSSPIAIV SGITRNARNG ILVKGGVFLE QLGKLDALAL
DKTGTLTMGE PHVEETIVYD NERFYMVAGA IEKASVHPLA KAVMREVNAK GIDTHDAEEI
ETVSGQGITA AYQGRRYWLG NEKSIRHLTF TDEVRTAVQA LKDKGLTLVL LADESGVLGM
FGIADRIREE SPSVIKELHR SGIKRTVMLT GDHAQTAAKV AQAVGVSEYY GDLLPEDKVA
KVKELARTGT VGMIGDGIND APALASAQLG IAMGKGTDSA IETADIVLMQ DHLGKLPSAI
RVSKKVNRII RFNIGTAMGL KLIALLLTIP GWLTLWIAIL SDMGATIFVT LVSLTVLIQR
QREQG
//
