Gene Ontology annotation through association of InterPro records with GO terms
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
UniProtKB record A0A0H2LVW9 (A0A0H2LVW9_VARPD) - P-type Zn(2+) transporter CadA2 from Variovorax paradoxus TBEA6
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VPARA_44980 (cadA2, A0A0H2LVW9) is a 759-aa P1B-2-type heavy-metal transporting ATPase (NCBIfam TIGR01512, InterPro IPR027256, PANTHER PTHR48085:SF5, PROSITE PS00154) containing an N-terminal HMA domain (InterPro IPR006121), a P-type ATPase actuator domain (Pfam PF00122, residues 251-352), and six RuleBase-annotated transmembrane helices.
"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}."
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VPARA_44980 (cadA2) corresponds to EMBL CDS accession KLN54354.1 on genomic contig JZWI01000024, four ORFs downstream of the czcA3-czcB-czcC-czcI-czcR-cusS (VPARA_44890-VPARA_44940, KLN54345.1-KLN54350.1) heavy-metal resistance cluster.
"DR EMBL; JZWI01000024; KLN54354.1; -; Genomic_DNA."
The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase.
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Everted membrane vesicles containing E. coli ZntA catalyze ATP-dependent, vanadate-sensitive accumulation of 65Zn(II) and 109Cd(II), and zntA disruption causes hypersensitivity to zinc and cadmium salts.
"Everted membrane vesicles from a wild-type strain accumulated 65Zn(II) and 109Cd(II) by using ATP as an energy source. Transport was sensitive to vanadate, an inhibitor of P-type ATPases."
Interplay of the Czc system and two P-type ATPases in conferring metal resistance to Ralstonia metallidurans.
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CadA and ZntA are soft-metal-transporting P1B-type ATPases that export cytoplasmic Cd(2+) and Zn(2+) in concert with the tripartite CzcCBA RND efflux system.
"Cadmium and zinc are removed from cells of Ralstonia metallidurans by the CzcCBA efflux pump and by two soft-metal-transporting P-type ATPases, CadA and ZntA."
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Both ZntA and CadA decrease cellular zinc and cadmium accumulation when expressed in E. coli, with ZntA predominantly conferring zinc resistance and CadA predominantly conferring cadmium resistance.
"Expression of zntA from R. metallidurans in Escherichia coli predominantly mediated resistance to zinc, and expression of cadA predominantly mediated resistance to cadmium. Both transporters decreased the cellular content of zinc or cadmium in this host."