Family Search for PF20238 (BIM1-like_dom)

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PF20238 hits 31 sequences in PaperBLAST's database above the trusted cutoff. Showing hits to curated sequences only. Or see all hits or try another family.

BIM1_CRYNH / J9VHN6 Copper acquisition factor BIM1; BCS-inducible membrane protein 1; Lytic polysaccharide monooxygenase-like protein BIM1; LPMO-like protein BIM1; EC 1.14.99.- from Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) (see paper)
Aligns to 18:166 / 218 (68.3%), covers 97.9% of PF20238, 97.4 bits

• function: Cell surface-bound protein that functions in the copper- accumulation pathway shared by the CUF1-dependent copper transporter CTR1 (PubMed:31932719). Binds Cu(2+) with an estimated 1:1 stoichiometry and might serve as an extracellular copper ligand (PubMed:31932719). FRE4 and FRE7 metalloreductases probably function together with CTR1 and BIM1 to liberate the Cu(2+) bound to the BIM1 copper-binding site for subsequent import of Cu(+) into the cell by CTR1, via the reduction of BIM1-bound Cu(2+) to Cu(+) to reduce binding affinity for BIM1 but increase affinity for CTR1 (Probable). Facilitates copper acquisition in the brain of mammalian hosts and acts as a copper-dependent virulence trait in fungal meningitis (PubMed:31932719). While BIM1 plays a critical role in cryptococcal meningitis, at least in part through its role in copper acquisition, it could play additional roles during copper limitation or as a means to invade and colonize host tissues in the brain, by compromising host carbohydrate integrity via its lytic polysaccharide monooxygenase (LPMO) activity, which has still to be determined (Probable).
  subunit: Interacts with the CUF1-dependent copper transporter CTR1.
  disruption phenotype: Exhibits growth defect on copper-deficient medium ot in the presence of the copper-specific chelator bathocuproine disulfonic acid (BCS) (PubMed:31932719). Shows a reduction in cell- associated copper, in the enzymatic activity of Cu/Zn superoxide dismutase, in laccase-dependent melanin production and in the accumulation of cellular iron, a well-established copper-dependent process (PubMed:31932719). Does not affect virulence in an A/J mouse pulmonary infection model (PubMed:31932719).

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