Identification of a copper-repressible C-type heme protein of Methylococcus capsulatus (Bath). A member of a novel group of the bacterial di-heme cytochrome c peroxidase family of proteins

摘要: Genomic sequencing of the methanotrophic bacterium, Methylococcus capsulatus (Bath), revealed an open reading frame (MCA2590) immediately upstream previously described mopE gene (MCA2589). Sequence analyses deduced amino acid sequence demonstrated that MCA2590-encoded protein shared significant, but restricted, similarity to bacterial di-heme cytochrome c peroxidase (BCCP) family proteins. Two putative C-type heme-binding motifs were predicted, and confirmed by positive heme staining. Immunospecific recognition biotinylation whole cells combined with MS expression MCA2590 in M. as a noncovalently associated cellular surface bacterium exposed cell exterior. Similar MopE, is regulated bioavailability copper most abundant cultures grown under low conditions, thus indicating important physiological role these growth conditions. distinguished from characterized members BCCP containing much longer primary generates increased distance between two its sequence. Furthermore, localization contrast periplasmic location reported members. Based on our experimental bioinformatical analyses, we suggest member novel group peroxidases not characterized.