Disease relevance of orf4

• As asp1-3, gtf and orf4, but not gly and nss, are conserved in the accessory sec loci of several staphylococcal and streptococcal species, these genes may also have crucial roles in the expression and export of GspB homologues in the other Gram-positive bacteria [1].
• When the fusion protein was expressed in Escherichia coli, glycosylation of this protein was observed only in the presence of both gtf and orf4 [2].
• The gene products of ORF1 and ORF4 reveal some similarities to transposon encoded proteins of Bacillus subtilis and Tn916 [3].

High impact information on orf4

• In addition, the fusion proteins formed insoluble aggregates in protoplasts of the gtf and orf4 mutants [2].
• The amino acid sequence of ORF4 showed homology with other site-specific recombination enzymes, including approximately 30% homology with the resolvase of Tn3 [4].
• ORF4 encodes for a protein highly homologous to orf3 of pVA380-1 of S. ferus, but its function is unknown [5].
• A hybrid protein containing the ORF4 protein fused to the carboxyl terminal end of maltose binding protein was purified from Escherichia coli and found to specifically nick plasmids carrying a 2-kb DNA segment derived from the transposon [6].
• In order to determine whether this open reading frame is part of an expressed gene, we isolated a DNA fragment containing intact ORF 4 and a portion of the downstream ORF 5 by inverse polymerase chain reaction [7].

Biological context of orf4

• These results indicate that the sequences of ORF 4 and ORF 5 are consistent with the structures of ribosomal proteins S10 and L3, respectively, and are present in a ribosomal protein operon [7].

Associations of orf4 with chemical compounds

• In this study, we further characterized the roles of Gly, Nss, Gtf, and Orf4 by investigating the expression and glycosylation of a series of glutathione S-transferase-GspB fusion proteins in M99 and in gly, nss, gtf, and orf4 mutants [2].

References