AI Article Synopsis
- The DNA sequence upstream of the amiE gene in Rhodococcus sp. R312 was analyzed, revealing a new open reading frame (ORF) called amiS2, which encodes a 206 amino acid protein with hydrophobic characteristics.
- The AmiS2 protein shares high similarity with proteins from Mycobacterium smegmatis, Pseudomonas aeruginosa, and Helicobacter pylori, and it likely contains seven transmembrane alpha-helices.
- The related amiB2 gene encodes a 351 amino acid protein with an ATP-binding motif and resembles the ATP-binding subunit of bacterial Clp protease, suggesting that both AmiB2 and AmiS2 are part of a novel family of ABC transporters
Article Abstract
The DNA sequence has been determined upstream of the amiE structural gene in the amidase operon of Rhodococcus sp. R312 and a new ORF (amiS2) identified. The amiS2 gene encodes a potential 206 amino acid (aa) protein containing a high proportion of hydrophobic residues. The AmiS2 protein possesses high homology to the ORFP3, amiS and ureI gene products from the Mycobacterium smegmatis (Ms) acetamidase operon, Pseudomonas aeruginosa (Pa) amidase operon and Helicobacter pylori (Hp) urease operon, respectively. Hydropathic analysis and secondary structure prediction of AmiS2 suggested the presence of seven potential transmembrane (TM) alpha-helices. Sequence analysis of the amiB2 gene, located downstream of the Rhodococcus sp. R312 amiE gene, showed that it encoded a 351-aa protein containing a potential ATP-binding motif. AmiB2 showed significant homology with the ATP-binding subunit of the bacterial Clp protease and high homology with the amiB product located within the Pa amidase operon. AmiB2 and AmiS2 appear to be two components of a recently identified novel family of ABC transporters (Wilson et al., 1995) and might be responsible for the adsorption of amidase substrates or release of their hydrolysis products.
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| http://dx.doi.org/10.1016/s0378-1119(96)00478-7 | DOI Listing |
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