HMM Summary Page: TIGR03082

Functionmembrane protein AbrB duplication
Trusted Cutoff94.70
Domain Trusted Cutoff94.70
Noise Cutoff70.45
Domain Noise Cutoff70.45
Isology Typedomain
HMM Length157
AuthorHaft DH
Entry DateSep 28 2006 1:27PM
Last ModifiedFeb 14 2011 3:27PM
CommentThe model describes a hydrophobic sequence region that is duplicated to form the AbrB protein of Escherichia coli (not to be confused with a Bacillus subtilis protein with the same gene symbol). In some species, notably the Cyanobacteria and Thermus thermophilus, proteins consist of a single copy rather than two copies. The member from Pseudomonas putida, PP_1415, was suggested to be an ammonia monooxygenase characteristic of heterotrophic nitrifiers, based on an experimental indication of such activity in the organism and a glimmer of local sequence similarity between parts of P. putida protein and an instance of the AmoA protein from Nitrosomonas europaea (PMID:9732537); we do not believe the sequence similarity to be meaningful. The member from E. coli (b0715, ybgN) appears to be the largely uncharacterized AbrB (aidB regulator) protein of E. coli cited in Volkert, et al. (PMID 8002588), although we did not manage to trace the origin of association of the article to the sequence.
ReferencesRN [1] RM PMID: 8002588 RT Induction of the Escherichia coli aidB gene under oxygen-limiting conditions requires a functional rpoS (katF) gene. RA Volkert MR, Hajec LI, Matijasevic Z, Fang FC, Prince R RL J Bacteriol. 1994 Dec;176(24):7638-45. RN [2] RM PMID: 9732537 RT Physiological and molecular biological characterization of ammonia oxidation of the heterotrophic nitrifier Pseudomonas putida. RA Daum M, Zimmer W, Papen H, Kloos K, Nawrath K, Bothe H RL Curr Microbiol. 1998 Oct;37(4):281-8.