title: Role of rhomboid proteases in bacteria.
abstract: The first member of the rhomboid family of intramembrane serine proteases in bacteria was discovered almost 20years ago. It is now known that rhomboid proteins are widely distributed in bacteria, with some bacteria containing multiple rhomboids. At the present time, only a single rhomboid-dependent function in bacteria has been identified, which is the cleavage of TatA in Providencia stuartii. Mutational analysis has shown that loss of the GlpG rhomboid in Escherichia coli alters cefotaxime resistance, loss of the YqgP (GluP) rhomboid in Bacillus subtilis alters cell division and glucose uptake, and loss of the MSMEG_5036 and MSMEG_4904 genes in Mycobacterium smegmatis results in altered colony morphology, biofilm formation and antibiotic susceptibilities. However, the cellular substrates for these proteins have not been identified. In addition, analysis of the rhombosortases, together with their possible Gly-Gly CTERM substrates, may shed new light on the role of these proteases in bacteria. This article is part of a Special Issue entitled: Intramembrane Proteases.
authors.affiliation: Department of Microbiology and Immunology, 3001 Rollins Research Bldg, Emory University School of Medicine, Atlanta, GA 30322, USA; Atlanta VA Medical Center, Decatur, GA, USA. Electronic address: prather@emory.edu.
authors.forename: Philip
authors.initials: P
authors.lastname: Rather
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D010450:Endopeptidases / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D020102:Mycobacterium smegmatis / Q000201:enzymology* / Q000235:genetics; D059748:Proteolysis; D011532:Providencia / Q000201:enzymology* / Q000235:genetics; D053038:Quorum Sensing; D015398:Signal Transduction; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins; D010450:Endopeptidases
keywords: AarA; GlpG; Rhomboid protease; Twin-arginine transport