Structure of the Protease Production Regulatory Protein hpr from Bacillus subtilis.Structure of the Protease Production Regulatory Protein hpr from Bacillus subtilis.
Structural highlights
2fxa is a 4 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
HPR_BACSU Negative regulator of protease production and sporulation. Acts by binding directly to the promoter of protease genes (aprE and nprE), and by repressing oligopeptide permease operons (appABCDF and oppABCDF), thereby preventing uptake of oligopeptides required for initiation of sporulation. Acts with SinR as a corepressor of epr expression.[1][2][3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
↑Kallio PT, Fagelson JE, Hoch JA, Strauch MA. The transition state regulator Hpr of Bacillus subtilis is a DNA-binding protein. J Biol Chem. 1991 Jul 15;266(20):13411-7. PMID:1906467
↑Koide A, Perego M, Hoch JA. ScoC regulates peptide transport and sporulation initiation in Bacillus subtilis. J Bacteriol. 1999 Jul;181(13):4114-7. PMID:10383984
↑Kodgire P, Dixit M, Rao KK. ScoC and SinR negatively regulate epr by corepression in Bacillus subtilis. J Bacteriol. 2006 Sep;188(17):6425-8. PMID:16923912 doi:10.1128/JB.00427-06
