Characterization of a novel PepF-like oligopeptidase secreted by Bacillus amyloliquefaciens 23-7A.
An oligopeptidase from Bacillus amyloliquefaciens 23-7A was characterized along with its biochemical activities and structural gene. The protein's amino acid sequence and enzymatic activities were similar to those of other bacterial PepFs, which belong to metallopeptidase family M3. While most bacterial PepFs are cytoplasmic endopeptidases, the identified PepFBa oligopeptidase is a secreted protein and may facilitate the process of sporulation.
Chao
Shiou-Huei
SH
Institute of Biochemistry, National Yang-Ming University, 155, Sec. 2, Li-Nong Street, Pei-Tou, Taipei 11221, Taiwan.
Cheng
Tzu-Hao
TH
Shaw
Chin-Ying
CY
Lee
Meng-Hwan
MH
Hsu
Yuan-Hsun
YH
Tsai
Ying-Chieh
YC
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology* / Q000235:genetics / Q000502:physiology; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D008969:Molecular Sequence Data; D017422:Sequence Analysis, DNA; D013379:Substrate Specificity
D001426:Bacterial Proteins; D008666:Metalloendopeptidases; C091036:Oligoendopeptidase F