The cell lysis activity of the Streptococcus agalactiae bacteriophage B30 endolysin relies on the cysteine, histidine-dependent amidohydrolase/peptidase domain.
The Streptococcus agalactiae bacteriophage B30 endolysin contains three domains: cysteine, histidine-dependent amidohydrolase/peptidase (CHAP), Acm glycosidase, and the SH3b cell wall binding domain. Truncations and point mutations indicated that the Acm domain requires the SH3b domain for activity, while the CHAP domain is responsible for nearly all the cell lysis activity.
Donovan
David M
DM
Biotechnology and Germplasm Laboratory, ANRI, ARS, USDA, Bldg. 230, Room 104, BARC-East, 10300 Baltimore Ave., Beltsville, MD 20705-23501, USA. ddonovan@anri.barc.usda.gov
Foster-Frey
Juli
J
Dong
Shengli
S
Rousseau
Geneviève M
GM
Moineau
Sylvain
S
Pritchard
David G
DG
D000581:Amidohydrolases / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003545:Cysteine; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D006639:Histidine; D008242:Lysogeny; D008414:Mastitis, Bovine / Q000382:microbiology; D010447:Peptide Hydrolases / Q000737:chemistry*; D017108:Streptococcus Phages / Q000201:enzymology*; D013292:Streptococcus agalactiae / Q000187:drug effects / Q000502:physiology / Q000821:virology*
D006639:Histidine; D010450:Endopeptidases; D010447:Peptide Hydrolases; C001143:endolysin; D000581:Amidohydrolases; D003545:Cysteine