title: The cell lysis activity of the Streptococcus agalactiae bacteriophage B30 endolysin relies on the cysteine, histidine-dependent amidohydrolase/peptidase domain.
abstract: 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.
authors.affiliation: 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
authors.forename: David M
authors.initials: DM
authors.lastname: Donovan
authors.forename: Juli
authors.initials: J
authors.lastname: Foster-Frey
authors.forename: Shengli
authors.initials: S
authors.lastname: Dong
authors.forename: Geneviève M
authors.initials: GM
authors.lastname: Rousseau
authors.forename: Sylvain
authors.initials: S
authors.lastname: Moineau
authors.forename: David G
authors.initials: DG
authors.lastname: Pritchard
mesh_terms: 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*
chemical_list: D006639:Histidine; D010450:Endopeptidases; D010447:Peptide Hydrolases; C001143:endolysin; D000581:Amidohydrolases; D003545:Cysteine