#=GF ID WW_like
#=GF AC PF17890.5
#=GF DE Peptidoglycan hydrolase LytB WW-like domain
#=GF AU El-Gebali S;0000-0003-1378-5495
#=GF SE ECOD:EUF00655
#=GF GA 37.80 37.80;
#=GF TC 71.30 71.30;
#=GF NC 34.10 23.00;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -E 1000 -Z 75585367 --cpu 4 HMM pfamseq
#=GF TP Domain
#=GF RN [1]
#=GF RM 25002590
#=GF RT Structure of pneumococcal peptidoglycan hydrolase LytB reveals
#=GF RT insights into the bacterial cell wall remodeling and
#=GF RT pathogenesis.
#=GF RA Bai XH, Chen HJ, Jiang YL, Wen Z, Huang Y, Cheng W, Li Q, Qi L,
#=GF RA Zhang JR, Chen Y, Zhou CZ;
#=GF RL J Biol Chem. 2014;289:23403-23416.
#=GF DR INTERPRO; IPR040742;
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC Structural analysis revealed that the catalytic domain of LytB
#=GF CC consists of three structurally independent modules: SH3b, WW
#=GF CC domain-like, and the glycoside hydrolase family 73 (GH73). This
#=GF CC entry is the WW like domain found in
#=GF CC endo-beta-N-acetylglucosaminidase LytB from Streptococcus
#=GF CC pneumoniae. Functional analysis show that the deletion of both
#=GF CC SH3b and WW modules almost completely abolished the activity of
#=GF CC LytB. Furthermore, it was shown that the SH3b and WW modules are
#=GF CC indispensable for LytB in cell separation [1].
#=GF SQ 5
#=GS J1DJ95_STREE/181-233 AC J1DJ95.1
#=GS F9PWK5_9STRE/490-542 AC F9PWK5.1
#=GS LYTB_STRR6/496-548 AC P59206.1
#=GS A0A2X4N2H5_9BACL/448-500 AC A0A2X4N2H5.1
#=GS A5M7A1_STREE/496-548 AC A5M7A1.1
J1DJ95_STREE/181-233 .DFIPYYESDGHRFYHYVAQNASIPVASHLSDMEVGKKYYSADGLHFDGFKLEN.
F9PWK5_9STRE/490-542 .EFIPHYTSDGRYIYHELSPYTSIRVAPHSSSMEIGKKYYSADGVNFDTFKVEN.
LYTB_STRR6/496-548 .DFIPYYESDGHRFYHYVAQNASIPVASHLSDMEVGKKYYSADGLHFDGFKLEN.
A0A2X4N2H5_9BACL/448-500 t-FIPDYVSDGKYVYHRYSQYSKVMVARHHQDMVVGKSYYSADGINFGTFKLD-h
A5M7A1_STREE/496-548 .DFIPYYESDGHRFYHYVAQNASIPVASHLSDMEVGKKYYSADGLHFDGFKLEN.
#=GC seq_cons .DFIPYYESDGHRFYHYVAQNASIPVASHLSDMEVGKKYYSADGLHFDGFKLEN.
//
