GenomeNet

Database: Pfam
Entry: LytB_WW
LinkDB: LytB_WW
Original site: LytB_WW 
#=GF ID   LytB_WW
#=GF AC   PF18342.3
#=GF DE   Endo-beta-N-acetylglucosaminidase LytB WW domain
#=GF AU   El-Gebali S;0000-0003-1378-5495
#=GF SE   ECOD:EUF00921
#=GF GA   25.80 25.80;
#=GF TC   26.80 33.80;
#=GF NC   25.10 23.70;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 57096847 -E 1000 --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; IPR041074;
#=GF DR   SO; 0000417; polypeptide_domain;
#=GF CC   This domain has can be found in
#=GF CC   endo-beta-N-acetylglucosaminidase LytB (EC 3.2.1.96) of S.
#=GF CC   pneumoniae and other gram positive bacteria. Comparative
#=GF CC   analysis revealed that the second all-beta module derived from
#=GF CC   the WW-like segments is structurally similar to the chitin
#=GF CC   binding domain of S. marcescens chitinase ChiB, implying a
#=GF CC   peptide binding function for this module [1].
#=GF SQ   4
#=GS A0A2N6S5E4_9STRE/306-371  AC A0A2N6S5E4.1
#=GS F9PWK5_9STRE/424-489      AC F9PWK5.1
#=GS LYTB_STRR6/429-495        AC P59206.1
#=GS F9Q1W1_STROR/154-219      AC F9Q1W1.1
A0A2N6S5E4_9STRE/306-371             ys--SYYKVTSLYIPVYDANGRILSHVSKDTILFRDNR.ATANGRIPVQVAGITGYVNSGQVAAVNSS-t..
F9PWK5_9STRE/424-489                 ..ALTYYKVKPITAYVYSASGTRLSYISQGSIVAVSAS.GSQGDRLPVQISGLSGFMNKSDLVAVNASD...
LYTB_STRR6/429-495                   na--AYYQVVPVTANVYDSDGEKLSYISQGSVVWLDKDrKSDDKRLAITISGLSGYMKTEDLQALDAS-k..
F9Q1W1_STROR/154-219                 kt--KYYKVKPITAYVYSASGEILSYINQGSIVSLDSS.TRKGGRLAVSISGLSGYMNQSDLTAVD---egs
#=GC seq_cons                        .s..sYYKVpPlTA.VYsAsGchLSYISQGSIVhlDss.sopssRLsVpISGLSGYMNpuDLsAVsuS.p..
//
DBGET integrated database retrieval system