ID A0A1J0GRX5_9CAUD Unreviewed; 162 AA. AC A0A1J0GRX5; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 19-JAN-2022, entry version 18. DE RecName: Full=Lysozyme {ECO:0000256|ARBA:ARBA00012732, ECO:0000256|RuleBase:RU003788}; DE EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732, ECO:0000256|RuleBase:RU003788}; GN ORFNames=SH6_0066 {ECO:0000313|EMBL:APC44908.1}; OS Shigella phage SH6. OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Caudovirales; Drexlerviridae; Tunavirinae; Tunavirus; Shigella virus SH6. OX NCBI_TaxID=1913048 {ECO:0000313|EMBL:APC44908.1, ECO:0000313|Proteomes:UP000224004}; RN [1] {ECO:0000313|EMBL:APC44908.1, ECO:0000313|Proteomes:UP000224004} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Hamdi S., Rousseau G.M., Labrie S.J., Tremblay D.M., Kourda R.S., RA Slama K.B., Moineau S.; RT "Characterization of two polyvalent phages infecting Enterobacteriaceae."; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and CC between N-acetyl-D-glucosamine residues in chitodextrins.; CC EC=3.2.1.17; Evidence={ECO:0000256|ARBA:ARBA00000632, CC ECO:0000256|RuleBase:RU003788}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family. CC {ECO:0000256|RuleBase:RU003788}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KX828710; APC44908.1; -; Genomic_DNA. DR Proteomes; UP000224004; Genome. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro. DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW. DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro. DR Gene3D; 1.10.530.40; -; 1. DR HAMAP; MF_04110; ENDOLYSIN_T4; 1. DR HAMAP; MF_04136; SAR_ENDOLYSIN; 1. DR InterPro; IPR034690; Endolysin_T4_type. DR InterPro; IPR002196; Glyco_hydro_24. DR InterPro; IPR023346; Lysozyme-like_dom_sf. DR InterPro; IPR023347; Lysozyme_dom_sf. DR InterPro; IPR043688; SAR_endolysin-like. DR Pfam; PF00959; Phage_lysozyme; 1. DR SUPFAM; SSF53955; SSF53955; 1. PE 3: Inferred from homology; KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529, KW ECO:0000256|RuleBase:RU003788}; KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638, KW ECO:0000256|RuleBase:RU003788}; Cytolysis {ECO:0000256|ARBA:ARBA00022852}; KW Glycosidase {ECO:0000256|RuleBase:RU003788}; KW Host cell inner membrane {ECO:0000256|ARBA:ARBA00022445}; KW Host cell lysis by virus {ECO:0000256|ARBA:ARBA00023142}; KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003788}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}; KW Viral release from host cell {ECO:0000256|ARBA:ARBA00022612}. SQ SEQUENCE 162 AA; 18262 MW; 353AC2665FFB22BC CRC64; MSLKNNVIGA SIGAALTLTP TLLERIEGIE YEVYYDIAGV PTVCSGITGP DVIPGKKYTK RECDALLIKH IGVAQRYVDK KVKVDIPVTM RASLYSFTFN VGTGAFGSST MLKLINQSKH KEACNQLWRW VYYYNPKTKK REVSRGLKNR RAEEYAYCVK EL //