ID A0A1J0GRX5_9CAUD Unreviewed; 162 AA. AC A0A1J0GRX5; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 17-JUN-2020, entry version 12. DE RecName: Full=Endolysin {ECO:0000256|HAMAP-Rule:MF_04110}; DE EC=3.2.1.17 {ECO:0000256|HAMAP-Rule:MF_04110}; DE AltName: Full=Lysis protein {ECO:0000256|HAMAP-Rule:MF_04110}; DE AltName: Full=Lysozyme {ECO:0000256|HAMAP-Rule:MF_04110}; DE AltName: Full=Muramidase {ECO:0000256|HAMAP-Rule:MF_04110}; GN ORFNames=SH6_0066 {ECO:0000313|EMBL:APC44908.1}; OS Shigella phage SH6. OC Viruses; Caudovirales; Siphoviridae; Tunavirinae; Tunavirus; OC unclassified Tunavirus. 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 -!- FUNCTION: Endolysin with lysozyme activity that degrades host CC peptidoglycans and participates with the holin and spanin proteins in CC the sequential events which lead to the programmed host cell lysis CC releasing the mature viral particles. Once the holin has permeabilized CC the host cell membrane, the endolysin can reach the periplasm and break CC down the peptidoglycan layer. {ECO:0000256|HAMAP-Rule:MF_04110}. 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|HAMAP-Rule:MF_04110}; CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04110}. CC Note=The endolysin is cytoplasmic, but can reach the periplasmic space CC with the help of the holins which disrupt the host cell membrane. CC {ECO:0000256|HAMAP-Rule:MF_04110}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family. CC {ECO:0000256|HAMAP-Rule:MF_04110}. 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:0003796; F:lysozyme activity; IEA:InterPro. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro. DR GO; GO:0019835; P:cytolysis; IEA:InterPro. DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro. DR GO; GO:0019076; P:viral release from host cell; IEA:InterPro. DR HAMAP; MF_04110; ENDOLYSIN_T4; 1. DR InterPro; IPR034690; Endolysin_T4_type. DR InterPro; IPR002196; Glyco_hydro_24. DR InterPro; IPR023346; Lysozyme-like_dom_sf. DR Pfam; PF00959; Phage_lysozyme; 1. DR SUPFAM; SSF53955; SSF53955; 1. PE 3: Inferred from homology; KW Antimicrobial {ECO:0000256|HAMAP-Rule:MF_04110}; KW Bacteriolytic enzyme {ECO:0000256|HAMAP-Rule:MF_04110}; KW Cytolysis {ECO:0000256|HAMAP-Rule:MF_04110}; KW Glycosidase {ECO:0000256|HAMAP-Rule:MF_04110}; KW Host cell lysis by virus {ECO:0000256|HAMAP-Rule:MF_04110}; KW Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04110}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04110}; KW Viral release from host cell {ECO:0000256|HAMAP-Rule:MF_04110}. FT ACT_SITE 27 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04110" FT ACT_SITE 36 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04110" 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 //