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}.
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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
//