ID   A0A1J0GRX5_9CAUD        Unreviewed;       162 AA.
AC   A0A1J0GRX5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   12-AUG-2020, entry version 13.
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; 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   -!- 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|ARBA:ARBA00000632,
CC         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|ARBA:ARBA00006786, ECO:0000256|HAMAP-Rule:MF_04110}.
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DR   EMBL; KX828710; APC44908.1; -; Genomic_DNA.
DR   Proteomes; UP000224004; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR   GO; GO:0044659; P:viral release from host cell by cytolysis; IEA:UniProtKB-UniRule.
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|ARBA:ARBA00022852, ECO:0000256|HAMAP-Rule:MF_04110};
KW   Glycosidase {ECO:0000256|HAMAP-Rule:MF_04110};
KW   Host cell lysis by virus {ECO:0000256|ARBA:ARBA00023142, ECO:0000256|HAMAP-
KW   Rule:MF_04110}; Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04110};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_04110};
KW   Viral release from host cell {ECO:0000256|ARBA:ARBA00022612,
KW   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
//