ID   ENLYS_LAMBD             Reviewed;         158 AA.
AC   P03706;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   08-NOV-2023, entry version 128.
DE   RecName: Full=Endolysin {ECO:0000255|HAMAP-Rule:MF_04109, ECO:0000303|Ref.2};
DE            EC=4.2.2.n2 {ECO:0000255|HAMAP-Rule:MF_04109, ECO:0000269|PubMed:10556513, ECO:0000269|PubMed:6448076};
DE   AltName: Full=Lysis protein {ECO:0000255|HAMAP-Rule:MF_04109};
DE   AltName: Full=Lysozyme {ECO:0000255|HAMAP-Rule:MF_04109, ECO:0000303|PubMed:10556513, ECO:0000303|PubMed:4889461};
DE   AltName: Full=Transglycosylase {ECO:0000255|HAMAP-Rule:MF_04109, ECO:0000303|PubMed:6460914};
GN   Name=R;
OS   Escherichia phage lambda (Bacteriophage lambda).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Lambdavirus; Lambdavirus lambda.
OX   NCBI_TaxID=2681611;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6221115; DOI=10.1016/0022-2836(82)90546-0;
RA   Sanger F., Coulson A.R., Hong G.F., Hill D.F., Petersen G.B.;
RT   "Nucleotide sequence of bacteriophage lambda DNA.";
RL   J. Mol. Biol. 162:729-773(1982).
RN   [2]
RP   PROTEIN SEQUENCE.
RA   Imada M., Tsugita A.;
RT   "Amino-acid sequence of lambda phage endolysin.";
RL   Nature New Biol. 233:230-231(1971).
RN   [3]
RP   CHARACTERIZATION, AND SUBUNIT.
RX   PubMed=4889461; DOI=10.1016/s0021-9258(18)94354-1;
RA   Black L.W., Hogness D.S.;
RT   "The lysozyme of bacteriophage lambda. I. Purification and molecular
RT   weight.";
RL   J. Biol. Chem. 244:1968-1975(1969).
RN   [4]
RP   CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=6448076; DOI=10.1016/0005-2744(80)90515-x;
RA   Bienkowska-Szewczyk K., Taylor A.;
RT   "Murein transglycosylase from phage lambda lysate. Purification and
RT   properties.";
RL   Biochim. Biophys. Acta 615:489-496(1980).
RN   [5]
RP   IDENTIFICATION.
RX   PubMed=6460914; DOI=10.1007/bf00271205;
RA   Bienkowska-Szewczyk K., Lipinska B., Taylor A.;
RT   "The R gene product of bacteriophage lambda is the murein
RT   transglycosylase.";
RL   Mol. Gen. Genet. 184:111-114(1981).
RN   [6]
RP   MUTAGENESIS OF HIS-31; HIS-48 AND HIS-137, AND CATALYTIC ACTIVITY.
RX   PubMed=10556513; DOI=10.1016/s0014-5793(99)01395-2;
RA   Evrard C., Fastrez J., Soumillion P.;
RT   "Histidine modification and mutagenesis point to the involvement of a large
RT   conformational change in the mechanism of action of phage lambda
RT   lysozyme.";
RL   FEBS Lett. 460:442-446(1999).
RN   [7]
RP   REVIEW.
RX   PubMed=24113139; DOI=10.1016/j.mib.2013.08.008;
RA   Young R.;
RT   "Phage lysis: do we have the hole story yet?";
RL   Curr. Opin. Microbiol. 16:790-797(2013).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND ACTIVE SITE.
RX   PubMed=9514719; DOI=10.1006/jmbi.1997.1499;
RA   Evrard C., Fastrez J., Declercq J.-P.;
RT   "Crystal structure of the lysozyme from bacteriophage lambda and its
RT   relationship with V and C-type lysozymes.";
RL   J. Mol. Biol. 276:151-164(1998).
RN   [9]
RP   STRUCTURE BY NMR.
RX   PubMed=20300891; DOI=10.1007/s12104-010-9219-8;
RA   Di Paolo A., Duval V., Matagne A., Redfield C.;
RT   "Backbone 1H, 13C, and 15N resonance assignments for lysozyme from
RT   bacteriophage lambda.";
RL   Biomol. NMR. Assign. 4:111-114(2010).
CC   -!- FUNCTION: Endolysin with transglycosylase 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:0000255|HAMAP-Rule:MF_04109,
CC       ECO:0000305|PubMed:10556513, ECO:0000305|PubMed:24113139}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endolytic cleavage of the (1->4)-beta-glycosidic linkage
CC         between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC         (GlcNAc) residues in peptidoglycan with concomitant formation of a
CC         1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_04109,
CC         ECO:0000269|PubMed:10556513, ECO:0000269|PubMed:6448076};
CC   -!- ACTIVITY REGULATION: Inactivated by zinc. {ECO:0000269|PubMed:6448076}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.6. {ECO:0000269|PubMed:6448076};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_04109,
CC       ECO:0000269|PubMed:4889461}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04109}.
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:0000255|HAMAP-Rule:MF_04109, ECO:0000305|PubMed:24113139}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC       {ECO:0000255|HAMAP-Rule:MF_04109}.
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DR   EMBL; J02459; AAA96598.1; -; Genomic_DNA.
DR   PIR; B04333; EYBPL.
DR   RefSeq; NP_040645.1; NC_001416.1.
DR   PDB; 1AM7; X-ray; 2.30 A; A/B/C=1-158.
DR   PDB; 1D9U; X-ray; 2.60 A; A/B=1-154.
DR   PDB; 3D3D; X-ray; 2.60 A; A/B=1-154.
DR   PDBsum; 1AM7; -.
DR   PDBsum; 1D9U; -.
DR   PDBsum; 3D3D; -.
DR   BMRB; P03706; -.
DR   SMR; P03706; -.
DR   IntAct; P03706; 1.
DR   DrugBank; DB04206; 7-Aza-L-tryptophan.
DR   CAZy; GH104; Glycoside Hydrolase Family 104.
DR   GeneID; 2703480; -.
DR   KEGG; vg:2703480; -.
DR   OrthoDB; 10116at10239; -.
DR   EvolutionaryTrace; P03706; -.
DR   Proteomes; UP000001711; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003796; F:lysozyme activity; IDA:UniProtKB.
DR   GO; GO:0008933; F:lytic transglycosylase activity; IDA:UniProtKB.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
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; IDA:UniProtKB.
DR   CDD; cd00736; lambda_lys-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   HAMAP; MF_04109; ENDOLYSIN_LAMBDA; 1.
DR   InterPro; IPR034691; Endolysin_lambda_type.
DR   InterPro; IPR002196; Glyco_hydro_24.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   Pfam; PF00959; Phage_lysozyme; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antimicrobial; Bacteriolytic enzyme; Cytolysis;
KW   Direct protein sequencing; Host cell lysis by virus; Host cytoplasm; Lyase;
KW   Reference proteome; Viral release from host cell.
FT   CHAIN           1..158
FT                   /note="Endolysin"
FT                   /id="PRO_0000218108"
FT   ACT_SITE        19
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04109,
FT                   ECO:0000269|PubMed:9514719"
FT   MUTAGEN         31
FT                   /note="H->D: No effect on lytic activity."
FT                   /evidence="ECO:0000269|PubMed:10556513"
FT   MUTAGEN         31
FT                   /note="H->N: No effect on lytic activity; when associated
FT                   with N-137."
FT                   /evidence="ECO:0000269|PubMed:10556513"
FT   MUTAGEN         48
FT                   /note="H->N: 97% loss of lytic activity."
FT                   /evidence="ECO:0000269|PubMed:10556513"
FT   MUTAGEN         137
FT                   /note="H->N: No effect on lytic activity; when associated
FT                   with N-31."
FT                   /evidence="ECO:0000269|PubMed:10556513"
FT   CONFLICT        74
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           6..16
FT                   /evidence="ECO:0007829|PDB:1AM7"
FT   STRAND          20..26
FT                   /evidence="ECO:0007829|PDB:1AM7"
FT   TURN            31..34
FT                   /evidence="ECO:0007829|PDB:1AM7"
FT   STRAND          53..56
FT                   /evidence="ECO:0007829|PDB:1AM7"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:1AM7"
FT   TURN            65..68
FT                   /evidence="ECO:0007829|PDB:1AM7"
FT   HELIX           76..81
FT                   /evidence="ECO:0007829|PDB:1AM7"
FT   HELIX           88..101
FT                   /evidence="ECO:0007829|PDB:1AM7"
FT   HELIX           105..110
FT                   /evidence="ECO:0007829|PDB:1AM7"
FT   HELIX           113..120
FT                   /evidence="ECO:0007829|PDB:1AM7"
FT   TURN            121..123
FT                   /evidence="ECO:0007829|PDB:1AM7"
FT   STRAND          132..134
FT                   /evidence="ECO:0007829|PDB:1D9U"
FT   HELIX           135..148
FT                   /evidence="ECO:0007829|PDB:1AM7"
SQ   SEQUENCE   158 AA;  17825 MW;  94F8E9A512EAA03E CRC64;
     MVEINNQRKA FLDMLAWSEG TDNGRQKTRN HGYDVIVGGE LFTDYSDHPR KLVTLNPKLK
     STGAGRYQLL SRWWDAYRKQ LGLKDFSPKS QDAVALQQIK ERGALPMIDR GDIRQAIDRC
     SNIWASLPGA GYGQFEHKAD SLIAKFKEAG GTVREIDV
//