ENLYS_LAMBD
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 25-MAY-2022, entry version 123.
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 Caudovirales; Siphoviridae; Lambdavirus.
OX NCBI_TaxID=10710;
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 EvolutionaryTrace; P03706; -.
DR Proteomes; UP000001711; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
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: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; IDA:UniProtKB.
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; SSF53955; 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
