ENLYS_BPT5
ID ENLYS_BPT5 Reviewed; 137 AA.
AC Q6QGP7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=L-alanyl-D-glutamate peptidase {ECO:0000303|PubMed:19919545};
DE EC=3.4.24.- {ECO:0000269|PubMed:19919545};
DE AltName: Full=Endolysin;
DE AltName: Full=Lysozyme;
GN Name=lys;
GN OrderedLocusNames=T5.040 {ECO:0000312|EMBL:AAS77087.1},
GN T5p039 {ECO:0000312|EMBL:AAU05192.1};
GN ORFNames=orf10c {ECO:0000312|EMBL:AAS19387.1};
OS Escherichia phage T5 (Enterobacteria phage T5).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Demerecviridae; Markadamsvirinae; Tequintavirus.
OX NCBI_TaxID=2695836;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ksenzenko V.N., Kaliman A.V., Krutilina A.I., Shlyapnikov M.G.;
RT "Bacteriophage T5 complete genome.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 11303-B5;
RX PubMed=15661140; DOI=10.1016/j.virol.2004.10.049;
RA Wang J., Jiang Y., Vincent M., Sun Y., Yu H., Wang J., Bao Q., Kong H.,
RA Hu S.;
RT "Complete genome sequence of bacteriophage T5.";
RL Virology 332:45-65(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=St0 deletion mutant;
RX PubMed=24198424; DOI=10.1128/jvi.02262-13;
RA Zivanovic Y., Confalonieri F., Ponchon L., Lurz R., Chami M., Flayhan A.,
RA Renouard M., Huet A., Decottignies P., Davidson A.R., Breyton C.,
RA Boulanger P.;
RT "Insights into bacteriophage T5 structure from analysis of its
RT morphogenesis genes and protein components.";
RL J. Virol. 88:1162-1174(2014).
RN [4]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND FUNCTION.
RX PubMed=19919545; DOI=10.1111/j.1742-4658.2009.07443.x;
RA Mikoulinskaia G.V., Odinokova I.V., Zimin A.A., Lysanskaya V.Y.,
RA Feofanov S.A., Stepnaya O.A.;
RT "Identification and characterization of the metal ion-dependent L-alanoyl-
RT D-glutamate peptidase encoded by bacteriophage T5.";
RL FEBS J. 276:7329-7342(2009).
RN [5] {ECO:0000312|PDB:2MXZ}
RP STRUCTURE BY NMR, AND COFACTOR.
RX DOI=10.1039/C5RA05993C;
RA Prokhorov D.A., Mikoulinskaia G.V., Molochkov N.V., Uversky V.N.,
RA Kutyshenko V.P.;
RT "High-resolution NMR structure of a Zn2+-containing form of the
RT bacteriophage T5 L-alanyl-D-glutamate peptidase.";
RL RSC Adv. 5:41041-41049(2015).
CC -!- FUNCTION: Endolysin with L-alanyl-D-glutamate peptidase activity that
CC degrades host peptidoglycans and participates with the holin in the
CC 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 by hydrolyzing the link between L-alanine
CC and D-glutamate residues. {ECO:0000305|PubMed:19919545}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|Ref.5};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:19919545};
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC {ECO:0000305|PubMed:15661140}.
CC -!- SIMILARITY: Belongs to the peptidase M15C family. {ECO:0000305}.
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DR EMBL; AY509815; AAS19387.1; -; Genomic_DNA.
DR EMBL; AY543070; AAS77087.1; -; Genomic_DNA.
DR EMBL; AY587007; AAX11973.1; -; Genomic_DNA.
DR EMBL; AY692264; AAU05192.1; -; Genomic_DNA.
DR RefSeq; YP_006868.1; NC_005859.1.
DR PDB; 2MXZ; NMR; -; A=1-137.
DR PDBsum; 2MXZ; -.
DR BMRB; Q6QGP7; -.
DR SMR; Q6QGP7; -.
DR MEROPS; M15.022; -.
DR GeneID; 2777574; -.
DR KEGG; vg:2777574; -.
DR Proteomes; UP000002107; Genome.
DR Proteomes; UP000002141; Genome.
DR Proteomes; UP000002503; Genome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0044659; P:viral release from host cell by cytolysis; IDA:UniProtKB.
DR Gene3D; 3.30.1380.10; -; 1.
DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR InterPro; IPR039561; Peptidase_M15C.
DR Pfam; PF13539; Peptidase_M15_4; 1.
DR SUPFAM; SSF55166; SSF55166; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Bacteriolytic enzyme;
KW Cell wall biogenesis/degradation; Cytolysis; Early protein;
KW Host cell lysis by virus; Hydrolase; Metal-binding; Reference proteome;
KW Viral release from host cell; Zinc.
FT CHAIN 1..137
FT /note="L-alanyl-D-glutamate peptidase"
FT /id="PRO_0000370250"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|Ref.5"
FT HELIX 7..14
FT /evidence="ECO:0007829|PDB:2MXZ"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:2MXZ"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:2MXZ"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2MXZ"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2MXZ"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:2MXZ"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2MXZ"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2MXZ"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:2MXZ"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:2MXZ"
FT HELIX 87..104
FT /evidence="ECO:0007829|PDB:2MXZ"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:2MXZ"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:2MXZ"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:2MXZ"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:2MXZ"
SQ SEQUENCE 137 AA; 15264 MW; 73E88385AB6F690A CRC64;
MSFKFGKNSE KQLATVKPEL QKVARRALEL SPYDFTIVQG IRTVAQSAQN IANGTSFLKD
PSKSKHITGD AIDFAPYING KIDWNDLEAF WAVKKAFEQA GKELGIKLRF GADWNASGDY
HDEIKRGTYD GGHVELV
