ENLYS_BPT3
ID ENLYS_BPT3 Reviewed; 151 AA.
AC P20331;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Endolysin {ECO:0000255|HAMAP-Rule:MF_04111};
DE EC=3.5.1.28 {ECO:0000255|HAMAP-Rule:MF_04111};
DE AltName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000255|HAMAP-Rule:MF_04111};
DE AltName: Full=T3 lysozyme;
GN Name=3.5;
OS Enterobacteria phage T3 (Bacteriophage T3).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Autographiviridae; Studiervirinae; Teetrevirus;
OC Escherichia virus T3.
OX NCBI_TaxID=10759;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Luria;
RX PubMed=2614843; DOI=10.1016/0022-2836(89)90102-2;
RA Beck P.J., Gonzalez S., Ward C.L., Molineux I.J.;
RT "Sequence of bacteriophage T3 DNA from gene 2.5 through gene 9.";
RL J. Mol. Biol. 210:687-701(1989).
CC -!- FUNCTION: Plays an important role in the switch between viral
CC transcription and genome replication. Once produced in sufficient
CC amount, interacts with and inhibits the viral RNA polymerase that
CC becomes unable to produce additional late transcripts. This lysozyme-
CC polymerase complex in turn plays an active role in viral genome
CC replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04111}.
CC -!- FUNCTION: Endolysin with amidase 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
CC breaking down the peptidoglycan layer. {ECO:0000255|HAMAP-
CC Rule:MF_04111}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04111};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04111};
CC Note=Zn(2+) is required for amidase activity. {ECO:0000255|HAMAP-
CC Rule:MF_04111};
CC -!- ACTIVITY REGULATION: Binding to the viral RNA polymerase inhibits
CC amidase activity. {ECO:0000255|HAMAP-Rule:MF_04111}.
CC -!- SUBUNIT: Interacts with the viral RNA polymerase. {ECO:0000255|HAMAP-
CC Rule:MF_04111}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04111}.
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_04111}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_04111}.
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DR EMBL; X17255; CAA35133.1; -; Genomic_DNA.
DR PIR; S07506; S07506.
DR RefSeq; NP_523313.1; NC_003298.1.
DR SMR; P20331; -.
DR GeneID; 927411; -.
DR KEGG; vg:927411; -.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; 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:0032897; P:negative regulation of viral transcription; IEA:InterPro.
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 CDD; cd06583; PGRP; 1.
DR Gene3D; 3.40.80.10; -; 1.
DR HAMAP; MF_04111; ENDOLYSIN_T7; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR034689; Endolysin_T7_type.
DR InterPro; IPR015510; PGRP.
DR InterPro; IPR006619; PGRP_domain_met/bac.
DR PANTHER; PTHR11022; PTHR11022; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF55846; SSF55846; 1.
PE 3: Inferred from homology;
KW Antimicrobial; Bacteriolytic enzyme; Cytolysis; Host cell lysis by virus;
KW Host cytoplasm; Hydrolase; Late protein; Metal-binding;
KW Viral release from host cell; Zinc.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..151
FT /note="Endolysin"
FT /id="PRO_0000164409"
FT DOMAIN 11..132
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04111"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04111"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04111"
FT SITE 47
FT /note="Essential for amidase activity and zinc hydrate
FT coordination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04111"
SQ SEQUENCE 151 AA; 16874 MW; 2C0880FFC920DE9E CRC64;
MAKVQFKPRA TTEAIFVHCS ATKPSQNVGV REIRQWHKEQ GWLDVGYHFI IKRDGTVEAG
RDELAVGSHA KGYNHNSIGV CLVGGIDDKG KFDANFTPAQ MQSLRSLLVT LLAKYEGSVL
RAHHDVAPKA CPSFDLKRWW EKNELVTSDR G
