ID   ENLYS_BPT7              Reviewed;         151 AA.
AC   P00806; Q38567;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Endolysin {ECO:0000255|HAMAP-Rule:MF_04111};
DE            EC=3.5.1.28 {ECO:0000255|HAMAP-Rule:MF_04111, ECO:0000269|PubMed:8171031};
DE   AltName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000255|HAMAP-Rule:MF_04111};
DE   AltName: Full=T7 endolysin {ECO:0000305};
GN   OrderedLocusNames=3.5;
OS   Escherichia phage T7 (Bacteriophage T7).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Autographiviridae; Studiervirinae; Teseptimavirus; Teseptimavirus T7.
OX   NCBI_TaxID=10760;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6864790; DOI=10.1016/s0022-2836(83)80282-4;
RA   Dunn J.J., Studier F.W.;
RT   "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of
RT   T7 genetic elements.";
RL   J. Mol. Biol. 166:477-535(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7310871; DOI=10.1016/0022-2836(81)90178-9;
RA   Dunn J.J., Studier F.W.;
RT   "Nucleotide sequence from the genetic left end of bacteriophage T7 DNA to
RT   the beginning of gene 4.";
RL   J. Mol. Biol. 148:303-330(1981).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7801634;
RA   Huang W., Cui X., Tian Y., Lin M., Peng X.;
RT   "Cloning of T7 lysozyme gene and construction of the vector for transgenic
RT   plants resistant to bacterial infection.";
RL   Wei Sheng Wu Xue Bao 34:261-265(1994).
RN   [4]
RP   FUNCTION.
RX   PubMed=3568126; DOI=10.1016/0092-8674(87)90563-0;
RA   Moffatt B.A., Studier F.W.;
RT   "T7 lysozyme inhibits transcription by T7 RNA polymerase.";
RL   Cell 49:221-227(1987).
RN   [5]
RP   FUNCTION.
RX   PubMed=9192997; DOI=10.1006/jmbi.1997.1016;
RA   Zhang X., Studier F.W.;
RT   "Mechanism of inhibition of bacteriophage T7 RNA polymerase by T7
RT   lysozyme.";
RL   J. Mol. Biol. 269:10-27(1997).
RN   [6]
RP   FUNCTION.
RX   PubMed=14764584; DOI=10.1074/jbc.m400139200;
RA   Stano N.M., Patel S.S.;
RT   "T7 lysozyme represses T7 RNA polymerase transcription by destabilizing the
RT   open complex during initiation.";
RL   J. Biol. Chem. 279:16136-16143(2004).
RN   [7]
RP   FUNCTION.
RX   PubMed=15223315; DOI=10.1016/j.jmb.2004.05.006;
RA   Zhang X., Studier F.W.;
RT   "Multiple roles of T7 RNA polymerase and T7 lysozyme during bacteriophage
RT   T7 infection.";
RL   J. Mol. Biol. 340:707-730(2004).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SEQUENCE REVISION TO 119, CATALYTIC
RP   ACTIVITY, INTERACTION WITH THE VIRAL RNA POLYMERASE, AND MUTAGENESIS OF
RP   HIS-18; TYR-47 AND LYS-129.
RX   PubMed=8171031; DOI=10.1073/pnas.91.9.4034;
RA   Cheng X., Zhang X., Pflugrath J.W., Studier F.W.;
RT   "The structure of bacteriophage T7 lysozyme, a zinc amidase and an
RT   inhibitor of T7 RNA polymerase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:4034-4038(1994).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH POLYMERASE, AND
RP   INTERACTION WITH THE VIRAL RNA POLYMERASE.
RX   PubMed=9670025; DOI=10.1093/emboj/17.14.4101;
RA   Jeruzalmi D., Steitz T.A.;
RT   "Structure of T7 RNA polymerase complexed to the transcriptional inhibitor
RT   T7 lysozyme.";
RL   EMBO J. 17:4101-4113(1998).
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       ECO:0000269|PubMed:14764584, ECO:0000269|PubMed:15223315,
CC       ECO:0000269|PubMed:9192997}.
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, ECO:0000305|PubMed:15223315}.
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         ECO:0000269|PubMed:8171031};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_04111, ECO:0000269|PubMed:8171031};
CC       Note=Zn(2+) is required for amidase activity. {ECO:0000255|HAMAP-
CC       Rule:MF_04111, ECO:0000269|PubMed:8171031};
CC   -!- ACTIVITY REGULATION: Binding to the viral RNA polymerase inhibits
CC       amidase activity. {ECO:0000255|HAMAP-Rule:MF_04111,
CC       ECO:0000269|PubMed:8171031}.
CC   -!- SUBUNIT: Interacts with the viral RNA polymerase. {ECO:0000255|HAMAP-
CC       Rule:MF_04111, ECO:0000269|PubMed:8171031, ECO:0000269|PubMed:9670025}.
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; V01146; CAA24403.1; -; Genomic_DNA.
DR   EMBL; V01127; CAA24346.1; -; Genomic_DNA.
DR   EMBL; S75616; AAB32819.1; -; Genomic_DNA.
DR   PIR; C94615; MUBPA7.
DR   RefSeq; NP_041973.1; NC_001604.1.
DR   PDB; 1ARO; X-ray; 2.80 A; L=1-151.
DR   PDB; 1LBA; X-ray; 2.20 A; A=7-151.
DR   PDBsum; 1ARO; -.
DR   PDBsum; 1LBA; -.
DR   SMR; P00806; -.
DR   DIP; DIP-6090N; -.
DR   IntAct; P00806; 1.
DR   MINT; P00806; -.
DR   GeneID; 1261077; -.
DR   KEGG; vg:1261077; -.
DR   OrthoDB; 13080at10239; -.
DR   EvolutionaryTrace; P00806; -.
DR   Proteomes; UP000000840; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB.
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; cd06583; PGRP; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 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; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1.
DR   PANTHER; PTHR11022:SF41; PEPTIDOGLYCAN-RECOGNITION PROTEIN SC1A-RELATED; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SMART; SM00701; PGRP; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antimicrobial; Bacteriolytic enzyme; Cytolysis;
KW   Host cell lysis by virus; Host cytoplasm; Hydrolase; Late protein;
KW   Metal-binding; Reference proteome; Viral release from host cell; Zinc.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT   CHAIN           2..151
FT                   /note="Endolysin"
FT                   /id="PRO_0000164410"
FT   DOMAIN          10..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                   ECO:0000269|PubMed:8171031, ECO:0007744|PDB:1LBA"
FT   BINDING         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04111,
FT                   ECO:0000269|PubMed:8171031, ECO:0007744|PDB:1LBA"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04111,
FT                   ECO:0000269|PubMed:8171031, ECO:0007744|PDB:1LBA"
FT   SITE            47
FT                   /note="Essential for amidase activity and zinc hydrate
FT                   coordination"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04111,
FT                   ECO:0000269|PubMed:8171031"
FT   SITE            129
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000269|PubMed:8171031,
FT                   ECO:0007744|PDB:1LBA"
FT   MUTAGEN         18
FT                   /note="H->N,Q,R: Complete loss of amidase activity."
FT                   /evidence="ECO:0000269|PubMed:8171031"
FT   MUTAGEN         47
FT                   /note="Y->D,F,L: Complete loss of amidase activity."
FT                   /evidence="ECO:0000269|PubMed:8171031"
FT   MUTAGEN         129
FT                   /note="K->I,M,Q,W,Y: Complete loss of amidase activity."
FT                   /evidence="ECO:0000269|PubMed:8171031"
FT   CONFLICT        90
FT                   /note="G -> V (in Ref. 3; AAB32819)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        119
FT                   /note="V -> G (in Ref. 1, 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   STRAND          14..19
FT                   /evidence="ECO:0007829|PDB:1LBA"
FT   HELIX           30..39
FT                   /evidence="ECO:0007829|PDB:1LBA"
FT   STRAND          48..51
FT                   /evidence="ECO:0007829|PDB:1LBA"
FT   STRAND          53..55
FT                   /evidence="ECO:0007829|PDB:1ARO"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:1LBA"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:1LBA"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:1LBA"
FT   STRAND          77..83
FT                   /evidence="ECO:0007829|PDB:1LBA"
FT   STRAND          90..92
FT                   /evidence="ECO:0007829|PDB:1ARO"
FT   HELIX           98..114
FT                   /evidence="ECO:0007829|PDB:1LBA"
FT   TURN            115..117
FT                   /evidence="ECO:0007829|PDB:1ARO"
FT   STRAND          119..122
FT                   /evidence="ECO:0007829|PDB:1LBA"
FT   HELIX           123..125
FT                   /evidence="ECO:0007829|PDB:1LBA"
FT   STRAND          127..129
FT                   /evidence="ECO:0007829|PDB:1LBA"
FT   HELIX           136..142
FT                   /evidence="ECO:0007829|PDB:1LBA"
SQ   SEQUENCE   151 AA;  16979 MW;  C36BC018754A4146 CRC64;
     MARVQFKQRE STDAIFVHCS ATKPSQNVGV REIRQWHKEQ GWLDVGYHFI IKRDGTVEAG
     RDEMAVGSHA KGYNHNSIGV CLVGGIDDKG KFDANFTPAQ MQSLRSLLVT LLAKYEGAVL
     RAHHEVAPKA CPSFDLKRWW EKNELVTSDR G
//