ENLYS_BPT7
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 03-AUG-2022, entry version 139.
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 Caudovirales; Autographiviridae; Studiervirinae; Teseptimavirus.
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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04111,
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 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: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; 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; -; 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 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
