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Endolysin (EC 3.5.1.28) (N-acetylmuramoyl-L-alanine amidase)

 ENLYS_BPT7              Reviewed;         151 AA.
P00806; Q38567;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
05-DEC-2018, entry version 124.
RecName: Full=Endolysin {ECO:0000255|HAMAP-Rule:MF_04111};
EC=3.5.1.28 {ECO:0000255|HAMAP-Rule:MF_04111, ECO:0000269|PubMed:8171031};
AltName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000255|HAMAP-Rule:MF_04111};
OrderedLocusNames=3.5;
Enterobacteria phage T7 (Bacteriophage T7).
Viruses; dsDNA viruses, no RNA stage; Caudovirales; Podoviridae;
Autographivirinae; T7virus.
NCBI_TaxID=10760;
NCBI_TaxID=562; Escherichia coli.
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=6864790; DOI=10.1016/S0022-2836(83)80282-4;
Dunn J.J., Studier F.W.;
"Complete nucleotide sequence of bacteriophage T7 DNA and the
locations of T7 genetic elements.";
J. Mol. Biol. 166:477-535(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7310871; DOI=10.1016/0022-2836(81)90178-9;
Dunn J.J., Studier F.W.;
"Nucleotide sequence from the genetic left end of bacteriophage T7 DNA
to the beginning of gene 4.";
J. Mol. Biol. 148:303-330(1981).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7801634;
Huang W., Cui X., Tian Y., Lin M., Peng X.;
"Cloning of T7 lysozyme gene and construction of the vector for
transgenic plants resistant to bacterial infection.";
Wei Sheng Wu Xue Bao 34:261-265(1994).
[4]
FUNCTION.
PubMed=3568126; DOI=10.1016/0092-8674(87)90563-0;
Moffatt B.A., Studier F.W.;
"T7 lysozyme inhibits transcription by T7 RNA polymerase.";
Cell 49:221-227(1987).
[5]
FUNCTION.
PubMed=9192997; DOI=10.1006/jmbi.1997.1016;
Zhang X., Studier F.W.;
"Mechanism of inhibition of bacteriophage T7 RNA polymerase by T7
lysozyme.";
J. Mol. Biol. 269:10-27(1997).
[6]
FUNCTION.
PubMed=14764584; DOI=10.1074/jbc.M400139200;
Stano N.M., Patel S.S.;
"T7 lysozyme represses T7 RNA polymerase transcription by
destabilizing the open complex during initiation.";
J. Biol. Chem. 279:16136-16143(2004).
[7]
FUNCTION.
PubMed=15223315; DOI=10.1016/j.jmb.2004.05.006;
Zhang X., Studier F.W.;
"Multiple roles of T7 RNA polymerase and T7 lysozyme during
bacteriophage T7 infection.";
J. Mol. Biol. 340:707-730(2004).
[8]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SEQUENCE REVISION TO 119,
CATALYTIC ACTIVITY, INTERACTION WITH THE VIRAL RNA POLYMERASE, AND
MUTAGENESIS OF HIS-18; TYR-47 AND LYS-129.
PubMed=8171031; DOI=10.1073/pnas.91.9.4034;
Cheng X., Zhang X., Pflugrath J.W., Studier F.W.;
"The structure of bacteriophage T7 lysozyme, a zinc amidase and an
inhibitor of T7 RNA polymerase.";
Proc. Natl. Acad. Sci. U.S.A. 91:4034-4038(1994).
[9]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH POLYMERASE, AND
INTERACTION WITH THE VIRAL RNA POLYMERASE.
PubMed=9670025; DOI=10.1093/emboj/17.14.4101;
Jeruzalmi D., Steitz T.A.;
"Structure of T7 RNA polymerase complexed to the transcriptional
inhibitor T7 lysozyme.";
EMBO J. 17:4101-4113(1998).
-!- FUNCTION: Plays an important role in the switch between viral
transcription and genome replication. Once produced in sufficient
amount, interacts with and inhibits the viral RNA polymerase that
becomes unable to produce additional late transcripts. This
lysozyme-polymerase complex in turn plays an active role in viral
genome replication and packaging. {ECO:0000255|HAMAP-
Rule:MF_04111, ECO:0000269|PubMed:14764584,
ECO:0000269|PubMed:15223315, ECO:0000269|PubMed:9192997}.
-!- FUNCTION: Endolysin with amidase activity that degrades host
peptidoglycans and participates with the holin and spanin proteins
in the sequential events which lead to the programmed host cell
lysis releasing the mature viral particles. Once the holin has
permeabilized the host cell membrane, the endolysin can reach the
periplasm and breaking down the peptidoglycan layer.
{ECO:0000255|HAMAP-Rule:MF_04111, ECO:0000305|PubMed:15223315}.
-!- CATALYTIC ACTIVITY:
Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and
L-amino acid residues in certain cell-wall glycopeptides.;
EC=3.5.1.28; Evidence={ECO:0000255|HAMAP-Rule:MF_04111,
ECO:0000269|PubMed:8171031};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_04111,
ECO:0000269|PubMed:8171031};
Note=Zn(2+) is required for amidase activity. {ECO:0000255|HAMAP-
Rule:MF_04111, ECO:0000269|PubMed:8171031};
-!- ACTIVITY REGULATION: Binding to the viral RNA polymerase inhibits
amidase activity. {ECO:0000255|HAMAP-Rule:MF_04111,
ECO:0000269|PubMed:8171031}.
-!- SUBUNIT: Interacts with the viral RNA polymerase.
{ECO:0000255|HAMAP-Rule:MF_04111, ECO:0000269|PubMed:8171031,
ECO:0000269|PubMed:9670025}.
-!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-
Rule:MF_04111}. Note=The endolysin is cytoplasmic, but can reach
the periplasmic space with the help of the holins which disrupt
the host cell membrane. {ECO:0000255|HAMAP-Rule:MF_04111}.
-!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2
family. {ECO:0000255|HAMAP-Rule:MF_04111}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; V01146; CAA24403.1; -; Genomic_DNA.
EMBL; V01127; CAA24346.1; -; Genomic_DNA.
EMBL; S75616; AAB32819.1; -; Genomic_DNA.
PIR; C94615; MUBPA7.
RefSeq; NP_041973.1; NC_001604.1.
PDB; 1ARO; X-ray; 2.80 A; L=1-151.
PDB; 1LBA; X-ray; 2.20 A; A=7-151.
PDBsum; 1ARO; -.
PDBsum; 1LBA; -.
ProteinModelPortal; P00806; -.
SMR; P00806; -.
DIP; DIP-6090N; -.
IntAct; P00806; 1.
MINT; P00806; -.
GeneID; 1261077; -.
KEGG; vg:1261077; -.
OrthoDB; VOG090000Z1; -.
EvolutionaryTrace; P00806; -.
Proteomes; UP000000840; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0044659; P:cytolysis by virus of host cell; IDA:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
GO; GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB.
GO; GO:0009253; P:peptidoglycan catabolic process; IEA:UniProtKB-UniRule.
CDD; cd06583; PGRP; 1.
Gene3D; 3.40.80.10; -; 1.
HAMAP; MF_04111; ENDOLYSIN_T7; 1.
InterPro; IPR036505; Amidase/PGRP_sf.
InterPro; IPR002502; Amidase_domain.
InterPro; IPR034689; Endolysin_T7_type.
InterPro; IPR015510; PGRP.
InterPro; IPR006619; PGRP_domain_met/bac.
PANTHER; PTHR11022; PTHR11022; 1.
Pfam; PF01510; Amidase_2; 1.
SMART; SM00644; Ami_2; 1.
SMART; SM00701; PGRP; 1.
SUPFAM; SSF55846; SSF55846; 1.
1: Evidence at protein level;
3D-structure; Antimicrobial; Bacteriolytic enzyme; Complete proteome;
Cytolysis; Host cell lysis by virus; Host cytoplasm; Hydrolase;
Late protein; Metal-binding; Reference proteome;
Viral release from host cell; Zinc.
INIT_MET 1 1 Removed; by host.
CHAIN 2 151 Endolysin.
/FTId=PRO_0000164410.
DOMAIN 10 132 N-acetylmuramoyl-L-alanine amidase.
{ECO:0000255}.
METAL 18 18 Zinc. {ECO:0000244|PDB:1LBA,
ECO:0000255|HAMAP-Rule:MF_04111,
ECO:0000269|PubMed:8171031}.
METAL 123 123 Zinc. {ECO:0000244|PDB:1LBA,
ECO:0000255|HAMAP-Rule:MF_04111,
ECO:0000269|PubMed:8171031}.
METAL 131 131 Zinc. {ECO:0000244|PDB:1LBA,
ECO:0000255|HAMAP-Rule:MF_04111,
ECO:0000269|PubMed:8171031}.
SITE 47 47 Essential for amidase activity and zinc
hydrate coordination. {ECO:0000255|HAMAP-
Rule:MF_04111,
ECO:0000269|PubMed:8171031}.
SITE 129 129 Important for catalytic activity.
{ECO:0000244|PDB:1LBA,
ECO:0000269|PubMed:8171031}.
MUTAGEN 18 18 H->N,Q,R: Complete loss of amidase
activity. {ECO:0000269|PubMed:8171031}.
MUTAGEN 47 47 Y->D,F,L: Complete loss of amidase
activity. {ECO:0000269|PubMed:8171031}.
MUTAGEN 129 129 K->I,M,Q,W,Y: Complete loss of amidase
activity. {ECO:0000269|PubMed:8171031}.
CONFLICT 90 90 G -> V (in Ref. 3; AAB32819).
{ECO:0000305}.
CONFLICT 119 119 V -> G (in Ref. 1, 2 and 3).
{ECO:0000305}.
STRAND 14 19 {ECO:0000244|PDB:1LBA}.
HELIX 30 39 {ECO:0000244|PDB:1LBA}.
STRAND 48 51 {ECO:0000244|PDB:1LBA}.
STRAND 53 55 {ECO:0000244|PDB:1ARO}.
STRAND 57 59 {ECO:0000244|PDB:1LBA}.
STRAND 68 70 {ECO:0000244|PDB:1LBA}.
HELIX 74 76 {ECO:0000244|PDB:1LBA}.
STRAND 77 83 {ECO:0000244|PDB:1LBA}.
STRAND 90 92 {ECO:0000244|PDB:1ARO}.
HELIX 98 114 {ECO:0000244|PDB:1LBA}.
TURN 115 117 {ECO:0000244|PDB:1ARO}.
STRAND 119 122 {ECO:0000244|PDB:1LBA}.
HELIX 123 125 {ECO:0000244|PDB:1LBA}.
STRAND 127 129 {ECO:0000244|PDB:1LBA}.
HELIX 136 142 {ECO:0000244|PDB:1LBA}.
SEQUENCE 151 AA; 16979 MW; C36BC018754A4146 CRC64;
MARVQFKQRE STDAIFVHCS ATKPSQNVGV REIRQWHKEQ GWLDVGYHFI IKRDGTVEAG
RDEMAVGSHA KGYNHNSIGV CLVGGIDDKG KFDANFTPAQ MQSLRSLLVT LLAKYEGAVL
RAHHEVAPKA CPSFDLKRWW EKNELVTSDR G


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