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P00806 (LYSO_BPT7) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-acetylmuramoyl-L-alanine amidase

EC=3.5.1.28
Alternative name(s):
T7 lysozyme
Gene names
Ordered Locus Names:3.5
OrganismEnterobacteria phage T7 (Bacteriophage T7) [Reference proteome]
Taxonomic identifier10760 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeAutographivirinaeT7likevirus
Virus hostEscherichia coli [TaxID: 562]

Protein attributes

Sequence length151 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in the switch between viral transcription and T7 genome replication. Once produced in sufficient amount, interacts with and inhibits T7 RNA polymerase that becomes unable to produce additional transcripts. This lysozyme-polymerase complex in turn plays an active role in T7 genome replication and packaging. Ref.4 Ref.5 Ref.6

Catalytic activity

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.

Cofactor

Zinc; required for amidase activity.

Enzyme regulation

Binding of T7 RNA polymerase inhibits amidase activity.

Subunit structure

Interacts with T7 RNA polymerase/Pol.

Sequence similarities

Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.

Ontologies

Keywords
   Developmental stageLate protein
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpeptidoglycan catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionN-acetylmuramoyl-L-alanine amidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

1P005731EBI-1026942,EBI-1026948

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host
Chain2 – 151150N-acetylmuramoyl-L-alanine amidase
PRO_0000164410

Sites

Metal binding181Zinc
Metal binding1231Zinc
Metal binding1311Zinc
Site471Essential for amidase activity and zinc hydrate coordination

Experimental info

Sequence conflict901G → V in AAB32819. Ref.3
Sequence conflict1191V → G Ref.1
Sequence conflict1191V → G Ref.2
Sequence conflict1191V → G Ref.3

Secondary structure

............................ 151
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00806 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: C36BC018754A4146

FASTA15116,979
        10         20         30         40         50         60 
MARVQFKQRE STDAIFVHCS ATKPSQNVGV REIRQWHKEQ GWLDVGYHFI IKRDGTVEAG 

        70         80         90        100        110        120 
RDEMAVGSHA KGYNHNSIGV CLVGGIDDKG KFDANFTPAQ MQSLRSLLVT LLAKYEGAVL 

       130        140        150 
RAHHEVAPKA CPSFDLKRWW EKNELVTSDR G 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements."
Dunn J.J., Studier F.W.
J. Mol. Biol. 166:477-535(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Nucleotide sequence from the genetic left end of bacteriophage T7 DNA to the beginning of gene 4."
Dunn J.J., Studier F.W.
J. Mol. Biol. 148:303-330(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of T7 lysozyme gene and construction of the vector for transgenic plants resistant to bacterial infection."
Huang W., Cui X., Tian Y., Lin M., Peng X.
Wei Sheng Wu Xue Bao 34:261-265(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"T7 lysozyme inhibits transcription by T7 RNA polymerase."
Moffatt B.A., Studier F.W.
Cell 49:221-227(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Mechanism of inhibition of bacteriophage T7 RNA polymerase by T7 lysozyme."
Zhang X., Studier F.W.
J. Mol. Biol. 269:10-27(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"T7 lysozyme represses T7 RNA polymerase transcription by destabilizing the open complex during initiation."
Stano N.M., Patel S.S.
J. Biol. Chem. 279:16136-16143(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase."
Cheng X., Zhang X., Pflugrath J.W., Studier F.W.
Proc. Natl. Acad. Sci. U.S.A. 91:4034-4038(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SEQUENCE REVISION TO 119.
[8]"Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme."
Jeruzalmi D., Steitz T.A.
EMBO J. 17:4101-4113(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH POLYMERASE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01146 Genomic DNA. Translation: CAA24403.1.
V01127 Genomic DNA. Translation: CAA24346.1.
S75616 Genomic DNA. Translation: AAB32819.1.
PIRMUBPA7. C94615.
RefSeqNP_041973.1. NC_001604.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AROX-ray2.80L1-151[»]
1LBAX-ray2.20A7-151[»]
ProteinModelPortalP00806.
SMRP00806. Positions 3-151.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6090N.
IntActP00806. 1 interaction.
MINTMINT-1513681.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1261077.

Phylogenomic databases

ProtClustDBPHA0447.

Family and domain databases

Gene3D3.40.80.10. 1 hit.
InterProIPR002502. Amidase_domain.
IPR015510. PGRP.
[Graphical view]
PANTHERPTHR11022. PTHR11022. 1 hit.
PfamPF01510. Amidase_2. 1 hit.
[Graphical view]
SMARTSM00644. Ami_2. 1 hit.
[Graphical view]
SUPFAMSSF55846. SSF55846. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP00806.

Entry information

Entry nameLYSO_BPT7
AccessionPrimary (citable) accession number: P00806
Secondary accession number(s): Q38567
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 98 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references