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P20331 (NAAA_BPT3) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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):
T3 lysozyme
Gene names
Name:3.5
OrganismEnterobacteria phage T3 (Bacteriophage T3)
Taxonomic identifier10759 [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 existenceInferred from homology

General annotation (Comments)

Function

This protein is not required for lysis but plays an important role in DNA synthesis. It is known to detach the host chromosome from the bacterial membrane to which it is normally bound. It is a bifunctional protein that cuts amide bonds in the bacterial cell wall and binds to and inhibits transcription by T3 RNA polymerase By similarity.

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 By similarity.

Enzyme regulation

Binding of T3 RNA polymerase inhibits amidase activity By similarity.

Sequence similarities

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

Ontologies

Keywords
   Developmental stageLate protein
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host By similarity
Chain2 – 151150N-acetylmuramoyl-L-alanine amidase
PRO_0000164409

Sites

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

Sequences

Sequence LengthMass (Da)Tools
P20331 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 2C0880FFC920DE9E

FASTA15116,874
        10         20         30         40         50         60 
MAKVQFKPRA TTEAIFVHCS ATKPSQNVGV REIRQWHKEQ GWLDVGYHFI IKRDGTVEAG 

        70         80         90        100        110        120 
RDELAVGSHA KGYNHNSIGV CLVGGIDDKG KFDANFTPAQ MQSLRSLLVT LLAKYEGSVL 

       130        140        150 
RAHHDVAPKA CPSFDLKRWW EKNELVTSDR G 

« Hide

References

[1]"Sequence of bacteriophage T3 DNA from gene 2.5 through gene 9."
Beck P.J., Gonzalez S., Ward C.L., Molineux I.J.
J. Mol. Biol. 210:687-701(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Luria.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17255 Genomic DNA. Translation: CAA35133.1.
PIRS07506.
RefSeqNP_523313.1. NC_003298.1.

3D structure databases

ProteinModelPortalP20331.
SMRP20331. Positions 3-151.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID927411.

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...

Entry information

Entry nameNAAA_BPT3
AccessionPrimary (citable) accession number: P20331
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 69 of the entry and version 3 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