Reviewed, UniProtKB/Swiss-Prot P20331 (NAAA_BPT3)

Names and origin

Protein names

Recommended name:
    N-acetylmuramoyl-L-alanine amidase
    EC=3.5.1.28
Alternative name(s):
    T3 lysozyme

Gene names

Name:

3.5

Organism

Enterobacteria phage T3 (Bacteriophage T3)

Taxonomic identifier

10759 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Caudovirales › Podoviridae › Autographivirinae › T7-like viruses

Virus host

Escherichia coli [TaxID: 562]

Protein attributes

Sequence length	151 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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 stage	Late protein
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Gene Ontology (GO)
Biological process	peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	N-acetylmuramoyl-L-alanine amidase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed; by host By similarity
	Chain	2 – 151	150	N-acetylmuramoyl-L-alanine amidase		PRO_0000164409
Sites
	Metal binding	18	1	Zinc By similarity
	Metal binding	123	1	Zinc By similarity
	Metal binding	131	1	Zinc By similarity
	Site	47	1	Essential for amidase activity and zinc hydrate coordination By similarity

Sequences

	Sequence		Length	Mass (Da)
	P20331-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 2C0880FFC920DE9E	FASTA	151	16,874
	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

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: 2614843] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Luria.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X17255 Genomic DNA. Translation: CAA35133.1.
PIR	S07506.
RefSeq	NP_523313.1.
3D structure databases
HSSP	HSSP built from PDB template 1ARO based on UniProtKB P00806.
SMR	P20331. Positions 3-151.
ModBase	Search...
Genome annotation databases
GeneID	927411.
Enzyme and pathway databases
BRENDA	3.5.1.28. 164907.
Family and domain databases
InterPro	IPR002502. Amidase_2. IPR015510. PGRP. [Graphical view]
Gene3D	G3DSA:3.40.80.10. Amidase_2. 1 hit.
PANTHER	PTHR11022. PGRPs. 1 hit.
Pfam	PF01510. Amidase_2. 1 hit. [Graphical view]
SMART	SM00644. Ami_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NAAA_BPT3

Accession

Primary (citable) accession number: P20331

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 54 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)