Reviewed, UniProtKB/Swiss-Prot P00806 (NAAA_BPT7)

Names and origin

Protein names

Recommended name:
    N-acetylmuramoyl-L-alanine amidase
    EC=3.5.1.28
Alternative name(s):
    T7 lysozyme

Gene names

Name:

3.5

Organism

Enterobacteria phage T7 (Bacteriophage T7)

Taxonomic identifier

10760 [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	Evidence at protein level.

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 T7 RNA polymerase.
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.
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
Technical term	3D-structure
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 protein binding Ref.5 Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
1	P00573	1	EBI-1026942,EBI-1026948

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed; by host

Chain

2 – 151

150

N-acetylmuramoyl-L-alanine amidase

PRO_0000164410

Sites

Metal binding

18

1

Zinc

Metal binding

123

1

Zinc

Metal binding

131

1

Zinc

Site

47

1

Essential for amidase activity and zinc hydrate coordination

Experimental info

Sequence conflict

90

1

G → V in AAB32819. Ref.3

Sequence conflict

119

1

V → G Ref.1

Sequence conflict

119

1

V → G Ref.2

Sequence conflict

119

1

V → G Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

151

Helix Strand Turn

Details...

Beta strand

14 – 19

6

Helix

30 – 39

10

Beta strand

48 – 51

4

Beta strand

57 – 59

3

Beta strand

68 – 70

3

Helix

74 – 76

3

Beta strand

77 – 83

7

Helix

98 – 114

17

Beta strand

119 – 122

4

Helix

123 – 125

3

Beta strand

127 – 129

3

Helix

136 – 142

7

Sequences

	Sequence		Length	Mass (Da)
	P00806-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: C36BC018754A4146	FASTA	151	16,979
	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

References

	« Hide 'large scale' referencesShow '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: 6864790] [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: 7310871] [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: 7801634] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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: 8171031] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SEQUENCE REVISION TO 119.
[5]	"Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme." Jeruzalmi D., Steitz T.A. EMBO J. 17:4101-4113(1998) [PubMed: 9670025] [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.

PIR

MUBPA7. C94615.

RefSeq

NP_041973.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ARO	X-ray	2.80	L	1-151	[»]
1LBA	X-ray	2.20	A	7-151	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6090N.

IntAct

P00806. 1 interaction.

Genome annotation databases

GeneID

1261077.

Enzyme and pathway databases

BRENDA

3.5.1.28. 1115.

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_BPT7

Accession

Primary (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:	February 9, 2010
This is version 78 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)