P00806 (NAAA_BPT7) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 94.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: N-acetylmuramoyl-L-alanine amidase EC=3.5.1.28 Alternative name(s): T7 lysozyme | ||
| Gene names |
| ||
| Organism | Enterobacteria phage T7 (Bacteriophage T7) [Reference proteome] | ||
| Taxonomic identifier | 10760 [NCBI] | ||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Caudovirales › Podoviridae › Autographivirinae › T7likevirus | ||
| 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 Complete proteome Reference proteome |
| 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 metal ion bindingInferred 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 | ||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||
| Beta strand | 14 – 19 | 6 | ||||||||||||||||||||||||||||||||||
| Helix | 30 – 39 | 10 | ||||||||||||||||||||||||||||||||||
| Beta strand | 48 – 51 | 4 | ||||||||||||||||||||||||||||||||||
| Beta strand | 53 – 55 | 3 | ||||||||||||||||||||||||||||||||||
| Beta strand | 57 – 59 | 3 | ||||||||||||||||||||||||||||||||||
| Beta strand | 68 – 70 | 3 | ||||||||||||||||||||||||||||||||||
| Helix | 74 – 76 | 3 | ||||||||||||||||||||||||||||||||||
| Beta strand | 77 – 83 | 7 | ||||||||||||||||||||||||||||||||||
| Beta strand | 90 – 92 | 3 | ||||||||||||||||||||||||||||||||||
| Helix | 98 – 114 | 17 | ||||||||||||||||||||||||||||||||||
| Turn | 115 – 117 | 3 | ||||||||||||||||||||||||||||||||||
| Beta strand | 119 – 122 | 4 | ||||||||||||||||||||||||||||||||||
| Helix | 123 – 125 | 3 | ||||||||||||||||||||||||||||||||||
| Beta strand | 127 – 129 | 3 | ||||||||||||||||||||||||||||||||||
| Helix | 136 – 142 | 7 | ||||||||||||||||||||||||||||||||||
Sequences
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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] | "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. |
| [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] [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. | ||||||||||||||||||
| PIR | MUBPA7. C94615. | ||||||||||||||||||
| RefSeq | NP_041973.1. NC_001604.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| ProteinModelPortal | P00806. | ||||||||||||||||||
| SMR | P00806. Positions 3-151. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| DIP | DIP-6090N. | ||||||||||||||||||
| IntAct | P00806. 1 interaction. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| GeneID | 1261077. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| ProtClustDB | PHA0447. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| Gene3D | 3.40.80.10. 1 hit. | ||||||||||||||||||
| InterPro | IPR002502. Amidase_domain. IPR015510. PGRP. [Graphical view] | ||||||||||||||||||
| PANTHER | PTHR11022. PTHR11022. 1 hit. | ||||||||||||||||||
| Pfam | PF01510. Amidase_2. 1 hit. [Graphical view] | ||||||||||||||||||
| SMART | SM00644. Ami_2. 1 hit. [Graphical view] | ||||||||||||||||||
| SUPFAM | SSF55846. Amidase_2. 1 hit. | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| EvolutionaryTrace | P00806. | ||||||||||||||||||
Entry information
| Entry name | NAAA_BPT7 | ||||||||
| Accession | Primary (citable) accession number: P00806 Secondary accession number(s): Q38567 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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