Protein

UniProt accession
A0AAX4Q9G1 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MTRFYKGIAGRRGANPSGVVIHNDAGSVYANAAFYRGWLPSHDAENGFAHYYVASDGTFQAEDEMNMAWHTANSTGNAYYIGIEACQSMGPENIFRQNEENSIKLAAQILKRYGLQPNRNTVKLHKQFSATSCPHRSVALHGDGYVMQDYFIARIKSYMGSNPTPAPAPNTGTRKYNIDLVNMNSKAFQIKGWFTPAKATKGQDIWVYIMKKGGPEIARFKAKKIQRPDVQKAVSNPNGADVGFQVDALTPEGVLGKDFDLLLRYNNDNKEEIRTKEHWKAPALINEGYLDKVAGDAKGVTFAGWHLNTRQKDGFKHYLFVTDAKTGKEYVRFDITGGSYLASPDITKKYGPEIAQRSNCRFHNWCALAANHPARGKTVNIISRYAPAKEIDTKTSTDKLWGTYRL
Physico‐chemical
properties
protein length:406 AA
molecular weight:45369,00000 Da
isoelectric point:9,45527
aromaticity:0,11330
hydropathy:-0,59852

Domains

Domains [InterPro]
IPR036505
11–157
IPR036505
IPR002502
6–145
IPR002502
IPR002502
14–135
IPR002502
IPR002502
15–136
IPR002502
IPR051206
14–139
IPR051206
IPR036505
3–161
IPR036505
Protein sequence: A0AAX4Q9G1
1 406
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Enterococcus phage VRE9_2
[NCBI] 		3141816 No lineage information
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
XAG97308.1 [NCBI]
Genbank nucleotide accession
PP680568 [NCBI]
CDS location
range 93597 -> 94817
strand +
CDS
ATGACTCGTTTTTATAAAGGAATCGCTGGGCGTCGAGGGGCTAACCCATCAGGTGTAGTTATTCACAATGATGCAGGCTCTGTTTATGCTAATGCTGCATTTTATCGTGGATGGTTACCTTCTCATGATGCAGAAAATGGCTTTGCTCATTATTACGTAGCTAGTGATGGAACATTCCAAGCAGAAGATGAAATGAATATGGCATGGCATACTGCGAACTCAACTGGTAACGCATATTATATCGGTATTGAAGCATGTCAATCAATGGGACCAGAAAATATTTTCCGACAAAATGAAGAAAATTCTATTAAACTAGCAGCTCAAATCTTAAAGAGATATGGTTTACAACCTAATAGAAATACTGTAAAATTGCATAAACAATTTTCAGCAACTTCTTGTCCTCATCGTTCTGTTGCTTTGCATGGCGATGGATACGTAATGCAAGATTATTTTATTGCTCGTATTAAATCTTATATGGGTTCTAATCCAACCCCAGCCCCAGCACCAAATACTGGAACTAGAAAATATAATATTGATCTAGTTAATATGAATTCAAAAGCTTTCCAAATCAAAGGTTGGTTTACCCCAGCTAAGGCTACAAAAGGTCAAGATATTTGGGTTTATATTATGAAAAAAGGTGGACCAGAAATTGCCCGCTTTAAAGCGAAAAAAATTCAACGTCCAGACGTTCAAAAAGCAGTTTCAAATCCTAACGGAGCAGATGTTGGTTTCCAAGTAGATGCTCTTACACCAGAAGGTGTCCTAGGAAAAGATTTTGATTTATTGCTTCGTTACAATAATGATAACAAAGAAGAAATTCGCACTAAAGAGCATTGGAAAGCTCCTGCATTAATTAATGAAGGATACCTAGATAAAGTTGCTGGAGATGCCAAAGGTGTTACATTCGCTGGATGGCATTTAAATACACGTCAAAAAGATGGATTTAAACATTATCTATTTGTAACTGACGCAAAAACTGGGAAAGAATATGTACGATTTGATATTACAGGAGGATCTTACTTAGCTTCTCCAGATATCACTAAAAAGTATGGTCCAGAAATTGCTCAACGTAGTAACTGTCGTTTCCATAATTGGTGCGCATTAGCAGCAAATCATCCAGCTAGAGGTAAAACTGTTAATATTATTAGCCGTTATGCTCCTGCAAAAGAAATTGATACAAAAACTTCTACAGATAAACTGTGGGGGACTTATAGACTATAA

Gene Ontology

Description Category Evidence (source)
GO:0001897 symbiont-mediated cytolysis of host cell Biological process Inferred from Electronic Annotation (InterPro)
GO:0008745 N-acetylmuramoyl-L-alanine amidase activity Molecular function Inferred from Electronic Annotation (UniProt)
GO:0009253 peptidoglycan catabolic process Biological process Inferred from Electronic Annotation (InterPro)
GO:0009254 peptidoglycan turnover Biological process Inferred from Electronic Annotation (TreeGrafter)
GO:0042742 defense response to bacterium Biological process Inferred from Electronic Annotation (UniProt)
GO:0071555 cell wall organization Biological process Inferred from Electronic Annotation (UniProt)

Enzymatic activity

EC Number Entry Name Reaction Catalyzed Classification Evidence Source
3.5.1.28 N-acetylmuramoyl-L-alanine amidase residues in certain cell-wall glycopeptides
Hydrolases
Acting on carbon-nitrogen bonds, other than peptide bonds
In linear amides
 match to sequence model evidence used in automatic assertion
ECO:0000256 		ARBA:ARBA00001561

Tertiary structure

No tertiary structures available.