Protein

UniProt accession
A0AAX4PSR7 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
METYSKLTTSVNPNAMYCELRQGIIEFIVIHHNATTNKDVAMSTWYTTSGNWTSAHYEITDNEIIGCVGENYTAYHAGGTGGSDVPSIPNVNHRSIGLEHVNSTGAPSWSVSDATLRNSAKLIADICQRYGLPINRNTIKAHNEVTATACPGGINVDKLVRMAQEAANGKQPEPPKPPLPKPQKEDDKMFIYMKRQKNGNTEQWFVCGDKRMYLPNMTYVKEANDLINRYGGSKNQTTYNYDNFGLKMIEKAYTEVKV
Physico‐chemical
properties
protein length:258 AA
molecular weight:28793,00000 Da
isoelectric point:7,64015
aromaticity:0,08527
hydropathy:-0,62016

Domains

Domains [InterPro]
IPR036505
12–172
IPR036505
IPR002502
8–152
IPR002502
IPR002502
25–153
IPR002502
IPR051206
24–203
IPR051206
IPR036505
24–154
IPR036505
IPR002502
25–152
IPR002502
Protein sequence: A0AAX4PSR7
1 258
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Enterococcus phage vB_Efs26_KEN12
[NCBI] 		3138323 Rountreeviridae > Copernicusvirus >
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
WZP35500.1 [NCBI]
Genbank nucleotide accession
PP582185 [NCBI]
CDS location
range 8273 -> 9049
strand +
CDS
ATGGAAACTTATTCAAAATTAACAACTAGCGTGAACCCTAATGCTATGTATTGTGAACTTAGACAAGGCATAATTGAGTTTATTGTTATACACCACAATGCGACAACTAATAAAGATGTTGCGATGTCAACGTGGTATACAACTTCAGGAAATTGGACTTCCGCTCACTATGAAATTACAGATAATGAAATTATCGGCTGTGTCGGTGAAAACTACACCGCTTATCACGCGGGAGGAACAGGCGGTAGCGACGTTCCAAGCATTCCTAATGTAAACCATCGTTCTATTGGATTAGAGCATGTAAACAGCACGGGAGCTCCCTCATGGAGCGTTAGCGACGCCACACTTAGAAACAGTGCTAAATTAATCGCTGACATTTGCCAACGTTACGGTTTACCTATCAACAGAAACACCATTAAAGCGCATAATGAAGTAACAGCAACAGCATGCCCTGGAGGTATCAACGTAGACAAACTTGTGAGAATGGCTCAAGAAGCAGCTAACGGAAAACAACCAGAACCACCAAAACCACCATTACCAAAACCACAGAAAGAGGATGATAAAATGTTTATTTATATGAAAAGACAAAAGAATGGAAATACTGAACAATGGTTTGTGTGCGGAGATAAACGCATGTACTTACCTAATATGACTTATGTAAAAGAAGCTAATGATTTAATCAATCGTTACGGAGGTTCAAAAAATCAAACAACATATAATTATGATAACTTTGGTTTAAAAATGATAGAGAAAGCTTATACAGAAGTTAAAGTATAA

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.