Protein

UniProt accession
D4P7C1 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MDVLRAFGVKVKEFDAWRDRGQGDFFTIWGVIAHHTGSNNASAASIAYGHEGLKGLLSQIHLDRNGVATITGAGIAWHAGVGSWPGIQTNNANAVTIGVEANSDGVSPWPPEMLDAYHRICAAICWFLGHSSLRTIGHKEWAKVQGKWDPGGIDMAQFRAKVQYYIDHPPFMPPPQPVTEAGEPMAFWDDQVPTILSPEKSFPRHEYLQLIDMHAFLANTQSKQVLDQMKLVRDDNQRILNEMQLMRDDLSELATAVLSGVKKDG
Physico‐chemical
properties
protein length:265 AA
molecular weight:29326,00000 Da
isoelectric point:5,84637
aromaticity:0,09057
hydropathy:-0,28340

Domains

Domains [InterPro]
Protein sequence: D4P7C1
1 265
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Rhodococcus phage ReqiPepy6
[NCBI]
691965 Pepyhexavirus > Pepyhexavirus pepy6
Host Rhodococcus equi
[NCBI]
43767 Bacteria > Actinobacteria > Actinobacteria > Corynebacteriales > Nocardiaceae > Rhodococcus

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
ADD80901.1 [NCBI]
Genbank nucleotide accession
GU580941 [NCBI]
CDS location
range 9009 -> 9806
strand +
CDS
GTGGATGTTCTTCGTGCGTTCGGAGTCAAAGTCAAAGAGTTCGACGCTTGGCGTGATCGTGGCCAGGGAGATTTCTTCACCATTTGGGGCGTCATCGCCCATCATACCGGATCGAACAATGCGTCGGCGGCATCCATTGCTTACGGTCACGAGGGTCTGAAGGGACTTCTCTCTCAGATTCATCTGGATCGAAATGGTGTCGCCACCATCACCGGTGCGGGTATTGCTTGGCATGCCGGTGTTGGATCTTGGCCTGGAATTCAAACCAACAACGCAAACGCTGTGACGATCGGTGTCGAAGCGAACTCCGACGGTGTTTCGCCTTGGCCTCCAGAGATGCTGGATGCCTACCATCGGATCTGCGCAGCAATCTGTTGGTTCCTCGGCCACTCCTCTCTCCGAACTATCGGCCACAAAGAATGGGCCAAGGTTCAGGGGAAGTGGGATCCGGGCGGAATCGACATGGCTCAGTTCCGAGCCAAGGTTCAGTACTACATCGACCATCCGCCGTTCATGCCGCCACCACAGCCCGTTACTGAAGCAGGAGAACCAATGGCTTTCTGGGACGATCAAGTACCGACAATTCTTTCGCCTGAGAAGAGTTTCCCTCGTCATGAATACTTGCAGCTCATCGACATGCACGCCTTCTTGGCGAACACGCAGTCGAAGCAGGTTCTTGATCAAATGAAGTTGGTTCGAGATGACAATCAGCGCATCCTGAACGAGATGCAGCTCATGCGAGATGACCTCTCTGAGTTGGCTACTGCCGTTCTCAGTGGCGTCAAGAAGGACGGTTAA

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.