Protein

UniProt accession
H7BW58 [UniProt]
Protein name
N-acetylmuramoyl-L-alanine amidase
PhaLP type
endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence
MTRMSNSTLISYTKLSPNHSGKRTKKIDTVTIHCMAGQLSVESCGALFAQSSREASSNYGIGNDGRIALYVDEGNHSWCTSSNANDQRAVTIEVASDAKHPYAVNSKAYDALLDLVTDICKRNGIKRLVWSTSKSDRMNHLNGCNMTVHRDYANKACPGDWLYNRHGEIAAEVNRRLGSGSSTPSTGESTGGAADIKIGDVVEFTGTKHYVSSTAAAASSCKPGKAKVTALAKGKAHPYHLIAVSGGGSTVYGWANVADIKTGTAAVATSYLVEVTTDVLNIRKGPGTSYGTNGSIKDKGTYTIVAESDGPGASKWGKLKSGAGWISLDYTKKV
Physico‐chemical
properties
protein length:334 AA
molecular weight:35284,00000 Da
isoelectric point:9,21526
aromaticity:0,06587
hydropathy:-0,37904

Domains

Domains [InterPro]
IPR051206
7–172
IPR051206
IPR036505
12–164
IPR036505
IPR002502
24–160
IPR002502
IPR002502
16–159
IPR002502
IPR002502
26–161
IPR002502
IPR036505
9–179
IPR036505
Protein sequence: H7BW58
1 334
Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Taxonomy

  Name Taxonomy ID Lineage
Phage Bacteriophage sp
[NCBI] 		38018 No lineage information
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)
Genbank protein accession
AFB76053.1 [NCBI]
Genbank nucleotide accession
JQ680374 [NCBI]
CDS location
range 9369 -> 10373
strand +
CDS
ATGACGAGGATGAGTAACAGCACCCTGATTTCCTACACCAAGCTCAGCCCCAACCACTCGGGCAAGCGCACCAAGAAGATCGACACCGTCACGATCCACTGTATGGCCGGCCAGCTCTCCGTCGAGAGCTGCGGCGCACTGTTCGCACAGAGCAGCCGGGAGGCGTCCAGCAACTACGGCATCGGCAACGACGGCCGCATCGCCCTCTATGTGGACGAGGGCAACCACTCGTGGTGCACCTCGTCCAACGCCAACGACCAGAGGGCCGTCACCATTGAGGTCGCCAGCGACGCGAAGCACCCCTACGCTGTCAACAGCAAGGCATACGACGCGCTGCTGGATCTCGTGACCGACATCTGCAAGCGCAACGGCATCAAGCGGCTCGTCTGGTCGACCAGCAAAAGCGACCGTATGAACCACCTGAACGGCTGCAACATGACCGTGCACCGGGACTACGCGAACAAAGCCTGCCCGGGCGACTGGCTCTACAACCGCCACGGGGAGATCGCGGCCGAGGTCAACCGCCGGCTCGGATCCGGCAGTAGCACCCCCTCCACCGGGGAGAGCACCGGCGGCGCGGCTGACATCAAGATCGGCGACGTGGTAGAGTTCACCGGCACCAAGCACTACGTCAGCTCCACGGCCGCGGCTGCGTCGAGCTGCAAGCCCGGCAAGGCCAAGGTCACAGCGCTTGCCAAGGGCAAGGCGCACCCATACCACCTGATCGCCGTCTCTGGCGGCGGCTCCACCGTCTACGGCTGGGCAAATGTGGCCGACATCAAGACCGGCACGGCAGCCGTGGCCACCTCGTACCTCGTGGAGGTGACGACCGACGTGCTGAACATCCGCAAGGGCCCCGGCACCAGCTACGGCACCAACGGCTCCATCAAGGACAAGGGCACCTACACCATCGTCGCCGAGAGCGACGGGCCCGGGGCCTCTAAGTGGGGCAAGCTCAAGAGTGGCGCCGGCTGGATCTCGCTGGATTACACCAAGAAGGTCTAA

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.