Protein

UniProt accession

Q94ML9 [UniProt]

Protein name

Endolysin

PhaLP type

endolysin

evidence: UniProt function annotation

probability: 99 % (predicted by ML model)

Protein sequence

MQISQAGINLIKSFEGLQLKAYKAVPTEKHYTIGYGHYGSDVSPRQVITAKQAEDMLRDDVQAFVDGVNKALKVSVTQNQFDALVSFAYNVGLGAFRSSSLLEYLNEGRTALAAAEFPKWNKSGGKVYQGLVNRRAQEQALFNSGTPKNVSRGTSSTKTTPKYKVKNGDNLTKIAKKHNTTVATLLKLNPGIKDPNMIRVGQTLNVTGSGGKTHKVKSGDTLSKIAVDNKTTVSKLMNLNPEITNPNHIKVGQTIRLS

Physico‐chemical properties

protein length:	258 AA
molecular weight:	28036,00000 Da
isoelectric point:	9,97108
aromaticity:	0,06202
hydropathy:	-0,45814

Domains

Domains [InterPro]

IPR033907

7–143

IPR033907 IPR018392 IPR018392

IPR051018

2–144

IPR051018 IPR036779 IPR018392

IPR034690

1–145

IPR034690 IPR018392

IPR023347

2–151

IPR023347 IPR036779

IPR002196

12–138

IPR002196

IPR023346

1–145

IPR023346

Protein sequence: Q94ML9

1 258

Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Domains [InterPro]

InterPro ID	Start	End	Source	Name
IPR033907	7	143	CDD	Endolysin/autolysin
IPR018392	214	257	Pfam	LysM domain
IPR051018	2	144	PANTHER	Bacteriophage Glycosyl Hydrolase 24
IPR018392	162	207	Pfam	LysM domain
IPR034690	1	145	HAMAP	Endolysin T4 type
IPR023347	2	151	Gene3D	Lysozyme domain superfamily
IPR036779	210	258	SUPFAM	LysM domain superfamily
IPR018392	161	206	Pfam	LysM domain
IPR018392	163	206	Pfam	LysM domain
IPR002196	12	138	Pfam	Glycoside hydrolase, family 24
IPR023346	1	145	SUPFAM	Lysozyme-like domain superfamily
IPR036779	162	206	SUPFAM	LysM domain superfamily

Taxonomy

	Name	Taxonomy ID	Lineage
Phage	Bacillus amyloliquefaciens phage Morita2001 [NCBI]	158197	No lineage information
Host	No host information

Coding sequence (CDS)

Genbank protein accession

AAK40280.1 [NCBI]

Genbank nucleotide accession

AY030242 [NCBI]

CDS location

range 1 -> 777
strand +

CDS

ATGCAAATTTCACAAGCAGGCATCAACTTGATTAAGAGTTTTGAAGGTTTACAACTGAAAGCCTATAAAGCTGTTCCAACTGAAAAGCATTACACTATTGGTTACGGTCATTACGGTTCTGATGTTTCACCTAGACAGGTTATCACTGCTAAACAGGCAGAAGACATGTTGCGTGATGATGTACAGGCTTTTGTAGACGGTGTTAATAAAGCATTGAAAGTGTCTGTTACTCAAAACCAGTTTGATGCTTTAGTATCATTCGCTTATAACGTTGGGTTAGGGGCTTTCAGGTCTTCTTCTCTACTGGAATACTTGAATGAAGGAAGAACAGCTCTAGCGGCGGCTGAATTCCCTAAATGGAATAAGTCAGGCGGTAAAGTGTATCAAGGGTTGGTTAACCGTAGAGCACAAGAACAAGCCTTGTTTAATAGTGGAACACCTAAAAATGTTTCACGTGGAACATCGTCTACTAAGACAACACCTAAGTACAAGGTGAAAAATGGGGACAACCTTACTAAAATCGCTAAAAAGCATAATACAACGGTTGCTACTTTGTTGAAGCTTAACCCAGGTATCAAAGACCCTAACATGATTAGAGTTGGACAAACACTAAATGTTACAGGTAGCGGCGGTAAAACACATAAGGTGAAGAGTGGTGACACACTCAGTAAAATTGCCGTTGATAATAAAACAACTGTAAGTAAGTTAATGAATCTAAACCCTGAAATTACGAATCCGAATCATATAAAAGTAGGTCAAACAATTAGATTAAGCTGA

Gene Ontology

	Description	Category	Evidence (source)
GO:0003796	lysozyme activity	Molecular function	Inferred from Electronic Annotation (UniProt)
GO:0009253	peptidoglycan catabolic process	Biological process	Inferred from Electronic Annotation (InterPro)
GO:0016998	cell wall macromolecule catabolic process	Biological process	Inferred from Electronic Annotation (InterPro)
GO:0030430	host cell cytoplasm	Cellular component	Inferred from Electronic Annotation (UniProt)
GO:0042742	defense response to bacterium	Biological process	Inferred from Electronic Annotation (UniProt)
GO:0044659	viral release from host cell by cytolysis	Biological process	Inferred from Electronic Annotation (InterPro)

Enzymatic activity

EC Number	Entry Name	Reaction Catalyzed	Classification	Evidence	Source
3.2.1.17	lysozyme aka muramidase	D-glucosamine residues in chitodextrins	Hydrolases Glycosylases Glycosidases, i.e. enzymes hydrolyzing O- and S-glycosyl compounds	match to sequence model evidence used in automatic assertion ECO:0000256	ARBA:ARBA00000632

Tertiary structure

PDB ID: upi000009b74a_model

Method: AlphaFold3 Non-commercial

Resolution: –

Chain position: A