Protein

UniProt accession

Q0SPG7 [UniProt]

Protein name

lysozyme

PhaLP type

endolysin

evidence: ML prediction

probability: 99 % (predicted by ML model)

Protein sequence

MQSRNNNNLKGIDVSNWKGNINFESVKNDGVEVVYIKATEGNYFKDKYAKQNYEGAKEQGLSVGFYHFFRANKGAKDQANFFIDYLNEIGAVNYDCKLALDIETTEGVGVRDLTSMCIEFLEEVKRLTGKEVVVYTYTSFANNNLDSRLGNYPVWIAHYGVNTPGANNIWSSWVGFQYSENGSVAGVNGGCDMNEFTEEIFIDSSNFNLDNATTKNVSTKLNIRAKGTTNSKIIGSIPAGETFKIKWVDEDYLGWYYVEYNGVVGYVNADYVEKLQMATTYNVSTFLNVREEGSLNSRIVDKINSGDIFRIDWVDSDFIGWYRITTKNGKVGFVNAEFVKKL

Physico‐chemical properties

protein length:	342 AA
molecular weight:	38594,00000 Da
isoelectric point:	5,06927
aromaticity:	0,13743
hydropathy:	-0,39737

Domains

Domains [InterPro]

IPR002053

12–187

IPR002053 IPR003646 IPR003646

IPR017853

8–197

IPR017853 IPR036028

IPR018077

9–115

IPR018077

IPR002053

8–211

IPR002053

Protein sequence: Q0SPG7

1 342

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

Domains [InterPro]

InterPro ID	Start	End	Source	Name
IPR002053	12	187	Pfam	Glycoside hydrolase, family 25
IPR003646	212	276	Pfam	SH3-like domain, bacterial-type
IPR003646	286	340	Pfam	SH3-like domain, bacterial-type
IPR017853	8	197	SUPFAM	Glycoside hydrolase superfamily
IPR018077	9	115	SMART	Glycoside hydrolase, family 25 subgroup
IPR002053	8	211	Pfam	Glycoside hydrolase, family 25
IPR036028	247	277	SUPFAM	SH3-like domain superfamily

Taxonomy

	Name	Taxonomy ID	Lineage
Phage	Clostridium phage phiSM101 [NCBI]	396359	No lineage information
Host	Clostridium perfringens SM101 [NCBI]	289380	Bacteria > Firmicutes > Clostridia > Clostridiales > Clostridiaceae > Clostridium

Coding sequence (CDS)

Genbank protein accession

ABG87925.1 [NCBI]

Genbank nucleotide accession

CP000315 [NCBI]

CDS location

range 32949 -> 33977
strand -

CDS

ATGCAAAGTAGAAACAATAATAATTTAAAAGGAATTGATGTATCAAACTGGAAAGGAAATATAAATTTTGAGAGTGTAAAAAATGATGGCGTAGAAGTAGTTTATATTAAAGCTACAGAAGGTAATTACTTTAAAGATAAATACGCTAAACAAAATTATGAAGGAGCGAAAGAGCAAGGATTAAGTGTAGGATTTTATCATTTTTTTAGAGCTAATAAAGGAGCTAAGGATCAAGCTAATTTCTTTATAGATTATTTAAATGAAATAGGAGCAGTTAATTATGATTGTAAATTAGCTTTAGATATAGAAACTACTGAAGGGGTAGGAGTAAGAGATTTAACTTCTATGTGTATAGAATTCTTAGAAGAAGTAAAAAGACTTACTGGAAAAGAAGTTGTTGTATATACATATACAAGCTTTGCAAATAACAACTTAGATAGTAGACTAGGTAATTATCCAGTTTGGATTGCACATTATGGGGTAAACACTCCAGGAGCCAATAACATATGGAGTTCATGGGTTGGATTCCAATATTCAGAGAATGGAAGTGTAGCTGGTGTAAACGGTGGCTGCGATATGAATGAGTTTACAGAAGAAATCTTTATTGATTCAAGTAACTTTAATTTAGATAATGCTACTACTAAAAATGTAAGCACTAAATTAAATATAAGAGCTAAAGGAACTACTAATTCTAAAATAATTGGCTCAATACCAGCTGGCGAAACATTTAAAATAAAATGGGTTGATGAAGATTATCTTGGTTGGTATTACGTTGAGTACAACGGAGTTGTTGGATATGTAAATGCAGATTATGTAGAAAAGCTACAAATGGCTACTACTTATAATGTTAGTACATTCTTAAATGTAAGAGAAGAAGGATCATTGAATTCTAGAATAGTAGACAAAATAAATTCAGGTGATATTTTTAGAATAGATTGGGTGGATTCCGATTTTATAGGATGGTATAGAATAACAACTAAAAATGGAAAAGTTGGATTTGTTAATGCTGAATTTGTTAAAAAATTATAG

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:0016052	carbohydrate catabolic process	Biological process	Inferred from Electronic Annotation (TreeGrafter)
GO:0016998	cell wall macromolecule catabolic process	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: 4KRU

Method: X-ray crystallography

Resolution: 1.37

Chain position: A

View on RCSB