Domains within Clostridium perfringens str. 13 protein LYS_CLOPE (P26836)

Probable autolytic lysozyme

Alternative representations: 1 /

Protein length342 aa
Source databaseUniProt
Identifiers LYS_CLOPE, P26836

Domain architecture analysis

Display all proteins with similar:

Domain organisationProteins having all the domains as the query in the same order. Additional domains are allowed.
Domain compositionProteins with the same domain composition have at least one copy of each of the domains of the query.

This domain architecture was probably invented with the emergence of Firmicutes

Predicted functional partners

LYS_CLOPE is shown as CPE0382 in the network

Click and drag to pan the network, and zoom by using your mouse wheel. Click the protein nodes for additional options.

The network on the left comes from STRING, a database of known and predicted protein interactions. Displayed here is the evidence view, where different line colors represent the types of evidence for the association.

Open the STRING annotation page for CPE0382

Protein LYS_CLOPE is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map01503Cationic antimicrobial peptide (CAMP) resistance
map01502Vancomycin resistance

KEGG orthologous groups

KONameDescription
K07273acmlysozyme
K08307mltD, dniRpeptidoglycan lytic transglycosylase D [EC:4.2.2.29]

Orthologous groups

Orthology information is taken from eggNOG, a database of orthologous groups of genes. Orthologous groups containing this protein are listed below. This protein is named 195102.gene:10489638 in eggNOG.

OGTaxonomic classDescription
LCOG1388All organisms (root)membrane-bound lytic murein transglycosylase D [EC:4.2.2.-],N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28],streptogrisin C [EC:3.4.21.-]
LCOG3757All organisms (root)lysozyme,N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28],zinc D-Ala-D-Ala carboxypeptidase [EC:3.4.17.14]
COG3757Bacteria (superkingdom)lysozyme,N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28],zinc D-Ala-D-Ala carboxypeptidase [EC:3.4.17.14]
COG1388Bacteria (superkingdom)membrane-bound lytic murein transglycosylase D [EC:4.2.2.-],N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28],streptogrisin C [EC:3.4.21.-]
9XKTUFirmicutes (phylum)lysozyme
997MZClostridia (class)lysozyme
7VZ20Eubacteriales (order)lysozyme
ECGRKClostridiaceae (family)lysozyme
FI158Clostridium (genus)lysozyme

The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Low complexity. In either case, features not shown in the above diagram are listed in the right side table below, and the reason for their omission is shown in the 'Reason' column.

Confidently predicted domains, repeats, motifs and features:

Outlier homologues and homologues of known structure:

Features NOT shown in the diagram: