Domains within Clostridium acetobutylicum ATCC 824 protein Q97FV5_CLOAB (Q97FV5)

Lysozyme

Alternative representations: 1 /

Protein length325 aa
Source databaseUniProt
Identifiers Q97FV5_CLOAB, Q97FV5

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 Clostridium acetobutylicum

Predicted functional partners

Q97FV5_CLOAB is shown as CA_C2621 in the network

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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 CA_C2621

Protein Q97FV5_CLOAB 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
K17733cwlKpeptidoglycan LD-endopeptidase CwlK [EC:3.4.-.-]
K07273acmlysozyme

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 272562.CA_C2621 in eggNOG.

OGTaxonomic classDescription
LCOG3409All organisms (root)N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28],peptidoglycan LD-endopeptidase CwlK [EC:3.4.-.-],membrane-bound lytic murein transglycosylase B [EC:4.2.2.-]
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]
COG3409Bacteria (superkingdom)N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28],peptidoglycan LD-endopeptidase CwlK [EC:3.4.-.-],membrane-bound lytic murein transglycosylase B [EC:4.2.2.-]
9XVJ7Firmicutes (phylum)lysozyme
9A0Y5Clostridia (class)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: