Domains within Lactococcus lactis subsp. cremoris MG1363 protein ACMA_LACLM (A2RHZ5)

Probable N-acetylmuramidase

Alternative representations: 1 /

Protein length437 aa
Source databaseUniProt
Identifiers A0A165FY27_LACLC, A0A165FY27, ACMA_LACLM, A2RHZ5

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 Lactococcus lactis

Predicted functional partners

ACMA_LACLM is shown as acmA 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 acmA

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

KEGG pathways

PathwayDescription
map02040Flagellar assembly
map01503Cationic antimicrobial peptide (CAMP) resistance

KEGG orthologous groups

KONameDescription
K02395flgJpeptidoglycan hydrolase FlgJ
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 416870.llmg_0280 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.-]
LCOG1705All organisms (root)peptidoglycan hydrolase FlgJ,N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28],peptidoglycan DL-endopeptidase CwlO [EC:3.4.-.-]
COG1705Bacteria (superkingdom)peptidoglycan hydrolase FlgJ,N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28],peptidoglycan DL-endopeptidase CwlO [EC:3.4.-.-]
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.-]
9WK7YFirmicutes (phylum)peptidoglycan DL-endopeptidase LytE [EC:3.4.-.-],peptidoglycan DL-endopeptidase CwlS [EC:3.4.-.-],peptidoglycan DL-endopeptidase LytF [EC:3.4.-.-]
G57Z7Bacilli (class)peptidoglycan DL-endopeptidase LytE [EC:3.4.-.-],peptidoglycan DL-endopeptidase CwlS [EC:3.4.-.-],peptidoglycan DL-endopeptidase LytF [EC:3.4.-.-]
HWQ5ZLactobacillales (order)peptidoglycan DL-endopeptidase CwlS [EC:3.4.-.-],peptidoglycan DL-endopeptidase LytF [EC:3.4.-.-]
8TTGKStreptococcaceae (family)Glucosaminidase,LysM
89AJBLactococcus (genus)Glucosaminidase,LysM

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: