Domains within Bacillus subtilis subsp. subtilis str. 168 protein YRVJ_BACSU (O32041)

Putative N-acetylmuramoyl-L-alanine amidase YrvJ

Alternative representations: 1 /

Protein length518 aa
Source databaseUniProt
Identifiers G4ET11_BACIU, G4ET11, A0A164WYP7_BACIU, A0A164WYP7, A0A1B2BDK8_BACIU, A0A1B2BDK8, L8AP58_BACIU, L8AP58, A0A0T8Q1N3_STREE, A0A0T8Q1N3, H9TZX3_BACIU, H9TZX3, I0F716_9BACI, I0F716, YRVJ_BACSU, O32041

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 Bacillus subtilis subsp. subtilis str. 168

Predicted functional partners

YRVJ_BACSU is shown as yrvJ 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 yrvJ

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

KEGG pathways

PathwayDescription
map01503Cationic antimicrobial peptide (CAMP) resistance

KEGG orthologous groups

KONameDescription
K01448amiABCN-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28]
K07184ygiMSH3 domain protein

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 224308.BSU27580 in eggNOG.

OGTaxonomic classDescription
LCOG3103All organisms (root)SH3 domain protein,N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28],peptidoglycan DL-endopeptidase CwlO [EC:3.4.-.-]
B32PFBacillus subtilis group (species group)N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28]
LCOG0860All organisms (root)N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28],bla regulator protein blaR1,stage II sporulation protein D
COG3103Bacteria (superkingdom)SH3 domain protein,N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28],peptidoglycan DL-endopeptidase CwlO [EC:3.4.-.-]
COG0860Bacteria (superkingdom)N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28],bla regulator protein blaR1,stage II sporulation protein D
9XIZKFirmicutes (phylum)N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28],peptidoglycan DL-endopeptidase CwlO [EC:3.4.-.-],stage II sporulation protein D
G62GKBacilli (class)N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28]
F2X9SBacillales (order)N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28]
F6EUPBacillaceae (family)N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28]
AARIIBacillus (genus)N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28]
BAJ96Bacillus subtilis (species)N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28]

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: