Q06320 · CWLC_BACSU
- ProteinSporulation-specific N-acetylmuramoyl-L-alanine amidase
- GenecwlC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids255 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. CwlC is able to hydrolyze type A cell walls such as B.subtilis. Its main function is to lyze the mother cell wall peptidoglycan, playing a role during sporulation.
Catalytic activity
Cofactor
Activity regulation
Inhibited by EDTA.
pH Dependence
Optimum pH is 8.5-9.5.
Temperature Dependence
Optimum temperature is 60 degrees Celsius.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | outer membrane-bounded periplasmic space | |
Molecular Function | metal ion binding | |
Molecular Function | N-acetylmuramoyl-L-alanine amidase activity | |
Molecular Function | peptidoglycan binding | |
Biological Process | cell wall organization | |
Biological Process | establishment of competence for transformation | |
Biological Process | peptidoglycan catabolic process | |
Biological Process | sporulation resulting in formation of a cellular spore |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSporulation-specific N-acetylmuramoyl-L-alanine amidase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionQ06320
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Is associated with the mother cell wall of sporulating cells.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 10 | 23% of wild-type activity. | ||||
Sequence: H → Q | ||||||
Mutagenesis | 24 | Loss of activity. | ||||
Sequence: E → A, Q, or S | ||||||
Mutagenesis | 55 | Loss of activity. | ||||
Sequence: D → V | ||||||
Mutagenesis | 79 | Loss of activity. | ||||
Sequence: H → L | ||||||
Mutagenesis | 79 | 15% of wild-type activity. | ||||
Sequence: H → Q | ||||||
Mutagenesis | 81 | Loss of activity. | ||||
Sequence: N → I | ||||||
Mutagenesis | 141 | Loss of activity. | ||||
Sequence: E → Q or V |
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000164418 | 2-255 | Sporulation-specific N-acetylmuramoyl-L-alanine amidase | |||
Sequence: VKIFIDPGHGGSDPGATGNGLQEKTLTLQIALALRTILTNEYEGVSLLLSRTSDQYVSLNDRTNAANNWGADFFLSIHVNSGGGTGFESYIYPDVGAPTTTYQSTIHSEVIQAVDFADRGKKTANFHVLRESAMPALLTENGFIDTVSDANKLKTSSFIQSLARGHANGLEQAFNLKKTSSSGLYKVQIGAFKVKANADSLASNAEAKGFDSIVLLKDGLYKVQIGAFSSKDNADTLAARAKNAGFDAIVILES |
Proteomic databases
Expression
Induction
Induced at 6 to 7 hours after sporulation.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, repeat, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-172 | MurNAc-LAA | ||||
Sequence: IFIDPGHGGSDPGATGNGLQEKTLTLQIALALRTILTNEYEGVSLLLSRTSDQYVSLNDRTNAANNWGADFFLSIHVNSGGGTGFESYIYPDVGAPTTTYQSTIHSEVIQAVDFADRGKKTANFHVLRESAMPALLTENGFIDTVSDANKLKTSSFIQSLARGHANGLE | ||||||
Domain | 180-254 | SPOR | ||||
Sequence: TSSSGLYKVQIGAFKVKANADSLASNAEAKGFDSIVLLKDGLYKVQIGAFSSKDNADTLAARAKNAGFDAIVILE | ||||||
Repeat | 184-219 | 1 | ||||
Sequence: GLYKVQIGAFKVKANADSLASNAEAKGFDSIVLLKD | ||||||
Region | 184-255 | 2 X 35 AA approximate tandem repeats | ||||
Sequence: GLYKVQIGAFKVKANADSLASNAEAKGFDSIVLLKDGLYKVQIGAFSSKDNADTLAARAKNAGFDAIVILES | ||||||
Repeat | 220-255 | 2 | ||||
Sequence: GLYKVQIGAFSSKDNADTLAARAKNAGFDAIVILES |
Domain
Contains an N-terminal catalytic domain and two C-terminal tandem repeat sequences that play an important role in peptidoglycan binding.
Sequence similarities
Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length255
- Mass (Da)27,146
- Last updated1995-02-01 v1
- Checksum30C950116784FBC1
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 158 | in Ref. 5; CAA92813 | ||||
Sequence: S → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D14666 EMBL· GenBank· DDBJ | BAA03500.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL009126 EMBL· GenBank· DDBJ | CAB13625.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z68500 EMBL· GenBank· DDBJ | CAA92813.1 EMBL· GenBank· DDBJ | Genomic DNA |