Reviewed,
UniProtKB/Swiss-Prot Q06320 (CWLC_BACSU)
Last modified
January 19, 2010.
Version 67.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Sporulation-specific N-acetylmuramoyl-L-alanine amidase EC=3.5.1.28 Alternative name(s): Cell wall hydrolase Autolysin | ||||
| Gene names |
| ||||
| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1423 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 255 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| 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. Ref.4 Ref.6 |
| Catalytic activity | Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. |
| Cofactor | Zinc Probable. Ref.7 |
| Enzyme regulation | Inhibited by EDTA. Ref.6 |
| Subcellular location | Secreted › cell wall. Note: Is associated with the mother cell wall of sporulating cells. Ref.4 |
| Induction | |
| Domain | Contains an N-terminal catalytic domain and two C-terminal tandem repeat sequences that play an important role in peptidoglycan binding. Ref.8 |
| Sequence similarities | Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family. |
| Biophysicochemical properties | pH dependence: Optimum pH is 8.5-9.5. Temperature dependence: Optimum temperature is 60 degrees Celsius. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||
Molecule processing | ||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.4 | |||||||||||||||||
| Chain | 2 – 255 | 254 | Sporulation-specific N-acetylmuramoyl-L-alanine amidase | PRO_0000164418 | ||||||||||||||||
Regions | ||||||||||||||||||||
| Repeat | 184 – 219 | 36 | 1 | |||||||||||||||||
| Repeat | 220 – 255 | 36 | 2 | |||||||||||||||||
| Region | 184 – 255 | 72 | 2 X 35 AA approximate tandem repeats | |||||||||||||||||
Sites | ||||||||||||||||||||
| Active site | 141 | 1 | Potential | |||||||||||||||||
| Metal binding | 10 | 1 | Zinc Potential | |||||||||||||||||
| Metal binding | 24 | 1 | Zinc Potential | |||||||||||||||||
| Metal binding | 79 | 1 | Zinc Potential | |||||||||||||||||
Experimental info | ||||||||||||||||||||
| Mutagenesis | 10 | 1 | H → Q: 23% of wild-type activity. Ref.7 | |||||||||||||||||
| Mutagenesis | 24 | 1 | E → A, Q or S: Loss of activity. Ref.7 | |||||||||||||||||
| Mutagenesis | 55 | 1 | D → V: Loss of activity. Ref.7 | |||||||||||||||||
| Mutagenesis | 79 | 1 | H → L: Loss of activity. Ref.7 | |||||||||||||||||
| Mutagenesis | 79 | 1 | H → Q: 15% of wild-type activity. Ref.7 | |||||||||||||||||
| Mutagenesis | 81 | 1 | N → I: Loss of activity. Ref.7 | |||||||||||||||||
| Mutagenesis | 141 | 1 | E → Q or V: Loss of activity. Ref.7 | |||||||||||||||||
| Sequence conflict | 158 | 1 | S → T in CAA92813. Ref.5 | |||||||||||||||||
Secondary structure | ||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||
| Beta strand | 185 – 194 | 10 | ||||||||||||||||||
| Helix | 196 – 209 | 14 | ||||||||||||||||||
| Beta strand | 213 – 218 | 6 | ||||||||||||||||||
| Beta strand | 221 – 231 | 11 | ||||||||||||||||||
| Helix | 232 – 245 | 14 | ||||||||||||||||||
| Beta strand | 250 – 254 | 5 | ||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular cloning of a sporulation-specific cell wall hydrolase gene of Bacillus subtilis." Kuroda A., Asami Y., Sekiguchi J. J. Bacteriol. 175:6260-6268(1993) [PubMed: 8407798] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION. Strain: 168. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 158. |
| [4] | "Characterization of the involvement of two compensatory autolysins in mother cell lysis during sporulation of Bacillus subtilis 168." Smith T.J., Foster S.J. J. Bacteriol. 177:3855-3862(1995) [PubMed: 7601853] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11, FUNCTION, CHARACTERIZATION, SUBCELLULAR LOCATION. Strain: 168. |
| [5] | Scotti C., Valbuzzi A., Perego M., Galizzi A., Albertini A.M. Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 115-255. Strain: 168. |
| [6] | "Overexpression, purification, and characterization of Bacillus subtilis N-acetylmuramoyl-L-alanine amidase CwlC." Shida T., Hattori H., Ise F., Sekiguchi J. Biosci. Biotechnol. Biochem. 64:1522-1525(2000) [PubMed: 10945275] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION. |
| [7] | "Mutational analysis of catalytic sites of the cell wall lytic N-acetylmuramoyl-L-alanine amidases CwlC and CwlV." Shida T., Hattori H., Ise F., Sekiguchi J. J. Biol. Chem. 276:28140-28146(2001) [PubMed: 11375403] [Abstract] Cited for: COFACTOR, MUTAGENESIS OF HIS-10; GLU-24; ASP-55; HIS-79; ASN-81 AND GLU-141. |
| [8] | "Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR." Mishima M., Shida T., Yabuki K., Kato K., Sekiguchi J., Kojima C. Biochemistry 44:10153-10163(2005) [PubMed: 16042392] [Abstract] Cited for: STRUCTURE BY NMR OF 177-255, DOMAIN. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | D14666 Genomic DNA. Translation: BAA03500.1. AL009126 Genomic DNA. Translation: CAB13625.2. Z68500 Genomic DNA. Translation: CAA92813.1. | ||||||||||||
| PIR | A36935. | ||||||||||||
| RefSeq | NP_389623.2. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| SMR | Q06320. Positions 1-178. | ||||||||||||
| ModBase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 940088. | ||||||||||||
| GenomeReviews | Gene locus BSU17410 in contig AL009126_GR. | ||||||||||||
| KEGG | bsu:BSU17410. | ||||||||||||
Organism-specific databases | |||||||||||||
| SubtiList | BG10825. cwlC. [Micado] | ||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | HBG656726. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 3.5.1.28. 150. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR002508. CW_Hdrlase/autolysin_cat. IPR007730. Sporulation_related_dom. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.40.630.40. Cell_wall_OHase/autolysin_cat. 1 hit. | ||||||||||||
| Pfam | PF01520. Amidase_3. 1 hit. PF05036. SPOR. 1 hit. [Graphical view] | ||||||||||||
| SMART | SM00646. Ami_3. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | CWLC_BACSU | ||||||||
| Accession | Primary (citable) accession number: Q06320 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


