P08750 (DACA_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 109.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: D-alanyl-D-alanine carboxypeptidase dacA Short name=CPase Short name=DD-carboxypeptidase Short name=DD-peptidase EC=3.4.16.4 Alternative name(s): Penicillin-binding protein 5 Short name=PBP-5 | ||||
| Gene names |
| ||||
| Organism | Bacillus subtilis | ||||
| Taxonomic identifier | 1423 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 443 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 | Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. |
| Catalytic activity | Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine. |
| Pathway | |
| Subcellular location | |
| Sequence similarities | Belongs to the peptidase S11 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis |
| Cellular component | Cell wall Secreted |
| Domain | Signal |
| Molecular function | Carboxypeptidase Hydrolase Protease |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW proteolysisInferred from electronic annotation. Source: UniProtKB-KW regulation of cell shapeInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular regionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | serine-type D-Ala-D-Ala carboxypeptidase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 31 | 31 | Ref.3 | ||||||
| Chain | 32 – 443 | 412 | D-alanyl-D-alanine carboxypeptidase dacA | PRO_0000027228 | |||||
Sites | |||||||||
| Active site | 67 | 1 | Acyl-ester intermediate Ref.6 | ||||||
| Active site | 70 | 1 | Proton acceptor By similarity | ||||||
| Active site | 131 | 1 | By similarity | ||||||
| Binding site | 258 | 1 | Substrate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 100 | 1 | E → Q AA sequence Ref.3 | ||||||
| Sequence conflict | 227 | 1 | E → Q in AAA22375. Ref.4 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin." Ogasawara N., Nakai S., Yoshikawa H. DNA Res. 1:1-14(1994) [PubMed: 7584024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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] | "Sequence of active site peptides from the penicillin-sensitive D-alanine carboxypeptidase of Bacillus subtilis. Mechanism of penicillin action and sequence homology to beta-lactamases." Waxman D.J., Strominger J.L. J. Biol. Chem. 255:3964-3976(1980) [PubMed: 6768745] [Abstract] Cited for: PROTEIN SEQUENCE OF 32-102. |
| [4] | "Reduced heat resistance of mutant spores after cloning and mutagenesis of the Bacillus subtilis gene encoding penicillin-binding protein 5." Todd J.A., Roberts A.N., Johnstone K., Piggot P.J., Winter G., Ellar D.J. J. Bacteriol. 167:257-264(1986) [PubMed: 3087956] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-443. |
| [5] | "Primary structure of the COOH-terminal membranous segment of a penicillin-sensitive enzyme purified from two Bacilli." Waxman D.J., Strominger J.L. J. Biol. Chem. 256:2067-2077(1981) [PubMed: 6780559] [Abstract] Cited for: PROTEIN SEQUENCE OF 414-443. |
| [6] | "Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases." Yocum R.R., Waxman D.J., Rasmussen J.R., Strominger J.L. Proc. Natl. Acad. Sci. U.S.A. 76:2730-2734(1979) [PubMed: 111240] [Abstract] Cited for: ACTIVE SITE SER-67. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D26185 Genomic DNA. Translation: BAA05246.1. AL009126 Genomic DNA. Translation: CAB11786.1. M13766 Genomic DNA. Translation: AAA22375.1. |
| PIR | S66040. |
| RefSeq | NP_387891.1. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | P08750. |
| SMR | P08750. Positions 36-412. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S11.001. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000000263; EBBACP00000000263; EBBACG00000000263. |
| GeneID | 940000. |
| GenomeReviews | Gene locus BSU00100 in contig AL009126_GR. |
| KEGG | bsu:BSU00100. |
| NMPDR | fig|224308.1.peg.10. |
| PATRIC | 18971479. VBIBacSub10457_0011. |
Organism-specific databases | |
| GenoList | BSU00100. [Micado] |
Phylogenomic databases | |
| GeneTree | EBGT00070000031765. |
| HOGENOM | HBG728991. |
| OMA | TMRSIGG. |
| PhylomeDB | P08750. |
| ProtClustDB | CLSK886544. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU00100-MONOMER. |
Family and domain databases | |
| InterPro | IPR012338. Beta-lactam/transpept-like. IPR015956. Peniciliin-bd_prot-assoc. IPR018044. Peptidase_S11. IPR012907. Peptidase_S11_C. IPR001967. Peptidase_S11_N. [Graphical view] |
| Gene3D | G3DSA:3.40.710.10. G3DSA:3.40.710.10. 1 hit. G3DSA:2.60.410.10. Peptidase_S11_C. 1 hit. |
| KO | K07258. |
| Pfam | PF07943. PBP5_C. 1 hit. PF00768. Peptidase_S11. 1 hit. [Graphical view] |
| PRINTS | PR00725. DADACBPTASE1. |
| SMART | SM00936. PBP5_C. 1 hit. [Graphical view] |
| SUPFAM | SSF56601. PBP_transp_fold. 1 hit. SSF69189. Peniciliin-bd_prot-assoc. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | DACA_BACSU | ||||||||
| Accession | Primary (citable) accession number: P08750 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with