B9DUS0 (DDL_STRU0) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 36.
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-alanine--D-alanine ligase EC=6.3.2.4 Alternative name(s): D-Ala-D-Ala ligase D-alanylalanine synthetase | ||||
| Gene names |
| ||||
| Organism | Streptococcus uberis (strain ATCC BAA-854 / 0140J) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 218495 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › ![]() |
Protein attributes
| Sequence length | 348 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Cell wall formation By similarity. |
| Catalytic activity | ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine. HAMAP-Rule MF_00047 |
| Cofactor | Binds 2 magnesium or manganese ions per subunit By similarity. |
| Pathway | Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00047 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the D-alanine--D-alanine ligase family. Contains 1 ATP-grasp domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shapeInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cell wall Inferred from electronic annotation. Source: InterPro cytoplasmInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: HAMAP D-alanine-D-alanine ligase activityInferred from electronic annotation. Source: HAMAP magnesium ion bindingInferred from electronic annotation. Source: HAMAP manganese ion bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 348 | 348 | D-alanine--D-alanine ligase HAMAP-Rule MF_00047 | PRO_1000189751 | |||||
Regions | |||||||||
| Domain | 132 – 334 | 203 | ATP-grasp | ||||||
| Nucleotide binding | 162 – 217 | 56 | ATP By similarity | ||||||
Sites | |||||||||
| Metal binding | 288 | 1 | Magnesium or manganese 1 By similarity | ||||||
| Metal binding | 301 | 1 | Magnesium or manganese 1 By similarity | ||||||
| Metal binding | 301 | 1 | Magnesium or manganese 2 By similarity | ||||||
| Metal binding | 303 | 1 | Magnesium or manganese 2 By similarity | ||||||
Sequences
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References
| [1] | "Evidence for niche adaptation in the genome of the bovine pathogen Streptococcus uberis." Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A., Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R., Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D., Parkhill J. BMC Genomics 10:54-54(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-854 / 0140J. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM946015 Genomic DNA. Translation: CAR42743.1. |
| RefSeq | YP_002562562.1. NC_012004.1. |
3D structure databases | |
| ProteinModelPortal | B9DUS0. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 218495.SUB1257. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAR42743; CAR42743; SUB1257. |
| GeneID | 7391862. |
| KEGG | sub:SUB1257. |
| PATRIC | 19808222. VBIStrUbe20775_1227. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1181. |
| HOGENOM | HOG000011593. |
| KO | K01921. |
| OMA | LLHGPFG. |
Enzyme and pathway databases | |
| UniPathway | UPA00219. |
Family and domain databases | |
| Gene3D | 3.30.1490.20. 1 hit. 3.30.470.20. 2 hits. 3.40.50.20. 1 hit. |
| HAMAP | MF_00047. Dala_Dala_lig. |
| InterPro | IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR000291. D-Ala_lig_Van_CS. IPR005905. D_ala_D_ala. IPR011095. Dala_Dala_lig_C. IPR011127. Dala_Dala_lig_N. IPR016185. PreATP-grasp_dom. [Graphical view] |
| PANTHER | PTHR23132. PTHR23132. 1 hit. |
| Pfam | PF07478. Dala_Dala_lig_C. 1 hit. PF01820. Dala_Dala_lig_N. 1 hit. [Graphical view] |
| SUPFAM | SSF52440. PreATP-grasp-like. 1 hit. |
| TIGRFAMs | TIGR01205. D_ala_D_alaTIGR. 1 hit. |
| PROSITE | PS50975. ATP_GRASP. 1 hit. PS00843. DALA_DALA_LIGASE_1. 1 hit. PS00844. DALA_DALA_LIGASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DDL_STRU0 | ||||||||
| Accession | Primary (citable) accession number: B9DUS0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
