Q8FKE3 (DDLA_ECOL6) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 65.
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 A EC=6.3.2.4 Alternative name(s): D-Ala-D-Ala ligase A D-alanylalanine synthetase A | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O6 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 217992 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 364 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Cell wall formation By similarity. HAMAP MF_00047 |
| Catalytic activity | ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine. HAMAP MF_00047 |
| Cofactor | Binds 2 magnesium or manganese ions per subunit By similarity. |
| Pathway | Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00047 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00047. |
| 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 | cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic processInferred 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: InterPro cytoplasmInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW D-alanine-D-alanine ligase activityInferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 364 | 364 | D-alanine--D-alanine ligase A HAMAP MF_00047 | PRO_0000177817 | |||||
Regions | |||||||||
| Domain | 145 – 348 | 204 | ATP-grasp | ||||||
| Nucleotide binding | 175 – 230 | 56 | ATP By similarity | ||||||
Sites | |||||||||
| Metal binding | 302 | 1 | Magnesium or manganese 1 By similarity | ||||||
| Metal binding | 315 | 1 | Magnesium or manganese 1 By similarity | ||||||
| Metal binding | 315 | 1 | Magnesium or manganese 2 By similarity | ||||||
| Metal binding | 317 | 1 | Magnesium or manganese 2 By similarity | ||||||
Sequences
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References
| [1] | "Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014075 Genomic DNA. Translation: AAN78965.1. |
| RefSeq | NP_752421.1. NC_004431.1. |
3D structure databases | |
| ProteinModelPortal | Q8FKE3. |
| SMR | Q8FKE3. Positions 3-363. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000041306; EBESCP00000039655; EBESCG00000040356. |
| GeneID | 1036174. |
| GenomeReviews | Gene locus c0487 in contig AE014075_GR. |
| KEGG | ecc:c0487. |
| PATRIC | 18279020. VBIEscCol75197_0455. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000009081. |
| HOGENOM | HBG427092. |
| OMA | LLHGPFG. |
| PhylomeDB | Q8FKE3. |
| ProtClustDB | PRK01966. |
Family and domain databases | |
| HAMAP | MF_00047. Dala_Dala_lig. [Tree] |
| 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. IPR013817. Pre-ATP_grasp. IPR016185. PreATP-grasp-like. [Graphical view] |
| Gene3D | G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit. |
| KO | K01921. |
| 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 | DDLA_ECOL6 | ||||||||
| Accession | Primary (citable) accession number: Q8FKE3 | ||||||||
| 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