Reviewed,
UniProtKB/Swiss-Prot Q03523 (MURE_BACSU)
Last modified
February 9, 2010.
Version 83.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase EC=6.3.2.13 Alternative name(s): UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase Meso-diaminopimelate-adding enzyme Meso-A2pm-adding enzyme UDP-N-acetylmuramyl-tripeptide synthetase UDP-MurNAc-tripeptide synthetase | ||||
| Gene names |
| ||||
| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1423 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 494 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan By similarity. HAMAP MF_00208 |
| Catalytic activity | ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate. HAMAP MF_00208 |
| Pathway | Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00208 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00208. |
| Post-translational modification | Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity. HAMAP MF_00208 |
| Sequence similarities | Belongs to the murCDEF family. MurE subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell divisionInferred from electronic annotation. Source: UniProtKB-KW cellular cell wall organizationInferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic processInferred from electronic annotation. Source: HAMAP regulation of cell shapeInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: HAMAP UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 494 | 494 | UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208 | PRO_0000101866 | |||||
Regions | |||||||||
| Nucleotide binding | 109 – 115 | 7 | ATP Potential | ||||||
| Region | 151 – 152 | 2 | UDP-MurNAc-L-Ala-D-Glu binding By similarity | ||||||
| Region | 408 – 411 | 4 | Meso-diaminopimelate binding By similarity | ||||||
| Motif | 408 – 411 | 4 | Meso-diaminopimelate recognition motif HAMAP MF_00208 | ||||||
Sites | |||||||||
| Binding site | 31 | 1 | UDP-MurNAc-L-Ala-D-Glu By similarity | ||||||
| Binding site | 150 | 1 | UDP-MurNAc-L-Ala-D-Glu By similarity | ||||||
| Binding site | 178 | 1 | UDP-MurNAc-L-Ala-D-Glu By similarity | ||||||
| Binding site | 186 | 1 | UDP-MurNAc-L-Ala-D-Glu By similarity | ||||||
| Binding site | 384 | 1 | Meso-diaminopimelate By similarity | ||||||
| Binding site | 458 | 1 | Meso-diaminopimelate; via carbonyl oxygen By similarity | ||||||
| Binding site | 462 | 1 | Meso-diaminopimelate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 218 | 1 | N6-carboxylysine By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "DNA sequence of the murE-murD region of Bacillus subtilis 168." Daniel R.A., Errington J. J. Gen. Microbiol. 139:361-370(1993) [PubMed: 8436954] [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] | "The Bacillus subtilis spoVD gene encodes a mother-cell-specific penicillin-binding protein required for spore morphogenesis." Daniel R.A., Drake S., Buchanan C.E., Scholle R., Errington J. J. Mol. Biol. 235:209-220(1994) [PubMed: 8289242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16. Strain: 168. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z15056 Genomic DNA. Translation: CAA78767.1. AL009126 Genomic DNA. Translation: CAB13391.1. Z25865 Genomic DNA. Translation: CAA81086.1. |
| PIR | B47691. |
| RefSeq | NP_389401.1. |
3D structure databases | |
| SMR | Q03523. Positions 13-490. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 937567. |
| GenomeReviews | Gene locus BSU15180 in contig AL009126_GR. |
| KEGG | bsu:BSU15180. |
| NMPDR | fig|224308.1.peg.1520. |
Organism-specific databases | |
| SubtiList | BG10223. murE. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG602753. |
| OMA | EHLDFHG. |
| PhylomeDB | Q03523. |
Enzyme and pathway databases | |
| BRENDA | 6.3.2.13. 150. |
Family and domain databases | |
| HAMAP | MF_00208. MurE. [Tree] |
| InterPro | IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR000713. Mur_ligase_N. IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase. [Graphical view] |
| Gene3D | G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit. |
| Pfam | PF01225. Mur_ligase. 1 hit. PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01085. murE. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | MURE_BACSU | ||||||||
| Accession | Primary (citable) accession number: Q03523 | ||||||||
| 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 |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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