Q0T8S7 (LPLA_ECOL5) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 41.
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: Lipoate-protein ligase A EC=2.7.7.63 Alternative name(s): Lipoate--protein ligase | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 362663 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 338 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes By similarity. HAMAP MF_01602 |
| Catalytic activity | ATP + lipoate = diphosphate + lipoyl-AMP. HAMAP MF_01602 Lipoyl-AMP + protein = protein N(6)-(lipoyl)lysine + AMP. HAMAP MF_01602 |
| Pathway | Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2. HAMAP MF_01602 |
| Subunit structure | Monomer By similarity. HAMAP MF_01602 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_01602. |
| Miscellaneous | In the transfer reaction, the free carboxyl group of lipoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes By similarity. HAMAP MF_01602 |
| Sequence similarities | Belongs to the lplA family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | peptidyl-lysine lipoylation Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW lipoate-protein ligase activityInferred from electronic annotation. Source: InterPro transferase activityInferred 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 – 338 | 338 | Lipoate-protein ligase A HAMAP MF_01602 | PRO_1000069380 | |||||
Regions | |||||||||
| Nucleotide binding | 76 – 79 | 4 | ATP By similarity | ||||||
Sites | |||||||||
| Binding site | 71 | 1 | ATP By similarity | ||||||
| Binding site | 134 | 1 | ATP By similarity | ||||||
| Binding site | 134 | 1 | Lipoate By similarity | ||||||
Sequences
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References
| [1] | "Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536." Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J. Mol. Microbiol. 61:584-595(2006) [PubMed: 16879640] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 536 / UPEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000247 Genomic DNA. Translation: ABG72652.1. |
| RefSeq | YP_672553.1. NC_008253.1. |
3D structure databases | |
| ProteinModelPortal | Q0T8S7. |
| SMR | Q0T8S7. Positions 2-338. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q0T8S7. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000046702; EBESCP00000044891; EBESCG00000045752. |
| GeneID | 4189671. |
| GenomeReviews | Gene locus ECP_4770 in contig CP000247_GR. |
| KEGG | ecp:ECP_4770. |
| NMPDR | fig|340197.3.peg.3272. |
| PATRIC | 18200367. VBIEscCol77757_4754. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0095. |
| GeneTree | EBGT00050000010598. |
| HOGENOM | HBG715377. |
| OMA | YDRMENL. |
| PhylomeDB | Q0T8S7. |
| ProtClustDB | PRK03822. |
Enzyme and pathway databases | |
| BioCyc | ECOL362663:ECP_4770-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01602. LplA. [Tree] |
| InterPro | IPR004143. BPL_LipA_LipB. IPR005107. CO_DH_flav_C. IPR023741. Lipoate_ligase_A. IPR019491. Lipoate_protein_ligase_C. IPR004562. LipoylTrfase_LipoateP_Ligase. [Graphical view] |
| Gene3D | G3DSA:3.30.390.50. CO_DH_flav_C. 1 hit. |
| KO | K03800. |
| Pfam | PF03099. BPL_LplA_LipB. 1 hit. PF10437. Lip_prot_lig_C. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00545. Lipoyltrans. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | LPLA_ECOL5 | ||||||||
| Accession | Primary (citable) accession number: Q0T8S7 | ||||||||
| 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 |

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