Q8XD57 (SYK1_ECO57) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 79.
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: Lysine--tRNA ligase EC=6.1.1.6 Alternative name(s): Lysyl-tRNA synthetase Short name=LysRS | ||||
| Gene names |
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| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 505 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). HAMAP-Rule MF_00252 |
| Cofactor | Binds 3 magnesium ions per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | lysyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: HAMAP lysine-tRNA ligase activityInferred from electronic annotation. Source: HAMAP magnesium ion bindingInferred from electronic annotation. Source: HAMAP nucleic acid bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 505 | 504 | Lysine--tRNA ligase HAMAP-Rule MF_00252 | PRO_0000152624 | |||||
Sites | |||||||||
| Metal binding | 415 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 422 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 422 | 1 | Magnesium 2 By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG58018.1. BA000007 Genomic DNA. Translation: BAB37185.1. |
| PIR | B91099. F85944. |
| RefSeq | NP_289459.1. NC_002655.2. NP_311789.1. NC_002695.1. |
3D structure databases | |
| ProteinModelPortal | Q8XD57. |
| SMR | Q8XD57. Positions 12-503. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 155864.Z4228. |
Proteomic databases | |
| PRIDE | Q8XD57. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAG58018; AAG58018; Z4228. BAB37185; BAB37185; BAB37185. |
| GeneID | 916412. 958385. |
| KEGG | ece:Z4228. ecs:ECs3762. |
| PATRIC | 18357007. VBIEscCol44059_3682. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1190. |
| HOGENOM | HOG000236578. |
| KO | K04567. |
| OMA | FLEPECH. |
| ProtClustDB | PRK00484. |
Enzyme and pathway databases | |
| BioCyc | ECOL386585:GJFA-3729-MONOMER. |
Family and domain databases | |
| Gene3D | 2.40.50.140. 1 hit. |
| HAMAP | MF_00252. Lys_tRNA_synth_class2. |
| InterPro | IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II. IPR002313. Lys-tRNA-ligase_II. IPR018149. Lys-tRNA-synth_II_C. IPR012340. NA-bd_OB-fold. IPR004365. NA-bd_OB_tRNA-helicase. [Graphical view] |
| PANTHER | PTHR22594. PTHR22594. 1 hit. PTHR22594:SF4. PTHR22594:SF4. 1 hit. |
| Pfam | PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view] |
| PRINTS | PR00982. TRNASYNTHLYS. |
| SUPFAM | SSF50249. Nucleic_acid_OB. 1 hit. |
| TIGRFAMs | TIGR00499. lysS_bact. 1 hit. |
| PROSITE | PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYK1_ECO57 | ||||||||
| Accession | Primary (citable) accession number: Q8XD57 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
