Lysine--tRNA ligase, heat inducible - Escherichia coli O157:H7

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P0A8N6 (SYK2_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Lysine--tRNA ligase, heat inducible
EC=6.1.1.6

Alternative name(s):
Lysyl-tRNA synthetase
Short name=LysRS

Gene names

Name:	lysU
Ordered Locus Names:	Z5732, ECs5111

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 MF_00252
Cofactor	Binds 3 magnesium ions per subunit By similarity. HAMAP MF_00252
Subunit structure	Homodimer By similarity. HAMAP MF_00252
Subcellular location	Cytoplasm HAMAP MF_00252.
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
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	lysyl-tRNA aminoacylation 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 lysine-tRNA ligase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid binding Inferred 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

Removed By similarity

Chain

2 – 505

504

Lysine--tRNA ligase, heat inducible HAMAP MF_00252

PRO_0000152628

Sites

Metal binding

415

Magnesium 1 By similarity

Metal binding

422

Magnesium 1 By similarity

Metal binding

422

Magnesium 2 By similarity

Amino acid modifications

Modified residue

114

N6-acetyllysine By similarity

Modified residue

156

N6-acetyllysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P0A8N6 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 547415F5875396E0
Show »

FASTA

505

57,827

        10         20         30         40         50         60 
MSEQETRGAN EAIDFNDELR NRREKLAALR QQGVAFPNDF RRDHTSDQLH EEFDAKDNQE 

        70         80         90        100        110        120 
LESLNIEVSV AGRMMTRRIM GKASFVTLQD VGGRIQLYVA RDSLPEGVYN DQFKKWDLGD 

       130        140        150        160        170        180 
IIGARGTLFK TQTGELSIHC TELRLLTKAL RPLPDKFHGL QDQEVRYRQR YLDLIANDKS 

       190        200        210        220        230        240 
RQTFVVRSKI LAAIRQFMVA RGFMEVETPM MQVIPGGASA RPFITHHNAL DLDMYLRIAP 

       250        260        270        280        290        300 
ELYLKRLVVG GFERVFEINR NFRNEGISVR HNPEFTMMEL YMAYADYHDL IELTESLFRT 

       310        320        330        340        350        360 
LAQEVLGTTK VTYGEHVFDF GKPFEKLTMR EAIKKYRPET DMADLDNFDA AKALAESIGI 

       370        380        390        400        410        420 
TVEKSWGLGR IVTEIFDEVA EAHLIQPTFI TEYPAEVSPL ARRNDVNPEI TDRFEFFIGG 

       430        440        450        460        470        480 
REIGNGFSEL NDAEDQAERF QEQVNAKAAG DDEAMFYDED YVTALEYGLP PTAGLGIGID 

       490        500 
RMIMLFTNSH TIRDVILFPA MRPQK

« Hide

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: 11206551] [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. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG59329.1. BA000007 Genomic DNA. Translation: BAB38534.1.
PIR	E86108. G91267.
RefSeq	NP_290763.1. NC_002655.2. NP_313138.1. NC_002695.1.
3D structure databases
ProteinModelPortal	P0A8N6.
SMR	P0A8N6. Positions 12-503.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1219482.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000027520; EBESCP00000026413; EBESCG00000026572. EBESCT00000059201; EBESCP00000057029; EBESCG00000058249.
GeneID	914181. 959994.
GenomeReviews	Gene locus Z5732 in contig AE005174_GR. Gene locus ECs5111 in contig BA000007_GR.
KEGG	ece:Z5732. ecs:ECs5111.
PATRIC	18359835. VBIEscCol44059_5054.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000009271.
HOGENOM	HBG631383.
OMA	AYSDYES.
ProtClustDB	PRK12445.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS5111-MONOMER.
Family and domain databases
HAMAP	MF_00252. Lys_tRNA_synth_class2. [Tree]
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II. IPR002313. Lys-tRNA-synth_II. IPR018149. Lys-tRNA-synth_II_C. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR004365. NA-bd_OB_tRNA-helicase. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KO	K04567.
PANTHER	PTHR22594. aa-tRNA-synt_II. 1 hit. PTHR22594:SF4. tRNA-synt_lys_2. 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

SYK2_ECO57

Accession

Primary (citable) accession number: P0A8N6
Secondary accession number(s): P14825

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 55 of the entry and version 2 of the sequence. [Complete history]

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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents