Lysine--tRNA ligase - Escherichia coli O157:H7

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Q8XD57 (SYK1_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. 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
EC=6.1.1.6

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

Gene names

Name:	lysS
Ordered Locus Names:	Z4228, ECs3762

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
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 HAMAP MF_00252

PRO_0000152624

Sites

Metal binding

415

Magnesium 1 By similarity

Metal binding

422

Magnesium 1 By similarity

Metal binding

422

Magnesium 2 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8XD57 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CDABF71FAC12A629
Show »

FASTA

505

57,631

        10         20         30         40         50         60 
MSEQHAQGAD AVVDLNNELK TRREKLANLR EQGIAFPNDF RRDHTSDQLH AEFDGKENEE 

        70         80         90        100        110        120 
LEALNIEVAV AGRMMTRRIM GKASFVTLQD VGGRIQLYVA RDDLPEGVYN EQFKKWDLGD 

       130        140        150        160        170        180 
ILGAKGKLFK TKTGELSIHC TELRLLTKAL RPLPDKFHGL QDQEARYRQR YLDLISNDES 

       190        200        210        220        230        240 
RNTFKVRSQI LSGIRQFMVN RGFMEVETPM MQVIPGGAAA RPFITHHNAL DLDMYLRIAP 

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

       310        320        330        340        350        360 
LAQDILGKTE VTYGDVTLDF GKPFEKLTMR EAIKKYRPET DMADLDNFDS AKAIVESIGI 

       370        380        390        400        410        420 
HVEKSWGLGR IVTEIFEEVA EAHLIQPTFI TEYPAEVSPL ARRNDVNPEI TDRFEFFIGG 

       430        440        450        460        470        480 
REIGNGFSEL NDAEDQAQRF LDQVAAKDAG DDEAMFYDED YVTALEHGLP PTAGLGIGID 

       490        500 
RMVMLFTNSH TIRDVILFPA MRPVK

« 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: 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...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000025531; EBESCP00000024424; EBESCG00000024584. EBESCT00000055989; EBESCP00000053817; EBESCG00000055037.
GeneID	916412. 958385.
GenomeReviews	Gene locus Z4228 in contig AE005174_GR. Gene locus ECs3762 in contig BA000007_GR.
KEGG	ece:Z4228. ecs:ECs3762.
PATRIC	18357007. VBIEscCol44059_3682.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000009271.
HOGENOM	HBG631383.
OMA	EFTMMEI.
ProtClustDB	PRK00484.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS3762-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

SYK1_ECO57

Accession

Primary (citable) accession number: Q8XD57

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 69 of the entry and version 3 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

Sequences

References

Cross-references

Sequence databases

3D structure 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