[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0378-1119(91)90503-4; PubMed=1761227 [NCBI, ExPASy, EBI, Israel, Japan] Kong L., Fromant M., Blanquet S., Plateau P.; "Evidence for a new Escherichia coli protein resembling a lysyl-tRNA synthetase."; Gene 108:163-164(1991).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1093/nar/23.12.2105; PubMed=7610040 [NCBI, ExPASy, EBI, Israel, Japan] Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.; "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."; Nucleic Acids Res. 23:2105-2119(1995).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-152. PubMed=7037404 [NCBI, ExPASy, EBI, Israel, Japan] Cole S.T.; "Nucleotide sequence coding for the flavoprotein subunit of the fumarate reductase of Escherichia coli."; Eur. J. Biochem. 122:479-484(1982).
[6]	SIMILARITY TO CLASS-II AA-TRNA SYNTHETASES. PubMed=2668951 [NCBI, ExPASy, EBI, Israel, Japan] Gampel A., Tzagoloff A.; "Homology of aspartyl- and lysyl-tRNA synthetases."; Proc. Natl. Acad. Sci. U.S.A. 86:6023-6027(1989).

Comments

FUNCTION: Could be a lysyl-tRNA synthetase. Mutants in poxA have a reduced pyruvate oxidase activity and a reduced growth rate.
CATALYTIC ACTIVITY: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys).
INTERACTION:
P0AFG8:aceE; NbExp=1; IntAct=EBI-562598, EBI-542683;
SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X59988; CAA42604.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U14003; AAA97054.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC77115.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE78159.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J01611; AAA23436.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S56383; S56383.

RefSeq

AP_004658.1; -.
NP_418579.2; -.

3D structure databases

HSSP

P14825; 1E1O. [HSSP ENTRY / PDB]

ModBase

P0A8N7.

Protein-protein interaction databases

IntAct

P0A8N7; 3.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11211-MON; -.

Organism-specific databases

EchoBASE

EB1196; -.

EcoGene

EG11211; poxA.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0004824;	Molecular function: lysine-tRNA ligase activity (inferred from electronic annotation from HAMAP).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006430;	Biological process: lysyl-tRNA aminoacylation (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00174; -; 1.
PBIL [Tree]

InterPro

IPR004364; aa-tRNA-synt_II.
IPR006195; aa-tRNA-synth_II.
IPR004525; Lys-tRNA-synth-rel.
IPR002313; Lys-tRNA-synth_II.
Graphical view of domain structure.

PANTHER

PTHR22594; aa-tRNA-synt_II; 1.

Pfam

PF00152; tRNA-synt_2; 1.
Pfam graphical view of domain structure.

PRINTS

PR00982; TRNASYNTHLYS.

TIGRFAMs

TIGR00462; genX; 1.

PROSITE

PS50862; AA_TRNA_LIGASE_II; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

948672; -.

GenomeReviews

AP009048_GR; JW4116.
U00096_GR; b4155.

KEGG

ecj:JW4116; -.
eco:b4155; -.

Phylogenomic databases

HOGENOM

P0A8N7; -.

Genome annotation databases

CMR

P0A8N7; b4155.

Other

ProtoNet

P0A8N7.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Nucleotide-binding; Protein biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 325`	`325`	`Putative lysyl-tRNA synthetase.`	`PRO_0000152719`
`CONFLICT`	`78 78`		`E -> Q (in Ref. 5; AAA23436).`
`CONFLICT`	`144 144`		`A -> E (in Ref. 5; AAA23436).`

Sequence information

Length: 325 AA [This is the length of the unprocessed precursor]

Molecular weight: 36976 Da [This is the MW of the unprocessed precursor]

CRC64: F72B535CCA23E4CC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSETASWQPS ASIPNLLKRA AIMAEIRRFF ADRGVLEVET PCMSQATVTD IHLVPFETRF 

        70         80         90        100        110        120 
VGPGHSQGMN LWLMTSPEYH MKRLLVAGCG PVFQLCRSFR NEEMGRYHNP EFTMLEWYRP 

       130        140        150        160        170        180 
HYDMYRLMNE VDDLLQQVLD CPAAESLSYQ QAFLRYLEID PLSADKTQLR EVAAKLDLSN 

       190        200        210        220        230        240 
VADTEEDRDT LLQLLFTFGV EPNIGKEKPT FVYHFPASQA SLAQISTEDH RVAERFEVYY 

       250        260        270        280        290        300 
KGIELANGFH ELTDAREQQQ RFEQDNRKRA ARGLPQHPID QNLIEALKVG MPDCSGVALG 

       310        320 
VDRLVMLALG AETLAEVIAF SVDRA

P0A8N7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools