O52914 (SYE2_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate--tRNA ligase 2
EC=6.1.1.17

Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2

Gene names

Name:	gltX2
Synonyms:	gltX1
Ordered Locus Names:	Cj1288c

Organism

Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]

Taxonomic identifier

192222 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter › Campylobacter jejuni › Campylobacter jejuni subsp. jejuni

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity. HAMAP-Rule MF_00022
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutamyl-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 glutamate-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP tRNA 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
	Chain	1 – 463	463	Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022		PRO_0000119531
Regions
	Motif	11 – 21	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	240 – 244	5	"KMSKS" region HAMAP-Rule MF_00022
Sites
	Binding site	243	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	O52914 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: D60A0032963E6BED	FASTA	463	53,059
	10 20 30 40 50 60 MHEKLTTRFA PSPTGYLHIG GLRTALYNYL YARKNGGNFL LRIEDTDLKR NSKEATKAII 70 80 90 100 110 120 EAFKWCGLEH DGEVTYQSER FDLYKEYVKK LLDEGKAYYC YMSKEELEEL RAKQEAAKER 130 140 150 160 170 180 PRYDGRYREF TGTPPQGIEP VVRIKAPQSG EIVFEDGVKG EVRFKAEDIM DDFIIARSDG 190 200 210 220 230 240 TPTYNFTVVI DDALMGVSDV IRGDDHLSNT PKQIVLYEAL GFKIPKFFHV AMIHGEDGKK 250 260 270 280 290 300 LSKRHGATDV MEYKEMGILP QALLNFLVRL GWSHGDDEVF SLEDLKKLFD PYHINKSASC 310 320 330 340 350 360 YNAKKLEWLN AHYIKTLPFE EINRQLKDLG FDLSVYEKAG FLLDLLRERA KTLHDIINGA 370 380 390 400 410 420 KSIVNAPQNY DENAVQKFVN KNNLELLQAF ANTLKDQKTG KDFEDFTNDF LEKKEAKLKD 430 440 450 460 LAQPIRIALT GSAVSPSIFE VLEFLGVDEC KKRIDNFLKV RGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168.
[2]	Woesten M.M.S.M., Boeve M., Koot M.G.A., Nuenen A.C., van der Zeijst B.A.M. Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82. Strain: 129108.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL111168 Genomic DNA. Translation: CAL35402.1. AJ002027 Genomic DNA. Translation: CAA05150.1.
PIR	A81337.
RefSeq	YP_002344678.1. NC_002163.1.
3D structure databases
ProteinModelPortal	O52914.
ModBase	Search...
Protein-protein interaction databases
IntAct	O52914. 32 interactions.
STRING	192222.Cj1288c.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAL35402; CAL35402; Cj1288c.
GeneID	905580.
KEGG	cje:Cj1288c.
PATRIC	20059540. VBICamJej33762_1270.
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252722.
KO	K01885.
OMA	HLANTID.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	CJEJ192222:GJTS-1261-MONOMER.
Family and domain databases
Gene3D	1.10.10.350. 1 hit. 1.10.1160.10. 1 hit. 3.40.50.620. 2 hits.
HAMAP	MF_00022_B. Glu_tRNA_synth_B.
InterPro	IPR008925. aa-tRNA-synth_I_codon-bd. IPR020751. aa-tRNA-synth_I_codon-bd_sub2. IPR001412. aa-tRNA-synth_I_CS. IPR004527. Glu-tRNA-ligase_Ib_bac/mito. IPR000924. Glu/Gln-tRNA-synth_Ib. IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl. IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
PANTHER	PTHR10119. PTHR10119. 1 hit. PTHR10119:SF1. PTHR10119:SF1. 1 hit.
Pfam	PF00749. tRNA-synt_1c. 1 hit. [Graphical view]
PRINTS	PR00987. TRNASYNTHGLU.
SUPFAM	SSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMs	TIGR00464. gltX_bact. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYE2_CAMJE

Accession

Primary (citable) accession number: O52914
Secondary accession number(s): Q0P8W9, Q9PN11

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program