A7H3M3 (SYE2_CAMJD) 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
Ordered Locus Names:	JJD26997_0994

Organism

Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / 269.97) [Complete proteome] [HAMAP]

Taxonomic identifier

360109 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	431 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 MF_00022_B
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B
Subunit structure	Monomer By similarity. HAMAP MF_00022_B
Subcellular location	Cytoplasm By similarity HAMAP MF_00022_B.
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
Gene Ontology (GO)
Biological process	glutamyl-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 glutamate-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 431	431	Glutamate--tRNA ligase 2 HAMAP MF_00022_B		PRO_0000367639
Regions
	Motif	6 – 16	11	"HIGH" region HAMAP MF_00022_B
	Motif	235 – 239	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Binding site	238	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7H3M3 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: D0F71C895AE13B71	FASTA	431	50,255
	10 20 30 40 50 60 MYRFAPSPTG DMHIGNLRAA IFNYICARQK NMDFILRIED TDKSRNIKGK EEEIKEILNL 70 80 90 100 110 120 FGISWQHYYI QSENLKFHRQ MALKLVSEKK AFACFCTEEE LEAKKELAKK QGKAYRYDGT 130 140 150 160 170 180 CEKLADIDVL ECEKSFVIRL KKPTHTMKFT DFIKGELSFE PENIDSFVIM RTDKTPTYNF 190 200 210 220 230 240 ACAVDDMLEN VTCIIRGEDH VSNTPKQEHI RASLGYDKAM TYAHLPIILN EEGVKMSKRE 250 260 270 280 290 300 AHSSVKWLLE SGILPSAITN YLIMLGNKTP YEIFTLEEAI KWFDISKVSK APARFDLKKL 310 320 330 340 350 360 LQINREHIKM IKDDELNKIL DLNKDLAQLA KFYTQEASTI KELKEKMRAI FNTKDFGEFE 370 380 390 400 410 420 TECKILKELL KDIELFENYE DFKNKLLNKS SLKGKKFFMP LRIILTGNIH GPELSDLYPY 430 IKNFIHELAR I

References

[1]

"Complete genome sequence of Campylobacter jejuni subsp doylei 269.97 isolated from human blood." Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E. Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-1458 / RM4099 / 269.97.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000768 Genomic DNA. Translation: ABS44636.1.
RefSeq	YP_001398103.1. NC_009707.1.
3D structure databases
ProteinModelPortal	A7H3M3.
ModBase	Search...
Protein-protein interaction databases
STRING	A7H3M3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5388693.
GenomeReviews	Gene locus JJD26997_0994 in contig CP000768_GR.
KEGG	cjd:JJD26997_0994.
PATRIC	20047649. VBICamJej122183_0996.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	SVKWLLN.
ProtClustDB	PRK12410.
Enzyme and pathway databases
BioCyc	CJEJ360109:JJD26997_0994-MONOMER.
Family and domain databases
HAMAP	MF_00022_B. Glu_tRNA_synth_B. [Tree]
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-synth_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]
Gene3D	G3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits. G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KO	K01885.
PANTHER	PTHR10119. Glu_tRNA-synt_1c. 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_CAMJD

Accession

Primary (citable) accession number: A7H3M3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	September 11, 2007
Last modified:	January 25, 2012
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program