A7I338 (SYE2_CAMHC) 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:	CHAB381_1380

Organism

Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A) [Complete proteome] [HAMAP]

Taxonomic identifier

360107 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	433 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 – 433	433	Glutamate--tRNA ligase 2 HAMAP MF_00022_B		PRO_0000367637
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)
	A7I338 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: 2F8E4B56B734C9AD	FASTA	433	49,568
	10 20 30 40 50 60 MYRFAPSPTG DMHIGNLRAA IFNYICSLQD KSGFILRIED TDTARNISGK GEEIKEILKQ 70 80 90 100 110 120 FGIKWDKLYI QSENLKFHRE LASKLLNDKK AFCCFCSEEE LAAKKAAAKK AGVAYRYDGT 130 140 150 160 170 180 CEKLSDLEVL NCEKPFVIRM KKPNRILKFN DLIKGEIGFE PENIDSFVIM RVDKTPTYNF 190 200 210 220 230 240 ACAVDDMLEG VTCVIRGEDH VSNTPKQNWI RECLGYTEEI SYAHLPIILN EDGKKMSKRE 250 260 270 280 290 300 NSSSVKWLLQ SGYLPEAIAN YLILLGNKTP CEVFTLDEAV EWFDISKISK NPAKFDISKL 310 320 330 340 350 360 AFLNREHIKR ADSARLVEVF GLDESFSELI KFYTQEASLV GEIKEKIKSI FSKKEIPAEF 370 380 390 400 410 420 AENVKILKDE ILKIKELPEN FENFKEILTK ATNLKGKNFF MPLRILLTGA NHGPELKELY 430 PLLRSQIKRI VNL

References

[1]

"Complete genome sequence of Campylobacter hominis ATCC BAA-381, a commensal isolated from the human gastrointestinal tract." Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Nelson K.E. Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000776 Genomic DNA. Translation: ABS51058.1.
RefSeq	YP_001406929.1. NC_009714.1.
3D structure databases
ProteinModelPortal	A7I338.
ModBase	Search...
Protein-protein interaction databases
STRING	A7I338.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5408726.
GenomeReviews	Gene locus CHAB381_1380 in contig CP000776_GR.
KEGG	cha:CHAB381_1380.
NMPDR	fig|360107.5.peg.1359.
PATRIC	20040876. VBICamHom81367_1332.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HBG628189.
OMA	VAYRYDG.
ProtClustDB	PRK12410.
Enzyme and pathway databases
BioCyc	CHOM360107:CHAB381_1380-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_CAMHC

Accession

Primary (citable) accession number: A7I338

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	September 11, 2007
Last modified:	January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program