Q9PP78 (SYE1_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate--tRNA ligase 1
EC=6.1.1.17

Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1

Gene names

Name:	gltX1
Synonyms:	gltX2
Ordered Locus Names:	Cj0845c

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	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-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 – 431	431	Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022		PRO_0000119532
Regions
	Motif	6 – 16	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	235 – 239	5	"KMSKS" region HAMAP-Rule MF_00022
Sites
	Binding site	238	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9PP78 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 480A5720D24F4509	FASTA	431	50,191
	10 20 30 40 50 60 MYRFAPSPTG DMHIGNLRAA IFNYICARQK NMDFILRIED TDKARNIAGK EEEIKEILNL 70 80 90 100 110 120 FSISWQHYYI QSENLKFHRQ MALKLVSEKK AFACFCTEEE LEAKKELAKK QGKAYRYDGT 130 140 150 160 170 180 CEKLADIDVL ECEKPFVIRL KKPTHTMKFT DFIKGELSFE PENIDSFVIM RTDKTPTYNF 190 200 210 220 230 240 ACAVDDMLEN VTCIIRGEDH VSNTPKQEHI RASLGYNKAM TYAHLPIILN EEGVKMSKRE 250 260 270 280 290 300 AHSSVKWLLE SGILPSAIAN YLIMLGNKTP CEIFTLEEAI KWFDISKVSK APARFDLKKL 310 320 330 340 350 360 LQINREHIKM IKDDELNKIL DLNKDLAQLA KFYTQETSTI KELKEKMQAI FNAKDFGEFE 370 380 390 400 410 420 TEYKILKELL KDIELFENYE DFKNELLNKS NLKGKKFFMP LRIILTGNIH GPELSDLYPY 430 IKNFIHELAR I

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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL111168 Genomic DNA. Translation: CAL34973.1.
PIR	E81357.
RefSeq	YP_002344252.1. NC_002163.1.
3D structure databases
ProteinModelPortal	Q9PP78.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9PP78. 1 interaction.
STRING	192222.Cj0845c.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAL34973; CAL34973; Cj0845c.
GeneID	905144.
KEGG	cje:Cj0845c.
PATRIC	20058638. VBICamJej33762_0833.
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252720.
KO	K01885.
OMA	SVKWLLN.
ProtClustDB	PRK12410.
Enzyme and pathway databases
BioCyc	CJEJ192222:GJTS-819-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

SYE1_CAMJE

Accession

Primary (citable) accession number: Q9PP78
Secondary accession number(s): Q0PA45

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program