B7LKT3 (SYQ_ESCF3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamine--tRNA ligase
EC=6.1.1.18

Alternative name(s):
Glutaminyl-tRNA synthetase
Short name=GlnRS

Gene names

Name:	glnS
Ordered Locus Names:	EFER_2429

Organism

Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73) [Complete proteome] [HAMAP]

Taxonomic identifier

585054 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia fergusonii

Protein attributes

Sequence length	554 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln). HAMAP-Rule MF_00126
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
Gene Ontology (GO)
Biological_process	glutaminyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro 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 glutamine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 554	554	Glutamine--tRNA ligase HAMAP-Rule MF_00126		PRO_1000199101
Regions
	Motif	34 – 44	11	"HIGH" region HAMAP-Rule MF_00126
	Motif	268 – 272	5	"KMSKS" region HAMAP-Rule MF_00126
Sites
	Binding site	271	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7LKT3 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: D00566FAA9DAA3C3	FASTA	554	63,508
	10 20 30 40 50 60 MSEAEARPTN FIRQIIDEDL ASGKHTTVHT RFPPEPNGYL HIGHAKSICL NFGIAQDYKG 70 80 90 100 110 120 QCNLRFDDTN PVKEDIEYVE SIKNDVEWLG FHWSGNVRYS SDYFDQLHAY AIELINKGLA 130 140 150 160 170 180 YVDELTPEQI REYRGTLTQP GKNSPYRDRS VEENLALFEK MRTGGFEEGK ACLRAKIDMA 190 200 210 220 230 240 SPFIVMRDPV LYRIKFAEHH QTGNKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL 250 260 270 280 290 300 YDWVLDNITI PVHPRQYEFS RLNLEYTVMS KRKLNLLVTD KHVEGWDDPR MPTISGLRRR 310 320 330 340 350 360 GYTAASIREF CKRIGVTKQD NTIEMASLES CIREDLNENA PRAMAVIDPV KLVIENYQGE 370 380 390 400 410 420 GEMVTMPNHP NKPEMGSRQV PFSGEIWIDR ADFREEANKQ YKRLVLGKEV RLRNAYVIKA 430 440 450 460 470 480 ERVEKDAEGN ITTIFCTYDA DTLSKDPADG RKVKGVIHWV SAAHALPVEI RLYDRLFSVP 490 500 510 520 530 540 NPGAADDFLS VINPESLVIK QGFAEPSLKD AVAGKAFQFE REGYFCLDSR HSTAEKPVFN 550 RTVGLRDTWA KVGE

References

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35469 / DSM 13698 / CDC 0568-73.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928158 Genomic DNA. Translation: CAQ89928.1.
RefSeq	YP_002383543.1. NC_011740.1.
3D structure databases
ProteinModelPortal	B7LKT3.
SMR	B7LKT3. Positions 9-548.
ModBase	Search...
Protein-protein interaction databases
STRING	585054.EFER_2429.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAQ89928; CAQ89928; EFER_2429.
GeneID	7122072.
KEGG	efe:EFER_2429.
PATRIC	32129218. VBIEscFer122920_2345.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000259232.
KO	K01886.
ProtClustDB	PRK05347.
Enzyme and pathway databases
BioCyc	EFER585054:GJJM-2428-MONOMER.
Family and domain databases
Gene3D	1.10.1160.10. 1 hit. 2.40.240.10. 2 hits. 3.40.50.620. 2 hits.
HAMAP	MF_00126. Gln_tRNA_synth.
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR004514. Gln-tRNA-synth_Ib. IPR022861. Gln_tRNA_ligase_bac. IPR000924. Glu/Gln-tRNA-synth_Ib. IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl. IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom. IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd. IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl. IPR011035. Ribosomal_L25/Gln-tRNA_synth. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
PANTHER	PTHR10119. PTHR10119. 1 hit.
Pfam	PF00749. tRNA-synt_1c. 1 hit. PF03950. tRNA-synt_1c_C. 1 hit. [Graphical view]
PRINTS	PR00987. TRNASYNTHGLU.
SUPFAM	SSF50715. Ribosomal_L25rel. 1 hit.
TIGRFAMs	TIGR00440. glnS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYQ_ESCF3

Accession

Primary (citable) accession number: B7LKT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 10, 2009
Last modified:	May 1, 2013
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program