Q0SNE1 (SYE_BORAP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate--tRNA ligase
EC=6.1.1.17

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

Gene names

Name:	gltX
Ordered Locus Names:	BAPKO_0381, BafPKo_0371

Organism

Borrelia afzelii (strain PKo) [Complete proteome] [HAMAP]

Taxonomic identifier

390236 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Spirochaetes › Spirochaetia › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group › Borrelia afzelii

Protein attributes

Sequence length	490 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. HAMAP-Rule MF_00022
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00022.
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: 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 – 490	490	Glutamate--tRNA ligase HAMAP-Rule MF_00022		PRO_1000001875
Regions
	Motif	9 – 19	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	251 – 255	5	"KMSKS" region HAMAP-Rule MF_00022
Sites
	Binding site	254	1	ATP By similarity
Experimental info
	Sequence conflict	479	1	N → I in AEL69597. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q0SNE1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: A4441D298C9F7779	FASTA	490	56,815
	10 20 30 40 50 60 MGIRVRYAPS PTGLQHIGGI RTALFNYFFA KSCGGKFLLR IEDTDQSRYF SEAENDLYSS 70 80 90 100 110 120 LKWLGISFDE GPVVGGDYAP YVQSQRSAIY KRYAEYLIES GHAYYCYCSP ERLERIKKIQ 130 140 150 160 170 180 NINKMPPGYD RHCRNLSDEE IENVLIKKIK PVVRFKIPLE GDTSFDDVLL GKITWSNKDI 190 200 210 220 230 240 SPDPVILKSD GLPTYHLANV VDDYLMKITH VLRAQEWVSS GPLHTLLYKA FKWNPPIYCH 250 260 270 280 290 300 LPMVMGNDGQ KLSKRHGSTA LRQFIEDGYL PEAIINYITL LGWSYDDKRE FFSKSDLEKF 310 320 330 340 350 360 FSIEKINKSP AIFDYHKLDF FNSYYIREKK DEDLFNLLLP FFQKKGYVSK PNTLEESQKL 370 380 390 400 410 420 KLLVPLIKSR IKKLSDALSM TKFFYEDIKS WNLDEFLGRK KTAKEVCSIL ELIKPILEGF 430 440 450 460 470 480 EKRSLEENDK IFYDFAKNNG FKLGEILLPI RIAVLGSKVS PPLFDSLKLI GKSKVFERNK 490 LAQEFLRINE

References

[1]	"Comparative genome analysis: selection pressure on the Borrelia vls cassettes is essential for infectivity." Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J., Wilske B., Platzer M. BMC Genomics 7:211-211(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PKo.
[2]	"Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii Lyme disease agent isolates." Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J., Fraser-Liggett C.M., Schutzer S.E. J. Bacteriol. 193:6995-6996(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PKo.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000395 Genomic DNA. Translation: ABH01637.1. CP002933 Genomic DNA. Translation: AEL69597.1.
RefSeq	YP_005592587.1. NC_017238.1. YP_709813.1. NC_008277.1.
3D structure databases
ProteinModelPortal	Q0SNE1.
ModBase	Search...
Protein-protein interaction databases
STRING	390236.BAPKO_0381.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABH01637; ABH01637; BAPKO_0381. AEL69597; AEL69597; BafPKo_0371.
GeneID	12159325. 4227560.
KEGG	baf:BAPKO_0381. bafz:BafPKo_0371.
PATRIC	37189046. VBIBorAfz3878_0435.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252720.
KO	K01885.
OMA	RYRDFKG.
ProtClustDB	PRK01406.
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. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYE_BORAP

Accession

Primary (citable) accession number: Q0SNE1
Secondary accession number(s): G0IS16

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	May 1, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program