B0BC83 (SYE_CHLTB) 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:	CTLon_0701

Organism

Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis) [Complete proteome] [HAMAP]

Taxonomic identifier

471473 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Chlamydiae/Verrucomicrobia group › Chlamydiae › Chlamydiia › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia › Chlamydia trachomatis

Protein attributes

Sequence length	506 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
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 – 506	506	Glutamate--tRNA ligase HAMAP-Rule MF_00022		PRO_1000090065
Regions
	Motif	12 – 22	11	"HIGH" region HAMAP-Rule MF_00022
	Motif	253 – 257	5	"KMSKS" region HAMAP-Rule MF_00022
Sites
	Binding site	256	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0BC83 [UniParc]. Last modified February 26, 2008. Version 1. Checksum: 7B3AA040504EF6B5	FASTA	506	58,563
	10 20 30 40 50 60 MTVQNVRVRV APSPTGDPHV GTAYMALFNE VFARKYNGQM ILRIEDTDQT RSRDDYEANI 70 80 90 100 110 120 FSALKWCGIR WDEGPDVGGA YGPYRQSERT EIYKKYAEIL LQTDCAYKCF ATPQELQEMR 130 140 150 160 170 180 AVASTLGYRG GYDRRYRYLS PEEVRQREEQ GQPYTIRLKV PLTGESVFED QCKGRVVFPW 190 200 210 220 230 240 ADVDDQVLVK SDGFPTYHFA NVVDDHLMGI THVLRGEEWL SSTPKHLLLY KAFGWEPPQF 250 260 270 280 290 300 FHMPLLLNPD GSKLSKRKNP TSIFYYRDAG YKKEAFMNFL TLMGYSMEGD EEIYSMQRLI 310 320 330 340 350 360 EAFDPKRIGR SGAVFDIRKL DWMNKHYLNH EGSPESLLQE LKGWLWNDEF LLKILPLCQS 370 380 390 400 410 420 RITTLADFVG LTSFFFTAIP QYSKEELLPS SLKQEQAAVM LYSLVKYLEK KDLWEKDFFY 430 440 450 460 470 480 QGSKWLAEAF QVHHKKAVIP LLYVAITGAK QGLPLFDSME LLGKARTRAR LTYAQNLLGG 490 500 VSKKVQQQVD KALQDQPLED IRFLDF

References

[1]

"Chlamydia trachomatis: genome sequence analysis of lymphogranuloma venereum isolates." Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P., Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D., Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N. Genome Res. 18:161-171(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: UCH-1/proctitis.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM884177 Genomic DNA. Translation: CAP07098.1.
RefSeq	YP_001653789.1. NC_010280.2.
3D structure databases
ProteinModelPortal	B0BC83.
ModBase	Search...
Protein-protein interaction databases
STRING	471473.CTLon_0701.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAP07098; CAP07098; CTLon_0701.
GeneID	5858990.
KEGG	ctl:CTLon_0701.
PATRIC	20383067. VBIChlTra68089_0759.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252720.
KO	K01885.
OMA	WENVRVR.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	CTRA471473:GHJK-701-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

SYE_CHLTB

Accession

Primary (citable) accession number: B0BC83

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	February 26, 2008
Last modified:	May 1, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program