Glutamate--tRNA ligase - Bacillus subtilis (strain 168)

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P22250 (SYE_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 106. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	BSU00920

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length	483 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
Cofactor	Binds 1 zinc ion per subunit Probable. Ref.6
Subunit structure	Monomer.
Subcellular location	Cytoplasm 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 Metal-binding Nucleotide-binding Zinc
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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 483

483

Glutamate--tRNA ligase HAMAP-Rule MF_00022

PRO_0000119508

Regions

Motif

11 – 21

"HIGH" region HAMAP-Rule MF_00022

Motif

252 – 256

"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding

108

Zinc By similarity

Metal binding

110

Zinc By similarity

Metal binding

135

Zinc By similarity

Metal binding

137

Zinc By similarity

Binding site

255

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P22250 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: EF61671AEE465DD5
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FASTA

483

55,722

        10         20         30         40         50         60 
MGNEVRVRYA PSPTGHLHIG NARTALFNYL FARNQGGKFI IRVEDTDKKR NIEGGEQSQL 

        70         80         90        100        110        120 
NYLKWLGIDW DESVDVGGEY GPYRQSERND IYKVYYEELL EKGLAYKCYC TEEELEKERE 

       130        140        150        160        170        180 
EQIARGEMPR YSGKHRDLTQ EEQEKFIAEG RKPSIRFRVP EGKVIAFNDI VKGEISFESD 

       190        200        210        220        230        240 
GIGDFVIVKK DGTPTYNFAV AIDDYLMKMT HVLRGEDHIS NTPKQIMIYQ AFGWDIPQFG 

       250        260        270        280        290        300 
HMTLIVNESR KKLSKRDESI IQFIEQYKEL GYLPEALFNF IGLLGWSPVG EEELFTKEQF 

       310        320        330        340        350        360 
IEIFDVNRLS KSPALFDMHK LKWVNNQYVK KLDLDQVVEL TLPHLQKAGK VGTELSAEEQ 

       370        380        390        400        410        420 
EWVRKLISLY HEQLSYGAEI VELTDLFFTD EIEYNQEAKA VLEEEQVPEV LSTFAAKLEE 

       430        440        450        460        470        480 
LEEFTPDNIK ASIKAVQKET GHKGKKLFMP IRVAVTGQTH GPELPQSIEL IGKETAIQRL 


KNI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Glutamyl-tRNA synthetases of Bacillus subtilis 168T and of Bacillus stearothermophilus. Cloning and sequencing of the gltX genes and comparison with other aminoacyl-tRNA synthetases." Breton R., Watson D., Yaguchi M., Lapointe J. J. Biol. Chem. 265:18248-18255(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"Clustering and co-transcription of the Bacillus subtilis genes encoding the aminoacyl-tRNA synthetases specific for glutamate and for cysteine and the first enzyme for cysteine biosynthesis." Gagnon Y., Breton R., Putzer H., Pelchat M., Grunberg-Manago M., Lapointe J. J. Biol. Chem. 269:7473-7482(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin." Ogasawara N., Nakai S., Yoshikawa H. DNA Res. 1:1-14(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[4]	Ishino Y., Kim S.I., Soell D. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[6]	"The glutamyl-tRNA synthetase of Escherichia coli contains one atom of zinc essential for its native conformation and its catalytic activity." Liu J., Lin S.-X., Blochet J.-E., Pezolet M., Lapointe J. Biochemistry 32:11390-11396(1993) [PubMed] [Europe PMC] [Abstract] Cited for: COFACTOR.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M55073 Genomic DNA. Translation: AAA22495.1. L14580 Genomic DNA. Translation: AAA21796.1. D26185 Genomic DNA. Translation: BAA05326.1. U49789 Genomic DNA. Translation: AAC31971.1. AL009126 Genomic DNA. Translation: CAB11868.1.
PIR	SYBSET. A36090.
RefSeq	NP_387973.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P22250.
SMR	P22250. Positions 5-482.
ModBase	Search...
Protein-protein interaction databases
STRING	224308.BSU00920.
Proteomic databases
PaxDb	P22250.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB11868; CAB11868; BSU00920.
GeneID	936862.
KEGG	bsu:BSU00920.
PATRIC	18971689. VBIBacSub10457_0093.
Organism-specific databases
GenoList	BSU00920. [Micado]
Phylogenomic databases
eggNOG	COG0008.
HOGENOM	HOG000252720.
KO	K09698.
OMA	ISFESDG.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	BSUB:BSU00920-MONOMER. MetaCyc:MONOMER-13959.
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_BACSU

Accession

Primary (citable) accession number: P22250

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents