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P22250

- SYE_BACSU

UniProt

P22250 - SYE_BACSU

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Protein
Glutamate--tRNA ligase
Gene
gltX, BSU00920
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).UniRule annotation

Cofactori

Binds 1 zinc ion per subunit Inferred.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi108 – 1081Zinc By similarity
Metal bindingi110 – 1101Zinc By similarity
Metal bindingi135 – 1351Zinc By similarity
Metal bindingi137 – 1371Zinc By similarity
Binding sitei255 – 2551ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glutamate-tRNA ligase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW
  4. tRNA binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. glutamyl-tRNA aminoacylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU00920-MONOMER.
MetaCyc:MONOMER-13959.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligase (EC:6.1.1.17)
Alternative name(s):
Glutamyl-tRNA synthetase
Short name:
GluRS
Gene namesi
Name:gltX
Ordered Locus Names:BSU00920
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU00920. [Micado]

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 483483Glutamate--tRNA ligaseUniRule annotation
PRO_0000119508Add
BLAST

Proteomic databases

PaxDbiP22250.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

IntActiP22250. 1 interaction.
MINTiMINT-8366956.
STRINGi224308.BSU00920.

Structurei

3D structure databases

ProteinModelPortaliP22250.
SMRiP22250. Positions 5-482.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi11 – 2111"HIGH" regionUniRule annotation
Add
BLAST
Motifi252 – 2565"KMSKS" regionUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
KOiK09698.
OMAiVTGQTHG.
OrthoDBiEOG6DRPF7.
PhylomeDBiP22250.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22250-1 [UniParc]FASTAAdd to Basket

« Hide

MGNEVRVRYA PSPTGHLHIG NARTALFNYL FARNQGGKFI IRVEDTDKKR    50
NIEGGEQSQL NYLKWLGIDW DESVDVGGEY GPYRQSERND IYKVYYEELL 100
EKGLAYKCYC TEEELEKERE EQIARGEMPR YSGKHRDLTQ EEQEKFIAEG 150
RKPSIRFRVP EGKVIAFNDI VKGEISFESD GIGDFVIVKK DGTPTYNFAV 200
AIDDYLMKMT HVLRGEDHIS NTPKQIMIYQ AFGWDIPQFG HMTLIVNESR 250
KKLSKRDESI IQFIEQYKEL GYLPEALFNF IGLLGWSPVG EEELFTKEQF 300
IEIFDVNRLS KSPALFDMHK LKWVNNQYVK KLDLDQVVEL TLPHLQKAGK 350
VGTELSAEEQ EWVRKLISLY HEQLSYGAEI VELTDLFFTD EIEYNQEAKA 400
VLEEEQVPEV LSTFAAKLEE LEEFTPDNIK ASIKAVQKET GHKGKKLFMP 450
IRVAVTGQTH GPELPQSIEL IGKETAIQRL KNI 483
Length:483
Mass (Da):55,722
Last modified:August 1, 1991 - v1
Checksum:iEF61671AEE465DD5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA36090. SYBSET.
RefSeqiNP_387973.1. NC_000964.3.
WP_004399675.1. NZ_CM000487.1.

Genome annotation databases

EnsemblBacteriaiCAB11868; CAB11868; BSU00920.
GeneIDi936862.
KEGGibsu:BSU00920.
PATRICi18971689. VBIBacSub10457_0093.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A36090. SYBSET.
RefSeqi NP_387973.1. NC_000964.3.
WP_004399675.1. NZ_CM000487.1.

3D structure databases

ProteinModelPortali P22250.
SMRi P22250. Positions 5-482.
ModBasei Search...

Protein-protein interaction databases

IntActi P22250. 1 interaction.
MINTi MINT-8366956.
STRINGi 224308.BSU00920.

Proteomic databases

PaxDbi P22250.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB11868 ; CAB11868 ; BSU00920 .
GeneIDi 936862.
KEGGi bsu:BSU00920.
PATRICi 18971689. VBIBacSub10457_0093.

Organism-specific databases

GenoListi BSU00920. [Micado ]

Phylogenomic databases

eggNOGi COG0008.
HOGENOMi HOG000252720.
KOi K09698.
OMAi VTGQTHG.
OrthoDBi EOG6DRPF7.
PhylomeDBi P22250.

Enzyme and pathway databases

BioCyci BSUB:BSU00920-MONOMER.
MetaCyc:MONOMER-13959.

Family and domain databases

Gene3Di 1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPi MF_00022_B. Glu_tRNA_synth_B.
InterProi 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_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
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 ]
PANTHERi PTHR10119. PTHR10119. 1 hit.
Pfami PF00749. tRNA-synt_1c. 1 hit.
[Graphical view ]
PRINTSi PR00987. TRNASYNTHGLU.
SUPFAMi SSF48163. SSF48163. 1 hit.
TIGRFAMsi TIGR00464. gltX_bact. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., 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.

Entry informationi

Entry nameiSYE_BACSU
AccessioniPrimary (citable) accession number: P22250
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: September 3, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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