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B2SE01

- SYE_FRATM

UniProt

B2SE01 - SYE_FRATM

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Protein

Glutamate--tRNA ligase

Gene
gltX, FTM_1545
Organism
Francisella tularensis subsp. mediasiatica (strain FSC147)
Status
Reviewed - Annotation score: 3 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 By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi97 – 971Zinc By similarity
Metal bindingi99 – 991Zinc By similarity
Metal bindingi124 – 1241Zinc By similarity
Metal bindingi126 – 1261Zinc By similarity
Binding sitei239 – 2391ATP 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

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

BioCyciFTUL441952:GIY0-1539-MONOMER.

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:FTM_1545
OrganismiFrancisella tularensis subsp. mediasiatica (strain FSC147)
Taxonomic identifieri441952 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
ProteomesiUP000001196: Chromosome

Subcellular locationi

Cytoplasm By similarity 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 – 468468Glutamate--tRNA ligaseUniRule annotationPRO_1000090076Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi441952.FTM_1545.

Structurei

3D structure databases

ProteinModelPortaliB2SE01.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi8 – 1811"HIGH" regionUniRule annotationAdd
BLAST
Motifi236 – 2405"KMSKS" regionUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252722.
KOiK01885.
OMAiWINGYYL.
OrthoDBiEOG6DRPF7.

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.

B2SE01-1 [UniParc]FASTAAdd to Basket

« Hide

MITTRFAPSP TGFLHVGGVR TALFSWLYAK NNNGKFILRI EDTDLERSTQ    50
EAVDAILDGM SWLGLKNDGE IYYQTKRFDR YKEVIQELIA DGKAYYCSCS 100
KERLEELREY QQANNLKTGY DGKCRDANYI PQQGESYVVR FKNPQDGVVS 150
WDDAVKGRIS ISNHELDDMI IQRADGSPTY NFCVVVDDID MAITHIIRGD 200
DHVNNTPKQI NIYKALNANV PVFAHVPMIL GPDGAKLSKR HGAVNVMQYR 250
EDGYLPQAIL NYLVRLGWSH GDQEIFSIEE MIKAFNLEHI NASPSRFDFE 300
KLKWLNKHYI KESKFDDIQT EVEYHFAKTG LDISNGPDLK ELVAVMAEKV 350
DTLVELAEKS SYFYSDDISY DENAVKKHIK ASTGEIFVKL LENFEALDAQ 400
QWQDPDVLHN IVSTTAEQCQ VGMGKVGMPL RVAITGSGQS PDIGITLKLL 450
GKNKVVARLT KALEELCK 468
Length:468
Mass (Da):52,939
Last modified:July 1, 2008 - v1
Checksum:iF5D3A1C70C11C12E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000915 Genomic DNA. Translation: ACD31365.1.
RefSeqiYP_001892144.1. NC_010677.1.

Genome annotation databases

EnsemblBacteriaiACD31365; ACD31365; FTM_1545.
GeneIDi6291039.
KEGGiftm:FTM_1545.
PATRICi17958079. VBIFraTul67519_1915.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000915 Genomic DNA. Translation: ACD31365.1 .
RefSeqi YP_001892144.1. NC_010677.1.

3D structure databases

ProteinModelPortali B2SE01.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 441952.FTM_1545.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACD31365 ; ACD31365 ; FTM_1545 .
GeneIDi 6291039.
KEGGi ftm:FTM_1545.
PATRICi 17958079. VBIFraTul67519_1915.

Phylogenomic databases

eggNOGi COG0008.
HOGENOMi HOG000252722.
KOi K01885.
OMAi WINGYYL.
OrthoDBi EOG6DRPF7.

Enzyme and pathway databases

BioCyci FTUL441952:GIY0-1539-MONOMER.

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

  1. "Molecular evolutionary consequences of niche restriction in Francisella tularensis, a facultative intracellular pathogen."
    Larsson P., Elfsmark D., Svensson K., Wikstroem P., Forsman M., Brettin T., Keim P., Johansson A.
    PLoS Pathog. 5:E1000472-E1000472(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FSC147.

Entry informationi

Entry nameiSYE_FRATM
AccessioniPrimary (citable) accession number: B2SE01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: May 14, 2014
This is version 44 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

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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