SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B0SKQ2

- SYE_LEPBP

UniProt

B0SKQ2 - SYE_LEPBP

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Glutamate--tRNA ligase
Gene
gltX, LEPBI_I0677
Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris)
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 bindingi107 – 1071Zinc By similarity
Metal bindingi109 – 1091Zinc By similarity
Metal bindingi134 – 1341Zinc By similarity
Metal bindingi136 – 1361Zinc By similarity
Binding sitei253 – 2531ATP 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

BioCyciLBIF456481:GCM0-672-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:LEPBI_I0677
OrganismiLeptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris)
Taxonomic identifieri456481 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira
ProteomesiUP000001847: Chromosome I

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 – 517517Glutamate--tRNA ligaseUniRule annotation
PRO_0000367700Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi456481.LEPBI_I0677.

Structurei

3D structure databases

ProteinModelPortaliB0SKQ2.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi10 – 2011"HIGH" regionUniRule annotation
Add
BLAST
Motifi250 – 2545"KMSKS" regionUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
KOiK09698.
OMAiWLPEEMG.
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.

B0SKQ2-1 [UniParc]FASTAAdd to Basket

« Hide

MTEVRTRFAP SPSGFLHVGG ARTALFNYLY AKAKKGKFLL RIEDTDQDRS    50
TEASFKIILE SLKWLGMEWD EGPGVGGPNG PYTQSERIHI YKEYTDKLIQ 100
EKKAYRCFCT AEELEGKKKQ ADAMGIPYIY DGKCSDLSDA EIGSQLEKKI 150
PFTVRFKTPH KIVIVDDMIQ GKVKFESKLI GDFIIVKSDG FPSYNYAVVI 200
DDALMKITHV IRGVGHLSNT PRQILIFEAF GFPLPRFAHA SEIVGTDGKK 250
LSKRAGATSV LAFRDLGYSS ETMRNYMALL GWTSPDGKEY MSDEELCSVF 300
DVERCSKSPA TFDVFKKLKE EEKESVDFNK LTILGLAEYL NPKSKLNWMS 350
NKYIRDTKIE TLGKALEPFL KDCQIPEAFK SGENPQLLSI LDSVRVYLDR 400
LIQAPPYIEE FFLENLSFEN DEAKQLVLEG KGKEVVAEFY RIVKESSLTT 450
PDAYKESMAK VGEITGEKGR TLFMPIRAIT TGKSHGLELP ILFSLLGQEK 500
MVKRMEQLAG ILGISLR 517
Length:517
Mass (Da):58,314
Last modified:April 8, 2008 - v1
Checksum:i01F51E9F307E26D0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000786 Genomic DNA. Translation: ABZ96809.1.
RefSeqiYP_001838085.1. NC_010602.1.

Genome annotation databases

EnsemblBacteriaiABZ96809; ABZ96809; LEPBI_I0677.
GeneIDi6224229.
KEGGilbi:LEPBI_I0677.
PATRICi22348068. VBILepBif123590_0682.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000786 Genomic DNA. Translation: ABZ96809.1 .
RefSeqi YP_001838085.1. NC_010602.1.

3D structure databases

ProteinModelPortali B0SKQ2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 456481.LEPBI_I0677.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABZ96809 ; ABZ96809 ; LEPBI_I0677 .
GeneIDi 6224229.
KEGGi lbi:LEPBI_I0677.
PATRICi 22348068. VBILepBif123590_0682.

Phylogenomic databases

eggNOGi COG0008.
HOGENOMi HOG000252720.
KOi K09698.
OMAi WLPEEMG.
OrthoDBi EOG6DRPF7.

Enzyme and pathway databases

BioCyci LBIF456481:GCM0-672-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. "Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis."
    Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., Rood J.I., Lajus A.
    , Davies J.K., Medigue C., Adler B.
    PLoS ONE 3:E1607-E1607(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Patoc 1 / ATCC 23582 / Paris.

Entry informationi

Entry nameiSYE_LEPBP
AccessioniPrimary (citable) accession number: B0SKQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: May 14, 2014
This is version 45 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

Similar proteinsi