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Q4L3I7

- SYE_STAHJ

UniProt

Q4L3I7 - SYE_STAHJ

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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Staphylococcus haemolyticus (strain JCSC1435)
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).UniRule annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei255 – 2551ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glutamate-tRNA ligase activity Source: UniProtKB-HAMAP
  3. 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, Nucleotide-binding

Enzyme and pathway databases

BioCyciSHAE279808:GJX7-2539-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligaseUniRule annotation (EC:6.1.1.17UniRule annotation)
Alternative name(s):
Glutamyl-tRNA synthetaseUniRule annotation
Short name:
GluRSUniRule annotation
Gene namesi
Name:gltXUniRule annotation
Ordered Locus Names:SH2481
OrganismiStaphylococcus haemolyticus (strain JCSC1435)
Taxonomic identifieri279808 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000543: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 484484Glutamate--tRNA ligasePRO_0000237405Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi279808.SH2481.

Structurei

3D structure databases

ProteinModelPortaliQ4L3I7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi11 – 2111"HIGH" regionAdd
BLAST
Motifi252 – 2565"KMSKS" region

Sequence similaritiesi

Belongs to the class-I aminoacyl-tRNA synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
KOiK09698.
OMAiKHYDGDF.
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.

Q4L3I7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSERIRVRYA PSPTGYLHIG NARTALFNYL FAKHYDGDFV VRIEDTDSKR
60 70 80 90 100
NLEDGESSQF DNLKWLGLDW DESIDKDKGY GPYRQSERGD IYNPLIQQLL
110 120 130 140 150
DEDKAYKCYM TEEELEKERE DQIARGEMPR YGGQHAHLTE EERQQFEAEG
160 170 180 190 200
RRPSIRFRVP QDQTYTFNDM VKGEISFDSN NIGDWVIVKK DGIPTYNFAV
210 220 230 240 250
AIDDYYMGIS DVIRGDDHVS NTPKQLMIYE AFGWEAPRFG HMSLIVNEER
260 270 280 290 300
KKLSKRDGQI LQFIEQYRDL GYLPEALFNF ITLLGWSPEG EEEIFSKEEF
310 320 330 340 350
IKIFDEKRLS KSPAMFDRQK LAWVNNQYMK TKDTDTVFEL ALPHLIKANL
360 370 380 390 400
IPESPSEDDK EWGRKLVALY QKEMSYAGEI VPLSEMFFHE MPELGEEEQE
410 420 430 440 450
VINGEQVPEL MTHLYGKLEA LEPFEAADIK KTIKEVQKET GIKGKQLFMP
460 470 480
IRVAVTGQMH GPELPNTIEV LGKDKVLSRL KKFV
Length:484
Mass (Da):56,301
Last modified:August 2, 2005 - v1
Checksum:iDACA3A30F6619E55
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE05790.1.
RefSeqiWP_011276733.1. NC_007168.1.
YP_254396.1. NC_007168.1.

Genome annotation databases

EnsemblBacteriaiBAE05790; BAE05790; SH2481.
GeneIDi3482194.
KEGGisha:SH2481.
PATRICi19621031. VBIStaHae67511_2435.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE05790.1 .
RefSeqi WP_011276733.1. NC_007168.1.
YP_254396.1. NC_007168.1.

3D structure databases

ProteinModelPortali Q4L3I7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 279808.SH2481.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAE05790 ; BAE05790 ; SH2481 .
GeneIDi 3482194.
KEGGi sha:SH2481.
PATRICi 19621031. VBIStaHae67511_2435.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SHAE279808:GJX7-2539-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. "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
    Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
    J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCSC1435.

Entry informationi

Entry nameiSYE_STAHJ
AccessioniPrimary (citable) accession number: Q4L3I7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: August 2, 2005
Last modified: November 26, 2014
This is version 66 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