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B8ZPC8 (B8ZPC8_STRPJ) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutamate--tRNA ligase HAMAP-Rule MF_00022
EC=6.1.1.17 HAMAP-Rule MF_00022
Alternative name(s):
Glutamyl-tRNA synthetase HAMAP-Rule MF_00022
Gene names
Name:gltX HAMAP-Rule MF_00022 EMBL CAR69835.1
Ordered Locus Names:SPN23F20940
OrganismStreptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1) [Complete proteome] [HAMAP] EMBL CAR69835.1
Taxonomic identifier561276 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceInferred 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

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00022

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. HAMAP-Rule MF_00022 RuleBase RU003489

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Motif11 – 2111"HIGH" region By similarity HAMAP-Rule MF_00022
Motif255 – 2595"KMSKS" region By similarity HAMAP-Rule MF_00022

Sites

Binding site2581ATP By similarity HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
B8ZPC8 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 88EBB13B9A4B3CD6

FASTA48655,909
        10         20         30         40         50         60 
MSKDIRVRYA PSPTGLLHIG NARTALFNYL YARHHGGTFL IRIEDTDRKR HVEDGERSQL 

        70         80         90        100        110        120 
ENLRWLGMDW DESPESHENY RQSERLDLYQ KYIDQLLAEG KAYKSYVTEE ELAAERERQE 

       130        140        150        160        170        180 
VAGETPRYIN EYLGMSEEEK AAYIAEREAA GIIPTVRLAV NESGIYKWHD MVKGDIEFEG 

       190        200        210        220        230        240 
GNIGGDWVIQ KKDGYPTYNF AVVIDDHDMQ ISHVIRGDDH IANTPKQLMV YEALGWEAPE 

       250        260        270        280        290        300 
FGHMTLIINS ETGKKLSKRD TNTLQFIEDY RKKGYLPEAV FNFIALLGWN PGGEDEIFSR 

       310        320        330        340        350        360 
EELIKLFDEN RLSKSPAAFD QKKLDWMSND YIKNADLETI FEMAKPFLEE AGRLTDKAEK 

       370        380        390        400        410        420 
LVELYKPQMK SVDEIIPLTD LFFSDFPELT EAEREVMTGE TVPTVLEAFK AKLEAMTDDE 

       430        440        450        460        470        480 
FVTENIFPQI KAVQKETGIK GKNLFMPIRI AVSGEMHGPE LPDTIFLLGR EKSIQHIENI 


LKEISK

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References

[1]"Role of conjugative elements in the evolution of the multidrug-resistant pandemic clone Streptococcus pneumoniae Spain23F ST81."
Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K., Bason N.C., Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J., Bentley S.D., Mitchell T.J.
J. Bacteriol. 191:1480-1489(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700669 / Spain 23F-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FM211187 Genomic DNA. Translation: CAR69835.1.
RefSeqYP_002511937.1. NC_011900.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING561276.SPN23F_20940.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7327606.
KEGGsne:SPN23F_20940.
PATRIC19675702. VBIStrPne132160_2199.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
KOK09698.
OMAESIIQFV.
ProtClustDBPRK01406.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. 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]
PANTHERPTHR10119. PTHR10119. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB8ZPC8_STRPJ
AccessionPrimary (citable) accession number: B8ZPC8
Entry history
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: May 1, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info