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B8ZLK0 (GATB_STRPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B

Short name=Asp/Glu-ADT subunit B
EC=6.3.5.-
Gene names
Name:gatB
Ordered Locus Names:SPN23F04090
OrganismStreptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1) [Complete proteome] [HAMAP]
Taxonomic identifier561276 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length480 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) By similarity. HAMAP-Rule MF_00121

Catalytic activity

ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. HAMAP-Rule MF_00121

ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate. HAMAP-Rule MF_00121

Subunit structure

Heterotrimer of A, B and C subunits By similarity. HAMAP-Rule MF_00121

Sequence similarities

Belongs to the GatB/GatE family. GatB subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

carbon-nitrogen ligase activity, with glutamine as amido-N-donor

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 480480Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B HAMAP-Rule MF_00121
PRO_1000122537

Sequences

Sequence LengthMass (Da)Tools
B8ZLK0 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: C21C477E1BD7FDBD

FASTA48053,716
        10         20         30         40         50         60 
MNFETVIGLE VHVELNTNSK IFSPTSAHFG NDQNANTNVI DWSFPGVLPV LNKGVVDAGI 

        70         80         90        100        110        120 
KAALALNMDI HKKMHFDRKN YFYPDNPKAY QISQFDEPIG YNGWIEVELE DGTTKKIGIE 

       130        140        150        160        170        180 
RAHLEEDAGK NTHGTDGYSY VDLNRQGVPL IEIVSEADMR SPEEAYAYLT ALKEVIQYAG 

       190        200        210        220        230        240 
ISDVKMEEGS MRVDANISLR PYGQEKFGTK TELKNLNSFS NVRKGLEYEV QRQAEILRSG 

       250        260        270        280        290        300 
GQIRQETRRY DEANKATILM RVKEGAADYR YFPEPDLPLF EISDEWIEEM RTELPEFPKE 

       310        320        330        340        350        360 
RRARYVSDLG LSDYDASQLT ANKVTSNFFE KAVALGGDAK QVSNWLQGEV AQFLNAEGKT 

       370        380        390        400        410        420 
LEQIELTPEN LVEMITIIED GTISSKIAKK VFVHLAKNGG GAREYVEKAG MVQISDPAIL 

       430        440        450        460        470        480 
IPIIHQVFAD NEAAVADFKS GKRNADKAFT GFLMRATKGQ ANPQVALKLL AQELAKLKEN 

« Hide

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: CAR68258.1.
RefSeqYP_002510451.1. NC_011900.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561276.SPN23F_04090.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7329251.
KEGGsne:SPN23F_04090.
PATRIC19672080. VBIStrPne132160_0443.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0064.
KOK02434.
OMAESADYRY.
OrthoDBEOG6RJV5B.
ProtClustDBPRK05477.

Enzyme and pathway databases

BioCycSPNE561276:GJFJ-403-MONOMER.

Family and domain databases

HAMAPMF_00121. GatB.
InterProIPR004413. Apn/Gln-ADT_bsu.
IPR017959. Asn/Gln-tRNA_amidoTrfase_suB/E.
IPR006075. Asn/Gln-tRNA_Trfase_suB/E_cat.
IPR018027. Asn/Gln_amidotransferase.
IPR003789. Asn/Gln_tRNA_amidoTrfrase-rel.
IPR017958. Gln-tRNA_amidoTrfase_suB_CS.
[Graphical view]
PANTHERPTHR11659. PTHR11659. 1 hit.
PfamPF02934. GatB_N. 1 hit.
PF02637. GatB_Yqey. 1 hit.
[Graphical view]
SMARTSM00845. GatB_Yqey. 1 hit.
[Graphical view]
SUPFAMSSF89095. SSF89095. 1 hit.
TIGRFAMsTIGR00133. gatB. 1 hit.
PROSITEPS01234. GATB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGATB_STRPJ
AccessionPrimary (citable) accession number: B8ZLK0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families