Skip Header

Contribute Send feedback
Read comments (?) or add your own

P64201 (GATB_STAAM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:SAV1899
OrganismStaphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]
Taxonomic identifier158878 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 MF_00121

Catalytic activity

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

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

Subunit structure

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

Sequence similarities

Belongs to the GatB/GatE family. GatB subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical term3D-structure
Complete 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 – 475475Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B HAMAP MF_00121
PRO_0000148834

Secondary structure

..................................................................... 475
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P64201 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 96805EE591658154

FASTA47553,657
        10         20         30         40         50         60 
MHFETVIGLE VHVELKTDSK MFSPSPAHFG AEPNSNTNVI DLAYPGVLPV VNKRAVDWAM 

        70         80         90        100        110        120 
RAAMALNMEI ATESKFDRKN YFYPDNPKAY QISQFDQPIG ENGYIDIEVD GETKRIGITR 

       130        140        150        160        170        180 
LHMEEDAGKS THKGEYSLVD LNRQGTPLIE IVSEPDIRSP KEAYAYLEKL RSIIQYTGVS 

       190        200        210        220        230        240 
DVKMEEGSLR CDANISLRPY GQEKFGTKAE LKNLNSFNYV RKGLEYEEKR QEEELLNGGE 

       250        260        270        280        290        300 
IGQETRRFDE STGKTILMRV KEGSDDYRYF PEPDIVPLYI DDAWKERVRQ TIPELPDERK 

       310        320        330        340        350        360 
AKYVNELGLP AYDAHVLTLT KEMSDFFEST IEHGADVKLT SNWLMGGVNE YLNKNQVELL 

       370        380        390        400        410        420 
DTKLTPENLA GMIKLIEDGT MSSKIAKKVF PELAAKGGNA KQIMEDNGLV QISDEATLLK 

       430        440        450        460        470 
FVNEALDNNE QSVEDYKNGK GKAMGFLVGQ IMKASKGQAN PQLVNQLLKQ ELDKR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000017 Genomic DNA. Translation: BAB58061.1.
RefSeqNP_372423.1. NC_002758.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DF4X-ray3.20B1-475[»]
2DQNX-ray2.55B1-475[»]
2F2AX-ray2.30B1-475[»]
2G5HX-ray2.50B1-475[»]
2G5IX-ray3.35B1-475[»]
3IP4X-ray1.90B1-475[»]
ProteinModelPortalP64201.
SMRP64201. Positions 2-411.
ModBaseSearch...

Protein-protein interaction databases

STRINGP64201.

2D gel databases

World-2DPAGE0002:P64201.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000006724; EBSTAP00000006542; EBSTAG00000006723.
GeneID1121912.
GenomeReviewsGene locus SAV1899 in contig BA000017_GR.
KEGGsav:SAV1899.
PATRIC19564652. VBIStaAur52173_1966.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0064.
GeneTreeEBGT00050000024664.
HOGENOMHBG395951.
OMAKNYFYAD.
PhylomeDBP64201.
ProtClustDBPRK05477.

Enzyme and pathway databases

BioCycSAUR158878:SAV1899-MONOMER.

Family and domain databases

HAMAPMF_00121. GatB.
[Tree]
InterProIPR017959. Asn/Gln-tRNA_amidoTrfase_suB/E.
IPR006075. Asn/Gln-tRNA_Trfase_suB/E_cat.
IPR018027. Asn/Gln_amidotransferase.
IPR003789. Asn/Gln_tRNA_amidoTrfrase-rel.
IPR023168. GatB_Yqey_C.
IPR004413. Gln-tRNA_amidoTrfase_bsu.
IPR017958. Gln-tRNA_amidoTrfase_suB_CS.
[Graphical view]
Gene3DG3DSA:1.10.10.410. GatB_Yqey_C. 1 hit.
KOK02434.
PANTHERPTHR11659. GatB. 1 hit.
PfamPF02934. GatB_N. 1 hit.
PF02637. GatB_Yqey. 1 hit.
[Graphical view]
SMARTSM00845. GatB_Yqey. 1 hit.
[Graphical view]
SUPFAMSSF89095. GatB_Yqey. 1 hit.
TIGRFAMsTIGR00133. GatB. 1 hit.
PROSITEPS01234. GATB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGATB_STAAM
AccessionPrimary (citable) accession number: P64201
Secondary accession number(s): Q99SY7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families