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Q49YU3 (GATB_STAS1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. 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:SSP0892
OrganismStaphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229) [Complete proteome] [HAMAP]
Taxonomic identifier342451 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length475 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 – 475475Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B HAMAP-Rule MF_00121
PRO_0000241279

Sequences

Sequence LengthMass (Da)Tools
Q49YU3 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 62202720AF90ED5D

FASTA47553,829
        10         20         30         40         50         60 
MHFETVIGLE VHVELKTDSK MFSPAPAHFG AKPNSNTNVI DLAYPGVLPV VNRRAVDWAM 

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

       130        140        150        160        170        180 
LHMEEDAGKS THKDGYSLVD LNRQGTPLIE IVSEPDIRSP QEAYAYLEKL RSIIQYTGVS 

       190        200        210        220        230        240 
DCKMEEGSLR CDANISLRPY GQEEFGTKAE LKNLNSFTYV RKGLEYEEKR QEEELLNGGE 

       250        260        270        280        290        300 
ILQETRRFDE SNGKTLLMRV KEGSDDYRYF PEPDIVPLYV DEEWKERVRQ TIPELPDERK 

       310        320        330        340        350        360 
EKYVNQYGLP AYDAHVLTLT KEMSDFFEGA VAEGADVKLT SNWLMGGVNE YLNKNQIDLL 

       370        380        390        400        410        420 
DTKLTPENLA GMIKLIEDGT MSSKIAKKVF PELAENGGDA KQIMEDKGLV QISDEATLLK 

       430        440        450        460        470 
FVNEALDNNE QSIEDYKNGK GKAMGFLVGQ IMKASKGQAN PQLVNQLLKQ ELDKR 

« Hide

References

[1]"Whole genome sequence of Staphylococcus saprophyticus reveals the pathogenesis of uncomplicated urinary tract infection."
Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.
Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15305 / DSM 20229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008934 Genomic DNA. Translation: BAE18037.1.
RefSeqYP_300982.1. NC_007350.1.

3D structure databases

ProteinModelPortalQ49YU3.
SMRQ49YU3. Positions 3-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342451.SSP0892.

Proteomic databases

PRIDEQ49YU3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE18037; BAE18037; SSP0892.
GeneID3617088.
KEGGssp:SSP0892.
PATRIC19623290. VBIStaSap90642_0891.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0064.
HOGENOMHOG000223742.
KOK02434.
OMAWIEIEVE.
OrthoDBEOG6RJV5B.

Enzyme and pathway databases

BioCycSSAP342451:GKFA-911-MONOMER.

Family and domain databases

Gene3D1.10.10.410. 1 hit.
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.
IPR023168. GatB_Yqey_C.
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_STAS1
AccessionPrimary (citable) accession number: Q49YU3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: September 13, 2005
Last modified: May 14, 2014
This is version 56 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