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O30509 (GATB_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 90. 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
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
Synonyms:yerN
Ordered Locus Names:BSU06690
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length476 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). 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.

Sequence similarities

Belongs to the GatB/GatE family. GatB subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference 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 – 476476Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B HAMAP-Rule MF_00121
PRO_0000148762

Experimental info

Sequence conflict27 – 282TP → PN in AAB87634. Ref.2
Sequence conflict431G → A in AAB87634. Ref.2
Sequence conflict240 – 2412FF → GV in CAB12489. Ref.3
Sequence conflict310 – 3112FA → LP in CAB12489. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O30509 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 095B056BF4B44676

FASTA47653,553
        10         20         30         40         50         60 
MNFETVIGLE VHVELKTKSK IFSSSPTPFG AEANTQTSVI DLGYPGVLPV LNKEAVEFAM 

        70         80         90        100        110        120 
KAAMALNCEI ATDTKFDRKN YFYPDNPKAY QISQFDKPIG ENGWIEIEVG GKTKRIGITR 

       130        140        150        160        170        180 
LHLEEDAGKL THTGDGYSLV DFNRQGTPLV EIVSEPDIRT PEEAYAYLEK LKSIIQYTGV 

       190        200        210        220        230        240 
SDCKMEEGSL RCDANISLRP IGQEEFGTKT ELKNLNSFAF VQKGLEHEEK RQEQVLLSGF 

       250        260        270        280        290        300 
FIQQETRRYD EATKKTILMR VKEGSDDYRY FPEPDLVELY IDDEWKERVK ASIPELPDER 

       310        320        330        340        350        360 
RKRYIEELGF AAYDAMVLTL TKEMADFFEE TVQKGAEAKQ ASNWLMGEVS AYLNAEQKEL 

       370        380        390        400        410        420 
ADVALTPEGL AGMIKLIEKG TISSKIAKKV FKELIEKGGD AEKIVKEKGL VQISDEGVLL 

       430        440        450        460        470 
KLVTEALDNN PQSIEDFKNG KDRAIGFLVG QIMKASKGQA NPPMVNKILL EEIKKR

« Hide

References

« Hide 'large scale' references
[1]"Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation."
Curnow A.W., Hong K.-W., Yuan R., Kim S.-I., Martins O., Winkler W., Henkin T.M., Soell D.
Proc. Natl. Acad. Sci. U.S.A. 94:11819-11826(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: 168.
[2]Hong K.-W., Martins O.M., Kim S.-I., Soell D.
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U49788 Genomic DNA. Translation: AAB87634.1.
AF008553 Genomic DNA. Translation: AAB83965.1.
AL009126 Genomic DNA. Translation: CAB12489.2.
PIRT51583.
RefSeqNP_388551.2. NC_000964.3.

3D structure databases

ProteinModelPortalO30509.
SMRO30509. Positions 1-476.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-8366537.
STRING224308.BSU06690.

Proteomic databases

PaxDbO30509.

Protocols and materials databases

DNASU936057.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12489; CAB12489; BSU06690.
GeneID936057.
KEGGbsu:BSU06690.
PATRIC18972984. VBIBacSub10457_0706.

Organism-specific databases

GenoListBSU06690. [Micado]

Phylogenomic databases

eggNOGCOG0064.
HOGENOMHOG000223742.
KOK02434.
ProtClustDBPRK05477.

Enzyme and pathway databases

BioCycBSUB:BSU06690-MONOMER.
MetaCyc:MONOMER-13956.

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. GatB_Yqey. 1 hit.
TIGRFAMsTIGR00133. gatB. 1 hit.
PROSITEPS01234. GATB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGATB_BACSU
AccessionPrimary (citable) accession number: O30509
Secondary accession number(s): O31499, O50554
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: May 29, 2013
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents