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O30509

- GATB_BACSU

UniProt

O30509 - GATB_BACSU

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Protein

Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B

Gene

gatB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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).

Catalytic activityi

ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. carbon-nitrogen ligase activity, with glutamine as amido-N-donor Source: InterPro

GO - Biological processi

  1. translation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU06690-MONOMER.
MetaCyc:MONOMER-13956.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (EC:6.3.5.-)
Short name:
Asp/Glu-ADT subunit B
Gene namesi
Name:gatB
Synonyms:yerN
Ordered Locus Names:BSU06690
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU06690. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 476476Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit BPRO_0000148762Add
BLAST

Proteomic databases

PaxDbiO30509.

Interactioni

Subunit structurei

Heterotrimer of A, B and C subunits.

Protein-protein interaction databases

IntActiO30509. 1 interaction.
MINTiMINT-8366537.
STRINGi224308.BSU06690.

Structurei

3D structure databases

ProteinModelPortaliO30509.
SMRiO30509. Positions 1-476.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GatB/GatE family. GatB subfamily.Curated

Phylogenomic databases

eggNOGiCOG0064.
HOGENOMiHOG000223742.
InParanoidiO30509.
KOiK02434.
OrthoDBiEOG6RJV5B.

Family and domain databases

HAMAPiMF_00121. GatB.
InterProiIPR004413. 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]
PANTHERiPTHR11659. PTHR11659. 1 hit.
PfamiPF02934. GatB_N. 1 hit.
PF02637. GatB_Yqey. 1 hit.
[Graphical view]
SMARTiSM00845. GatB_Yqey. 1 hit.
[Graphical view]
SUPFAMiSSF89095. SSF89095. 1 hit.
TIGRFAMsiTIGR00133. gatB. 1 hit.
PROSITEiPS01234. GATB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O30509-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNFETVIGLE VHVELKTKSK IFSSSPTPFG AEANTQTSVI DLGYPGVLPV
60 70 80 90 100
LNKEAVEFAM KAAMALNCEI ATDTKFDRKN YFYPDNPKAY QISQFDKPIG
110 120 130 140 150
ENGWIEIEVG GKTKRIGITR LHLEEDAGKL THTGDGYSLV DFNRQGTPLV
160 170 180 190 200
EIVSEPDIRT PEEAYAYLEK LKSIIQYTGV SDCKMEEGSL RCDANISLRP
210 220 230 240 250
IGQEEFGTKT ELKNLNSFAF VQKGLEHEEK RQEQVLLSGF FIQQETRRYD
260 270 280 290 300
EATKKTILMR VKEGSDDYRY FPEPDLVELY IDDEWKERVK ASIPELPDER
310 320 330 340 350
RKRYIEELGF AAYDAMVLTL TKEMADFFEE TVQKGAEAKQ ASNWLMGEVS
360 370 380 390 400
AYLNAEQKEL ADVALTPEGL AGMIKLIEKG TISSKIAKKV FKELIEKGGD
410 420 430 440 450
AEKIVKEKGL VQISDEGVLL KLVTEALDNN PQSIEDFKNG KDRAIGFLVG
460 470
QIMKASKGQA NPPMVNKILL EEIKKR
Length:476
Mass (Da):53,553
Last modified:May 30, 2000 - v2
Checksum:i095B056BF4B44676
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 282TP → PN in AAB87634. 1 PublicationCurated
Sequence conflicti43 – 431G → A in AAB87634. 1 PublicationCurated
Sequence conflicti240 – 2412FF → GV in CAB12489. (PubMed:9384377)Curated
Sequence conflicti310 – 3112FA → LP in CAB12489. (PubMed:9384377)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49788 Genomic DNA. Translation: AAB87634.1.
AF008553 Genomic DNA. Translation: AAB83965.1.
AL009126 Genomic DNA. Translation: CAB12489.2.
PIRiT51583.
RefSeqiNP_388551.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB12489; CAB12489; BSU06690.
GeneIDi936057.
KEGGibsu:BSU06690.
PATRICi18972984. VBIBacSub10457_0706.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49788 Genomic DNA. Translation: AAB87634.1 .
AF008553 Genomic DNA. Translation: AAB83965.1 .
AL009126 Genomic DNA. Translation: CAB12489.2 .
PIRi T51583.
RefSeqi NP_388551.2. NC_000964.3.

3D structure databases

ProteinModelPortali O30509.
SMRi O30509. Positions 1-476.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O30509. 1 interaction.
MINTi MINT-8366537.
STRINGi 224308.BSU06690.

Proteomic databases

PaxDbi O30509.

Protocols and materials databases

DNASUi 936057.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12489 ; CAB12489 ; BSU06690 .
GeneIDi 936057.
KEGGi bsu:BSU06690.
PATRICi 18972984. VBIBacSub10457_0706.

Organism-specific databases

GenoListi BSU06690. [Micado ]

Phylogenomic databases

eggNOGi COG0064.
HOGENOMi HOG000223742.
InParanoidi O30509.
KOi K02434.
OrthoDBi EOG6RJV5B.

Enzyme and pathway databases

BioCyci BSUB:BSU06690-MONOMER.
MetaCyc:MONOMER-13956.

Family and domain databases

HAMAPi MF_00121. GatB.
InterProi IPR004413. 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 ]
PANTHERi PTHR11659. PTHR11659. 1 hit.
Pfami PF02934. GatB_N. 1 hit.
PF02637. GatB_Yqey. 1 hit.
[Graphical view ]
SMARTi SM00845. GatB_Yqey. 1 hit.
[Graphical view ]
SUPFAMi SSF89095. SSF89095. 1 hit.
TIGRFAMsi TIGR00133. gatB. 1 hit.
PROSITEi PS01234. GATB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiGATB_BACSU
AccessioniPrimary (citable) accession number: O30509
Secondary accession number(s): O31499, O50554
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: October 29, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3