P64198 (GATB_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	BR0899, BS1330_I0895

Organism

Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella suis

Protein attributes

Sequence length	500 AA.
Sequence status	Complete.
Protein existence	Inferred 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.
Sequence similarities	Belongs to the GatB/GatE family. GatB subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	translation Inferred from electronic annotation. Source: HAMAP
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 500	500	Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B HAMAP-Rule MF_00121		PRO_0000148771

Sequences

	Sequence		Length	Mass (Da)
	P64198 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: FEBA3251275BE195	FASTA	500	54,714
	10 20 30 40 50 60 MSIIDTRTPE PKRFISGATG DWEVVIGMEV HAQVTSESKL FSGASTAFGA EPNSNVSLVD 70 80 90 100 110 120 AAMPGMLPVI NLECVRQAVR TGIGLNAQIN LKSVFDRKNY FYPDLPQGYQ ISQFKQPIVG 130 140 150 160 170 180 EGKIMISVGP DNKGQFEDVE IGIERLHLEQ DAGKSMHDQH PTMSYVDLNR SGVALMEIVS 190 200 210 220 230 240 KPDLRSSDEA RAYLTKLRTI VRYLGTCDGN MDEGSMRADV NVSVRRPGGE FGTRCEIKNV 250 260 270 280 290 300 NSIRFVGQAI EYEARRQIAI LEDGGVIDQE TRLFDPVKGE TRSMRSKEEA HDYRYFPDPD 310 320 330 340 350 360 LLPLEFDQAF VDALAAKLPE LPDVKKQRLV ETLGISVYDA SILVTEKAIA DYYEAVAEGR 370 380 390 400 410 420 DGKAAANWVI NDLLGALNKA GKDIEESPIS PAQLGAIIDL IKEGTISGKI AKDLFEIVWN 430 440 450 460 470 480 EGGDPKKLVE ERGMKQVTDT GAIEKAVDDV IAANPDKVEQ AKAKPTLAGW FVGQVMKATG 490 500 GKANPQAVNE LVKSKLGIEE

References

[1]

"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

[2]

"Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014291 Genomic DNA. Translation: AAN29827.1. CP002997 Genomic DNA. Translation: AEM18244.1.
RefSeq	NP_697912.1. NC_004310.3. YP_005615736.1. NC_017251.1.
3D structure databases
ProteinModelPortal	P64198.
ModBase	Search...
Protein-protein interaction databases
STRING	204722.BR0899.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN29827; AAN29827; BR0899. AEM18244; AEM18244; BS1330_I0895.
GeneID	1166568. 12137222.
KEGG	bms:BR0899. bsi:BS1330_I0895.
PATRIC	17790106. VBIBruSui107850_0913.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0064.
HOGENOM	HOG000223743.
KO	K02434.
OMA	KNYFYAD.
ProtClustDB	PRK05477.
Family and domain databases
HAMAP	MF_00121. GatB.
InterPro	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]
PANTHER	PTHR11659. PTHR11659. 1 hit.
Pfam	PF02934. GatB_N. 1 hit. PF02637. GatB_Yqey. 1 hit. [Graphical view]
SMART	SM00845. GatB_Yqey. 1 hit. [Graphical view]
SUPFAM	SSF89095. GatB_Yqey. 1 hit.
TIGRFAMs	TIGR00133. gatB. 1 hit.
PROSITE	PS01234. GATB. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GATB_BRUSU

Accession

Primary (citable) accession number: P64198
Secondary accession number(s): G0K9C7, Q8YGT9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program