O51316 (GATB_BORBU) 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:	BB_0341

Organism

Borrelia burgdorferi (Lyme disease spirochete)

Taxonomic identifier

139 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length	485 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 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 process	Protein biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	translation Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 485	485	Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B HAMAP MF_00121		PRO_0000148766

Sequences

	Sequence		Length	Mass (Da)
	O51316 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 622C10C208EDE845	FASTA	485	54,521
	10 20 30 40 50 60 MEYKLVIGLE IHVQLGLKTK AFCGCKNEFG GVPNSRVCPI CLGLPGSLPS VNVELINSAI 70 80 90 100 110 120 LAGHATNSKI RNVVKFDRKH YYYPDLPKGY QISQNDKPIC EGGSLLIETP SGPKKINIIR 130 140 150 160 170 180 IHMEEDSGKS LHLLDSENQS YVDFNRSGAP LLEIVSAPDI NSGDEAVAFL SSLREIFRYL 190 200 210 220 230 240 DLSECNMENG SFRCDVNVNL IVKENGVEHK TPIAEIKNLN SFKSIKAAIE YEELRQQQEW 250 260 270 280 290 300 IQFKKTLNSC GKHTRGFDDR SGVTVIQRNK ETVSDYRYFQ EPDLPLIEID DSYIDNIKNL 310 320 330 340 350 360 KLIELPFHAR IRLKGQYGLS DFDVITLTAD KHLLKYFEEA VINSSDPKKV ANWILSEVLS 370 380 390 400 410 420 VLNDKGISVL EFNLLPSYIT ELVEFIVAGK ISGKMAKRVF SEMMTRGVSA SVVISENQLE 430 440 450 460 470 480 QVSDKFVIKQ IVLEVLDENP KSIELYKKGK DHAIKFMMGQ IMKKSSGKIN PILANEILLE SLSNV

References

[1]

"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C. Nature 390:580-586(1997) [PubMed: 9403685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000783 Genomic DNA. Translation: AAC66716.1.
PIR	D70142.
RefSeq	NP_212475.1. NC_001318.1.
3D structure databases
ProteinModelPortal	O51316.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBORT00000008715; EBBORP00000008045; EBBORG00000008714.
GeneID	1195178.
GenomeReviews	Gene locus BB_0341 in contig AE000783_GR.
KEGG	bbu:BB0341.
NMPDR	fig|224326.1.peg.725.
PATRIC	20557294. VBIBorBur75917_0737.
TIGR	BB_0341.
Phylogenomic databases
GeneTree	EBGT00050000007362.
HOGENOM	HBG395951.
OMA	KNYFYAD.
PhylomeDB	O51316.
ProtClustDB	PRK05477.
Enzyme and pathway databases
BioCyc	BBUR224326:BB_0341-MONOMER.
Family and domain databases
HAMAP	MF_00121. GatB. [Tree]
InterPro	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. IPR004413. Gln-tRNA_amidoTrfase_bsu. IPR017958. Gln-tRNA_amidoTrfase_suB_CS. [Graphical view]
KO	K02434.
PANTHER	PTHR11659. GatB. 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_BORBU

Accession

Primary (citable) accession number: O51316

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	June 1, 1998
Last modified:	January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program