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Q3KN18 (GATB_CHLTA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 50. 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:CTA_0005
OrganismChlamydia trachomatis serovar A (strain HAR-13 / ATCC VR-571B) [Complete proteome] [HAMAP]
Taxonomic identifier315277 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length488 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 – 488488Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B HAMAP-Rule MF_00121
PRO_0000241208

Sequences

Sequence LengthMass (Da)Tools
Q3KN18 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 7E2014461830698E

FASTA48855,048
        10         20         30         40         50         60 
MGIAHTEWES VIGLEVHVEL NTESKLFSPA RNHFGDEPNT NISPVCTGMP GSLPVLNKDA 

        70         80         90        100        110        120 
VRKAVLFGCA VEGDVALFSR FDRKSYFYPD SPRNFQITQY EHPIVRGGCI RAVVEGEEKT 

       130        140        150        160        170        180 
FELAQTHLED DAGMLKHFGD FAGVDYNRAG VPLIEIVSKP CMFSAEDAVA YANALVSILG 

       190        200        210        220        230        240 
YIGISDCNME EGSIRFDVNI SVRPRGSREL RNKVEIKNMN SFTFMAQALE AEKRRQIEEY 

       250        260        270        280        290        300 
LSYPNEDPKK VVPAATYRWD PEKKKTVLMR LKERAEDYMY FVEPDLPVLQ ITETYIDEVR 

       310        320        330        340        350        360 
QTLPELPHSK YMRYITDFDI AEDLAMILVS DRHTAHFFET ATMSCKNYRA LSNWITVEFA 

       370        380        390        400        410        420 
GRCKARGKTL PFTGILPEWV AQLVNFIDRG VITGKIAKEI ADRMVSSFGE SPEDILRRHP 

       430        440        450        460        470        480 
SLLPMTDDHA LRAIVKEVVA QNTASVADYK NGKAKALGFL VGQIMKRTEG KAPPKRVNEL 


LLAAMRDM 

« Hide

References

[1]"Comparative genomic analysis of Chlamydia trachomatis oculotropic and genitotropic strains."
Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.
Infect. Immun. 73:6407-6418(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HAR-13 / ATCC VR-571B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000051 Genomic DNA. Translation: AAX50254.1.
RefSeqYP_327802.1. NC_007429.1.

3D structure databases

ProteinModelPortalQ3KN18.
ModBaseSearch...

Protein-protein interaction databases

STRING315277.CTA_0005.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX50254; AAX50254; CTA_0005.
GeneID3688099.
KEGGcta:CTA_0005.
PATRIC32021852. VBIChlTra31516_0007.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0064.
HOGENOMHOG000223742.
KOK02434.
OMAKNYFYAD.
ProtClustDBPRK05477.

Enzyme and pathway databases

BioCycCTRA315277:GI4C-5-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. GatB_Yqey. 1 hit.
TIGRFAMsTIGR00133. gatB. 1 hit.
PROSITEPS01234. GATB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGATB_CHLTA
AccessionPrimary (citable) accession number: Q3KN18
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 8, 2005
Last modified: May 29, 2013
This is version 50 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