ID GATB_CAMHC Reviewed; 473 AA.
AC A7I1W4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 01-MAY-2013, entry version 37.
DE RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B;
DE Short=Asp/Glu-ADT subunit B;
DE EC=6.3.5.-;
GN Name=gatB; OrderedLocusNames=CHAB381_0944;
OS Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 /
OS CH001A).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360107;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Nelson K.E.;
RT "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a
RT commensal isolated from the human gastrointestinal tract.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn)
CC or Gln-tRNA(Gln) through the transamidation of misacylated Asp-
CC tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both
CC of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction
CC takes place in the presence of glutamine and ATP through an
CC activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP
CC + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
CC -!- CATALYTIC ACTIVITY: ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP
CC + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate.
CC -!- SUBUNIT: Heterotrimer of A, B and C subunits (By similarity).
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
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DR EMBL; CP000776; ABS50951.1; -; Genomic_DNA.
DR RefSeq; YP_001406505.1; NC_009714.1.
DR ProteinModelPortal; A7I1W4; -.
DR SMR; A7I1W4; 2-396.
DR STRING; 360107.CHAB381_0944; -.
DR EnsemblBacteria; ABS50951; ABS50951; CHAB381_0944.
DR GeneID; 5409008; -.
DR KEGG; cha:CHAB381_0944; -.
DR PATRIC; 20040020; VBICamHom81367_0905.
DR eggNOG; COG0064; -.
DR HOGENOM; HOG000223742; -.
DR KO; K02434; -.
DR OMA; KNYFYAD; -.
DR ProtClustDB; PRK05477; -.
DR BioCyc; CHOM360107:GHCX-978-MONOMER; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:HAMAP.
DR GO; GO:0006412; P:translation; IEA:HAMAP.
DR HAMAP; MF_00121; GatB; 1; -.
DR InterPro; IPR004413; Apn/Gln-ADT_bsu.
DR InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E.
DR InterPro; IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat.
DR InterPro; IPR018027; Asn/Gln_amidotransferase.
DR InterPro; IPR003789; Asn/Gln_tRNA_amidoTrfrase-rel.
DR InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
DR PANTHER; PTHR11659; PTHR11659; 1.
DR Pfam; PF02934; GatB_N; 1.
DR Pfam; PF02637; GatB_Yqey; 1.
DR SMART; SM00845; GatB_Yqey; 1.
DR SUPFAM; SSF89095; GatB_Yqey; 1.
DR TIGRFAMs; TIGR00133; gatB; 1.
DR PROSITE; PS01234; GATB; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1 473 Aspartyl/glutamyl-tRNA(Asn/Gln)
FT amidotransferase subunit B.
FT /FTId=PRO_1000015953.
SQ SEQUENCE 473 AA; 53414 MW; C3D175A1924D7C19 CRC64;
MFETIIGLEV HCQLNTKTKI FCSCPTSFGD KANVHVCPTC LALPGALPVL NKEAVKKAIM
FGTAVNATIN KKSVFDRKNY FYPDLPKAYQ ISQFTIPIVE HGELFINING ENKRIGITRA
HLEEDAGKNT HEEGRSLVDL NRAGTPLLEI VSEPDMRSGD EAVAYLKKLH SILRFINISD
ANMQEGSFRC DVNVSIRPKG DEKLYTRVEI KNLNSFKFVQ KAIEYEVARQ IDAWEDGKYS
ELVVQETRLF DTSNFTTRSM RSKEDSAEYR YFPDPDLLTV EISDEMLEEA RKIPELPNEK
KERYINELGL KKDDAEVIIS SYEHAKFFED LINAGHEPKL CVTWLNVELN GRLKNGLTIE
DSPIDSAKMS DLLSRIEDGT ISQKAAKEVL DFIMENIEIS VDDVIKKLGL KQVSDDATIL
AVIDAVISKN EQKVAEYRNG KDKLFGFFVG QVMKEGKGAF NPAKVNELLK QKL
//
