ID D2P623_LISM2 Unreviewed; 476 AA.
AC D2P623;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 01-MAY-2013, entry version 27.
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=LM5923_1905;
OS Listeria monocytogenes serotype 1/2a (strain 08-5923).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=637381;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=08-5923;
RX PubMed=20167121; DOI=10.1186/1471-2164-11-120;
RA Gilmour M.W., Graham M., Van Domselaar G., Tyler S., Kent H.,
RA Trout-Yakel K.M., Larios O., Allen V., Lee B., Nadon C.;
RT "High-throughput genome sequencing of two Listeria monocytogenes
RT clinical isolates during a large foodborne outbreak.";
RL BMC Genomics 11:120-120(2010).
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-aspartyl-tRNA(Asn) + L-glutamine = ADP
CC + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate.
CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP
CC + phosphate + L-glutaminyl-tRNA(Gln) + 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; CP001604; ADB71746.1; -; Genomic_DNA.
DR RefSeq; YP_003417108.1; NC_013768.1.
DR ProteinModelPortal; D2P623; -.
DR SMR; D2P623; 2-412.
DR EnsemblBacteria; ADB71746; ADB71746; LM5923_1905.
DR GeneID; 8758699; -.
DR KEGG; lmy:LM5923_1905; -.
DR PATRIC; 32257636; VBILisMon5116_1922.
DR HOGENOM; HOG000223742; -.
DR KO; K02434; -.
DR OMA; KNYFYAD; -.
DR BioCyc; LMON637381:GH7Z-1901-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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; Transferase.
SQ SEQUENCE 476 AA; 53237 MW; 5FCBBBC3582CFF44 CRC64;
MNFETVIGLE VHVELKTNSK IFSSAPAHFG AEPNTNTTVV DLGMPGVLPV LNKRAVEFGM
KAAMAINCEI AEHTKFDRKN YFYPDNPKAY QISQFDKPIG EHGWIEIEVG GKKKKIGITR
LHLEEDAGKN THTSHGYSLV DINRQGTPLI EIVSEPDIRS AEEAYAYLEK LKSIIQYTGV
SDVKMEEGSM RCDANISIRP IGQEEFGVKT ELKNLNSFNN VRKGIEYEEK RQAEVLKSGG
IIEQETRRFE EATGKTSLMR IKEGSDDYRY FPEPDLVDLF IDDAWKERIR AEIPELPDKR
QIRYINDLGL PAYDAMVLTL TKEMSDFFEA TLVAGADAKQ ASNWLMGEVS AYLNAEQKEL
HETGLTPENL AGMIKLIEAG TISSKIAKKV FRELAQNGGD AEQVVKDKGL VQISDEGALR
TIISEILDNN EQSIVDFKNG KDRAVGFLVG QVMKATKGQA NPPMVNKLLL EEMNKR
//
