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Database: UniProt/TrEMBL
Entry: D2P623_LISM2
LinkDB: D2P623_LISM2
Original site: D2P623_LISM2 
ID   D2P623_LISM2            Unreviewed;       476 AA.
AC   D2P623;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   19-FEB-2014, entry version 30.
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; RAMRTKE; -.
DR   BioCyc; LMON637381:GH7Z-1938-MONOMER; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
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; SSF89095; 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
//
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