ID   GATB_STAAB              Reviewed;         475 AA.
AC   Q2YU27;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B {ECO:0000255|HAMAP-Rule:MF_00121};
DE            Short=Asp/Glu-ADT subunit B {ECO:0000255|HAMAP-Rule:MF_00121};
DE            EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00121};
GN   Name=gatB {ECO:0000255|HAMAP-Rule:MF_00121}; OrderedLocusNames=SAB1832c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
CC   -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or
CC       Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn)
CC       or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-
CC       tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the
CC       presence of glutamine and ATP through an activated phospho-Asp-
CC       tRNA(Asn) or phospho-Glu-tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_00121}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +
CC         L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate;
CC         Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+)
CC         + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:14513, Rhea:RHEA-COMP:9674, Rhea:RHEA-COMP:9677,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78515, ChEBI:CHEBI:78516, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00121};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_00121}.
CC   -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00121}.
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DR   EMBL; AJ938182; CAI81521.1; -; Genomic_DNA.
DR   RefSeq; WP_000545366.1; NC_007622.1.
DR   AlphaFoldDB; Q2YU27; -.
DR   SMR; Q2YU27; -.
DR   KEGG; sab:SAB1832c; -.
DR   HOGENOM; CLU_019240_0_0_9; -.
DR   OMA; ARKWWMG; -.
DR   GO; GO:0050566; F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:RHEA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.410; -; 1.
DR   Gene3D; 1.10.150.380; -; 1.
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_amidoTrase-B-like.
DR   InterPro; IPR042114; GatB_C_1.
DR   InterPro; IPR023168; GatB_Yqey_C_2.
DR   InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
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; SSF55931; SSF55931; 1.
DR   SUPFAM; SSF89095; SSF89095; 1.
DR   TIGRFAMs; TIGR00133; gatB; 1.
DR   PROSITE; PS01234; GATB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..475
FT                   /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT                   subunit B"
FT                   /id="PRO_0000241276"
SQ   SEQUENCE   475 AA;  53641 MW;  F7322BA5134324B9 CRC64;
     MHFETVIGLE VHVELKTDSK MFSPSPAHFG AEPNSNTNVI DLAYPGVLPV VNKRAVDWAM
     RAAMALNMEI ATESKFDRKN YFYPDNPKAY QISQFDQPIG ENGYIDIEVD GETKRIGITR
     LHMEEDAGKS THKGEYSLVD LNRQGTPLIE IVSEPDIRSP IEAYAYLEKL RSIIQYTGVS
     DVKMEEGSLR CDANISLRPY GQEKFGTKAE LKNLNSFNYV RKGLEYEEKR QEEELLNGGE
     IGQETRRFDE STGKTILMRV KEGSDDYRYF PEPDIVPLYI DDAWKKRVRQ TIPELPDERK
     AKYVNELGLP AYDAHVLTLT KEMSDFFEST IEHGADVKLT SNWLMGGVNE YLNKNQVELL
     DTKLTPENLA GMIKLIEDGT MSSKIAKKVF PELAAKGGNA KQIMEDNGLV QISDEATLLK
     FVNEALDNNE QSVEDYKNGK GKAMGFLVGQ IMKASKGQAN PQLVNQLLKQ ELDKR