ID   GATB_STAAU              Reviewed;         475 AA.
AC   Q9RF06;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 92.
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};
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25923 / DSM 1104 / JCM 2413 / NBRC 14462 / NCIMB 12702 / NCTC
RC   12981 / Seattle 1945;
RA   Namgoong S., Hong K.-W., Lee S.Y.;
RT   "Glu-tRNAGln amidotransferase of Staphylococcus aureus.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   MASS SPECTROMETRY.
RC   STRAIN=MRSA-M2;
RX   PubMed=16714572; DOI=10.1128/iai.00392-06;
RA   Brady R.A., Leid J.G., Camper A.K., Costerton J.W., Shirtliff M.E.;
RT   "Identification of Staphylococcus aureus proteins recognized by the
RT   antibody-mediated immune response to a biofilm infection.";
RL   Infect. Immun. 74:3415-3426(2006).
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   -!- MASS SPECTROMETRY: Mass=53670; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16714572};
CC   -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00121}.
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DR   EMBL; AF205033; AAF18137.1; -; Genomic_DNA.
DR   RefSeq; WP_000545373.1; NZ_WKIW01000007.1.
DR   AlphaFoldDB; Q9RF06; -.
DR   SMR; Q9RF06; -.
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   1: Evidence at protein level;
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_0000148839"
SQ   SEQUENCE   475 AA;  53630 MW;  9FA4C53EFCD35CA8 CRC64;
     MHFETVIGLE VHVELKTDSK MFSPSPAHFG AEPNSNTNVI DLAYPGVLPV VNKRAVDWAM
     RAAMALNMEI ATESKFDRKN YFYPDNPKAY QISQFDQPIG ENGYIDIEVD GETKRIGITR
     LHMEEDAGKS THKGEYSLVD LNRQGTPLIE IVSEPDIRSP KEAYAYLEKL RSIIQYTGVS
     DVKMEEGSLR CDANISLRPY GQEKFGTKAE LKNLNSFNYV RKGLEYEEKR QEEELLSGGE
     IGQETRRFDE STGKTILMRV KEGSDDYRYF PEPDIVPLYI DDAWKERVRQ TIPELPDERK
     AKYVNELGLP AYDAHVLTLT KEMSDFFEST IEHGADVKLT SNWLMGGVNE YLNKNQVELL
     DTKLTPENLA GMIKLIEDGT MSSKIAKKVF PELAAKGGNA KQIMEDNGLV QISDEATLLK
     FVNEALDNNE QSVEDYKNGK GKAMGFLVGQ IMKASKGQAN PQLVNQLLKQ ELDKR