ID   GATB_ORITB              Reviewed;         486 AA.
AC   A5CEC9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=OTBS_1368;
OS   Orientia tsutsugamushi (strain Boryong) (Rickettsia tsutsugamushi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Orientia.
OX   NCBI_TaxID=357244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boryong;
RX   PubMed=17483455; DOI=10.1073/pnas.0611553104;
RA   Cho N.-H., Kim H.-R., Lee J.-H., Kim S.-Y., Kim J., Cha S., Kim S.-Y.,
RA   Darby A.C., Fuxelius H.-H., Yin J., Kim J.H., Kim J., Lee S.J., Koh Y.-S.,
RA   Jang W.-J., Park K.-H., Andersson S.G.E., Choi M.-S., Kim I.-S.;
RT   "The Orientia tsutsugamushi genome reveals massive proliferation of
RT   conjugative type IV secretion system and host-cell interaction genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7981-7986(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; AM494475; CAM80434.1; -; Genomic_DNA.
DR   RefSeq; WP_011944873.1; NC_009488.1.
DR   AlphaFoldDB; A5CEC9; -.
DR   SMR; A5CEC9; -.
DR   EnsemblBacteria; CAM80434; CAM80434; OTBS_1368.
DR   KEGG; ots:OTBS_1368; -.
DR   eggNOG; COG0064; Bacteria.
DR   HOGENOM; CLU_019240_1_1_5; -.
DR   OMA; ARKWWMG; -.
DR   Proteomes; UP000001565; Chromosome.
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;
KW   Reference proteome.
FT   CHAIN           1..486
FT                   /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT                   subunit B"
FT                   /id="PRO_1000016013"
SQ   SEQUENCE   486 AA;  54428 MW;  A86B2684BD286B8B CRC64;
     MTFIEGKTEK WEYVIGLEIH AQIKSNAKLF SSASTEFGSS PNSQVELLDA AMPGSLPVLN
     EFCVHQAIKT ALGINAKINK LSIFDRKNYF YADLPAGYQI SQFYHPIAQG GWIEILDENG
     NIKCIQINRL HIEQDTGKST HDQSDTYSYI DLNRSGIALM EIVSEPDISS PMQAAEYIKK
     LRAILRYLDS CNGDMEKGAL RCDANISVRK PNSELGTKCE IKNLNSIKSI VRALEFEGQR
     QVNILESGGT VKQESLLFDA TLGKTFPMRS KENATDYRYF PDPDLPPIIL DQSLIDNIAS
     SLPELPDAKI TRYVNEIKLS DYNAQVLAAD KDISCFFEEV IKTANPILTA NWILSELFGL
     MNKDGITINE CKITANHFSE LIQLISSKAI SSKIAKTVLK EMFDSGKSPK IIMQEKNIQQ
     ISDPNQIADI IDDVLKDNYQ SVVSYRNGKD RLFGFFVGQV MKKTAGNANP ELINEILHTK
     LKQFQI