GATB_TREPA
ID GATB_TREPA Reviewed; 509 AA.
AC O83984;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 116.
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=TP_1021;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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) (By similarity). {ECO:0000250}.
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 -!- 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 -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000520; AAC65971.1; -; Genomic_DNA.
DR PIR; A71254; A71254.
DR RefSeq; WP_010882465.1; NC_021490.2.
DR AlphaFoldDB; O83984; -.
DR SMR; O83984; -.
DR STRING; 243276.TPANIC_1021; -.
DR EnsemblBacteria; AAC65971; AAC65971; TP_1021.
DR GeneID; 57879533; -.
DR KEGG; tpa:TP_1021; -.
DR eggNOG; COG0064; Bacteria.
DR HOGENOM; CLU_019240_0_0_12; -.
DR OMA; ARKWWMG; -.
DR OrthoDB; 497127at2; -.
DR Proteomes; UP000000811; 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..509
FT /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT subunit B"
FT /id="PRO_0000148861"
SQ SEQUENCE 509 AA; 56865 MW; C28B90122236BF52 CRC64;
MSDLQTGTVP SIAGATDDTH AAPFFYEVII GCEIHCQLLT KTKAFCACAN RSGGMPNSRV
CPVCLGLPGA LPVVSEEYVR LGVRAGLALG CTIQLWSAFD RKHYFYPDLP KGYQITQYDA
PLCTDGAVDV QGVDMPVQRR VRIERIHLEE DAGKSLHAAD AYSYIDFNRC GVPLIEIVSR
PDLRSAEEAA CFMQTIREIL TFIEVTDGNL EEGALRCDAN VNVRILYKGQ EHHTPISEIK
NMNSYRMVRD ACTYEVQRQL QEFWQKGPAS KEEMQRKRTM GWDPVEGVTL LQRTKHSLRD
YRFMRDPDLP DLHLTPAYVQ HLSYTVGELP AARRARFKLD LGLSAFAAQT LTGSRMLADW
FEKAAHASKN ARRVANWILS EVLAVVNEKN ICIAELNLSP EAIAELMDAV EDQRITGKQA
KDIFAQMLAT GARAQDIISA QGLAQLSDEE EIATLVQTVF QEHPKALRDW QHGKTNVAAW
LMGQVMKRSR GRAHPARVAT LVHQALSQL
