SYGB_BAUCH
ID SYGB_BAUCH Reviewed; 699 AA.
AC Q1LTU2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00255};
DE AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00255};
GN Name=glyS {ECO:0000255|HAMAP-Rule:MF_00255}; OrderedLocusNames=BCI_0160;
OS Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX NCBI_TaxID=374463;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H.,
RA Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.;
RT "Metabolic complementarity and genomics of the dual bacterial symbiosis of
RT sharpshooters.";
RL PLoS Biol. 4:1079-1092(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC EC=6.1.1.14; Evidence={ECO:0000255|HAMAP-Rule:MF_00255};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00255}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00255}.
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DR EMBL; CP000238; ABF13850.1; -; Genomic_DNA.
DR RefSeq; WP_011520355.1; NC_007984.1.
DR AlphaFoldDB; Q1LTU2; -.
DR SMR; Q1LTU2; -.
DR STRING; 374463.BCI_0160; -.
DR PRIDE; Q1LTU2; -.
DR EnsemblBacteria; ABF13850; ABF13850; BCI_0160.
DR KEGG; bci:BCI_0160; -.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000002427; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR PANTHER; PTHR30075; PTHR30075; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01045; TRNASYNTHGB.
DR TIGRFAMs; TIGR00211; glyS; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..699
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101265"
SQ SEQUENCE 699 AA; 80353 MW; A9EA2256F1575E41 CRC64;
MKQHIFLVEI GTEELPAKEL RRLAQYFTAN FINELNANGI NYNDINWFAA PRRLAIKVNS
INSIPTKSYM EKRGPAINKA FDAEGKPTPA AIGWARNCGI TVNQAERFTT DKGEWLIYRM
LVETKPVQKL LCSMVYNALT KFSSLTKIMR WGEKNYKFIR PVRTITLLLD DLVIPGNIFG
IDSNRIILGH RFMGESVISL LHADYYPNVL LERGRVIADY ELRKDTIRRN IEIMVKKIGG
FTKINDKLLE EVTSLVDWPI VLTASFNANF LRIPAEALIY TMENNQKYFP VYDAKGKLLP
YFIFVTNIES TNTNQIVVGN EKVMRSRLAD VEFFFNIDRK QKLEDYLLLL GQVKFQMELG
TLLDKSYRLE ILASWIAEII STDIKQAARA ALISKCDLMT QMVFEYPEIQ GIIGMHYATL
DGETELVALA QKEQYLPLFS GDNLPTTLVS CAVSIADKMD NLAGIFGINQ QYTKQANDPL
ALRRAALGIL RIIIEKQLPI DLLSLIDKAV FLYNKKLTNT IVVEQIIHFM LNRLLSWYKK
QGYSIDTINA VMAVYKPTGK LIHFDARLRA VHYLRQIPHA ENLTKRIFNI IAKHKDLING
EVNFTLLKQP EEVILINSIT QLHKKLILFF EKGKYQEALW ELINLREIIN TFFSKIIIMT
ENKELCINRL NIINKVRQLF LIIADFSLLQ CSKEKSNVD