SYGB_ACTP2
ID SYGB_ACTP2 Reviewed; 689 AA.
AC A3N3A1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=APL_1803;
OS Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=416269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L20;
RX PubMed=18065534; DOI=10.1128/jb.01845-07;
RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA Nash J.H.E.;
RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT (serotype 5b).";
RL J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN74887.1; -; Genomic_DNA.
DR RefSeq; WP_009875135.1; NC_009053.1.
DR AlphaFoldDB; A3N3A1; -.
DR SMR; A3N3A1; -.
DR STRING; 416269.APL_1803; -.
DR EnsemblBacteria; ABN74887; ABN74887; APL_1803.
DR KEGG; apl:APL_1803; -.
DR PATRIC; fig|416269.6.peg.1874; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000001432; 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..689
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006348"
SQ SEQUENCE 689 AA; 76379 MW; C6B06294DC9D8346 CRC64;
MTTQNFLAEI GTEELPPKAL KKLATAFAEN VENELNQADL SFEKVEWFAA PRRLAVKALG
LATAQPSKEI EKRGPAVSAA FDADGKPTKA AEGWARGCGI TVDQADRIAT DKGEWLVHRA
VIEGQPTKNL LVDIISRSLA NLPIPKMMRW GDKTEQFVRP VHTVTLFFGS ELIEGEILGV
KINNVIRGHR FLGEREFTIS HADEYLTALR EKGMVVADFN ERKALILAKS QEKATALGGV
ADIEEDLLDE VTSLVEFPNV LTAKFEERFL AVPAEALVYT MKGDQKYFPI YDKDGKLLPH
FIFVSNINPE DPTAIIEGNE KVVRPRLTDA EFFFKTDLKQ RLEDRLPRLE TVLFQQQLGT
LRDKTARIEA LAGEIAAQIG ADKAKAERAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
GEDEEVAVAL NEQYMPRFAG DELPKSLVAC SVALADKFDT LTGIFGIGQA PKGSADPFAL
RRAALGSLRI IVEKNLPLDL EDLVRKSAAL FGNKLTNANV VEDVVDFMLG RFRAWYQDEG
IAVDVIQAVL ARRPTKPADF DARVRAVSHF RTLDSAEALA AANKRVSNIL AKVEGEISIE
IDRTLLVEAE EKALAEQVIS LQTELAPTFA NGEYQTALDR LASLRETVDN FFEKVMVNAE
DANLRRNRQA ILNNLRNLFL QVADISVLQ