ID   SYGB_DELAS              Reviewed;         704 AA.
AC   A9BXZ8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=Daci_1289;
OS   Delftia acidovorans (strain DSM 14801 / SPH-1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=398578;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT   "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000884; ABX33933.1; -; Genomic_DNA.
DR   RefSeq; WP_012203219.1; NC_010002.1.
DR   AlphaFoldDB; A9BXZ8; -.
DR   SMR; A9BXZ8; -.
DR   STRING; 398578.Daci_1289; -.
DR   PRIDE; A9BXZ8; -.
DR   EnsemblBacteria; ABX33933; ABX33933; Daci_1289.
DR   KEGG; dac:Daci_1289; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_4; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000000784; 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..704
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101270"
SQ   SEQUENCE   704 AA;  75565 MW;  B9A2AE97429181EE CRC64;
     MNASNLLVEL FVEELPPKAL QKLGDAFAGV LFEQLKAQGL LASSEARLTA YASPRRLAAH
     ITEVLPQAED KAVSQKLMPV SVGLDADGKP TPALIKKLAA LGAGEEAVAG LTRQGEGKAE
     ALFHSSTVRG VMLADGVQKA LDEAIAKLPI PKVMRYQLAD GWSSVHFVRP AHGLVVLHGT
     EVLIGVKALG LTAGTATHGH RFEAAVDPVV IRSADDYAAQ LREEGAVIAS FAERRAEIAR
     QLQAAAERLG GGVRPIEDEA LLDEVTALVE RPNVLVCEFE KEFLDVPQEC LILTMKANQK
     YFPLLDAAGK LTHQFLVVSN ISPQDASAVI GGNERVVRPR LADAKFFFDQ DRKKTLASRV
     EGLGKVVYHN KLGTQGERVE RVRSIAKSIA RQLGDTGLAQ QADLAAQLAK TDLVTDMVGE
     FPELQGTMGR YYALNDGLDV AVADAIEDHY KPRFAGDELP RGNAGVVVAL ADKLETLVGM
     FGIGNLPTGD RDPFALRRHA LGVIRMLVEK DLALDLETLL VSVLPAFGDK IEDATPQLAD
     FIYDRLAGNL REQGFSAQEV DSVLALRPQR LSDVQKRLEA VRAFGELPEA PALAAANKRV
     GNILKKADQA VQAQVDAAVL AEVAEKDLYA ALQSVAPKAQ QQFAAGDYTA SLQTLAALRA
     PVDAFFEHVM VNAEDPALKA NRLGLLATLH EAMNRVADLS RLAA