ID   SYGB_RICBR              Reviewed;         658 AA.
AC   Q1RGS4;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=RBE_1359;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(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; CP000087; ABE05440.1; -; Genomic_DNA.
DR   RefSeq; WP_011478009.1; NC_007940.1.
DR   AlphaFoldDB; Q1RGS4; -.
DR   SMR; Q1RGS4; -.
DR   STRING; 336407.RBE_1359; -.
DR   EnsemblBacteria; ABE05440; ABE05440; RBE_1359.
DR   KEGG; rbe:RBE_1359; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_1_5; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000001951; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   PANTHER; PTHR30075; PTHR30075; 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.
FT   CHAIN           1..658
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_0000274897"
SQ   SEQUENCE   658 AA;  75180 MW;  5C6BE8DD3EA19CF9 CRC64;
     MSELLLELFS EEIPAFIQKD AEEGYLSIFT KIFEENEIFA KIQVFSGPRR ITLYATHLPK
     VTLPKEIEIK GPSTEAPEAA INGFCKAHNV SKLELSTKLI NNQLYYFYIK KVEERQIKEI
     LPEIIVEAIN KYSWAKSMFW GNYNIKWIRP LRNILCIFDS EILPLQFGHL AANNVTFGHR
     LTDNKKLEVT DFEDYKTKLT ENYVILERLK REEIIKTSLL EQANSHNLTI KEDLRLIEEV
     AGLSEFPVVL CGAIPQKFLE LPKEVLISSM RTHQKYFCLF DRSENFAPYF LFVSNGQFAN
     SKLVVQGNEK VLSARLSDAL YFYKQDISKT LEANLEKLAA VTFHTKLGSL KEKVERITNI
     CKYIDPDNKD LITAAKLCKS DLVSEMVGEF PELQGIMGYY YAKHENLNEE IAVAIRDHYK
     PQGLSDSVPV GNAALLAIAD KLDSLVGLMI AGEAPTGSGD PYALRRQVLG IIRIIIENKL
     ELNLNSLIDF SLKLYSSDKD KDLIISFFEE RAKFYFKNEY DISLINAVLD LNLANIKFKL
     DALKEFLEKE DGKQLLNAYK RASNILGSQN IDGAVEPSLF NTQPEKELFE VTQKLSLQIV
     DKDYDKALNL LQTLLTPITS FFDNVLVNDS DPKIAKNRLL ILQDVCKLFH KIAKFNRL