ID   SYGB_LAWIP              Reviewed;         695 AA.
AC   Q1MRM1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=LI0299;
OS   Lawsonia intracellularis (strain PHE/MN1-00).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Lawsonia.
OX   NCBI_TaxID=363253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHE/MN1-00;
RA   Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA   Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT   "The complete genome sequence of Lawsonia intracellularis: the causative
RT   agent of proliferative enteropathy.";
RL   Submitted (NOV-2005) 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; AM180252; CAJ54355.1; -; Genomic_DNA.
DR   RefSeq; WP_011526384.1; NC_008011.1.
DR   AlphaFoldDB; Q1MRM1; -.
DR   SMR; Q1MRM1; -.
DR   STRING; 363253.LI0299; -.
DR   KEGG; lip:LI0299; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_7; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000002430; 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; Reference proteome.
FT   CHAIN           1..695
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000197204"
SQ   SEQUENCE   695 AA;  78112 MW;  7697F0C00859C4F9 CRC64;
     MATFILEIGT EELPARFLLE LQSELGVRFL DSLQSMGYRP TEVSDYSTPR RLVVCIKGLD
     MIQPHCEEVV IGPPINIAFD KDGNPTKAAE GFAKNLGITI GSLSQISTDR GEYISGLKVK
     GGIPTKEVLA RLCPEIITAL PLPKRMRWGN NPFTFIRPIR WIMALLDSDI VPFELAGIHS
     NRNTVGLRNN NVPFIEVPSS TDYYMLLKEV GNVILDPNSR KDSILQLGNK EAQLIGGVVN
     WNERLLNEVI GLVEHPYPLL GTINSVFLNL PREVLLTSIE THQKSFGILD SQGNLLPYFL
     TVLNMTPPDL ALVKQGWERV LQARLEDARF FWNEDINSSF DEWQEKLTHL IFLDPLGSIA
     QKEHRVSLLC EWIAKYIPTS NAEEARKAGS LSKVDLVSKM VEEFPELQGV MGGIYARHKG
     ESESIATAIA EQYLPSGPDT DVPVTDLGAI LSIADKIDTL VGCFGCGIIP TGTADPYGLR
     RCALGIIRIL IEKEYPINLH QLYTRAQDNF VNVSWKLAPE DVLQKLHEFI IARLKNYFLA
     LGYDTLVVEA IVSTQTSQLW SIKDRLDSFI LLSQHEDFSQ LVQTIKRVIN IIKKQDKETE
     IVLTGHWNPS LFKDTAEKVL AEKLMIAVNK FNQESQTASL PVFMMLLKLQ PAINTFFDQV
     MIMSNDIEVR RNRLNLLKAL LLYIESLADF SVLQI