ID   SYGB_LACCB              Reviewed;         689 AA.
AC   B3WEK6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=LCABL_17260;
OS   Lacticaseibacillus casei (strain BL23) (Lactobacillus casei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=543734;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL23;
RA   Maze A., Boel G., Bourand A., Loux V., Gibrat J.F., Zuniga M., Hartke A.,
RA   Deutscher J.;
RT   "Lactobacillus casei BL23 complete genome sequence.";
RL   Submitted (JUN-2008) 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; FM177140; CAQ66807.1; -; Genomic_DNA.
DR   RefSeq; WP_003598794.1; NC_010999.1.
DR   AlphaFoldDB; B3WEK6; -.
DR   SMR; B3WEK6; -.
DR   KEGG; lcb:LCABL_17260; -.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
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..689
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101291"
SQ   SEQUENCE   689 AA;  76051 MW;  1E7AB35A9899E12F CRC64;
     MTHQYLIEIG LEDMPAHVVT PSLQQFHDKT VAFLKENHLD HGAIDQYATP RRLALLIHDL
     ADKQADVEED VKGPAKKIAQ DADGNWTKAA IGFSRGQGMT PDDIVFKTIK GVDYVYLHKA
     IKGKTAAAIL PGMLDVIKSL TFPTRMKWGA YDFEYIRPIH WLVSLLDDAI VPMKLLDVDA
     GRTTQGHRFL GRPVTLGNAA DYVAALKAQF VIVEPAARKQ LISDQIHQIA ADHQWQIDLD
     ADLLEEVNNL VEWPTAFAGN FDEKYLKIPE AVLITSMKDN QRYFYARDAS GKMVNAFIGV
     RNGNADHLAN VIAGNEKVLT ARLEDAAFFY AEDQKRSIAD DVDRLKAVSF HDKISSMYDK
     MARTRVIADL LADRFGLSAT DKADLDRAAS IYKFDLVTSM VGEFPELQGI MGEHYAQLAG
     EKPAVAQAIA EHYEPISADG ALPESLVGTV LAIADKFDSL MSFFAVDLIP SGSNDPYALR
     RQAYGIVRMI AKHDWPFAVA ELQTTIADAL KAAGKTNNLD FAAHQQDLNA FMIDRAKQVL
     QGQKIRHDIV DAVTVRADAD LAGILDAAKI LSAHADDTDF KPVMEALGRV LRITKKQQVK
     VDVDTAKFEN PSEGQLYDAT VATAKKFDDE PTEADYQALK ALADPINAYF DATMVMADDQ
     AIRQNRLAAL LQLAALIKQF GDVSQVIVK