ID   SYGB_LIMRJ              Reviewed;         691 AA.
AC   B2G6Z6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=LAR_0712;
OS   Limosilactobacillus reuteri (strain JCM 1112) (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=557433;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 1112;
RX   PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA   Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA   Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA   Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA   Hattori M.;
RT   "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT   fermentum reveal a genomic island for reuterin and cobalamin production.";
RL   DNA Res. 15:151-161(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; AP007281; BAG25228.1; -; Genomic_DNA.
DR   RefSeq; WP_003668126.1; NC_010609.1.
DR   AlphaFoldDB; B2G6Z6; -.
DR   SMR; B2G6Z6; -.
DR   GeneID; 66470885; -.
DR   KEGG; lrf:LAR_0712; -.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
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..691
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101295"
SQ   SEQUENCE   691 AA;  78537 MW;  797E026626F6C2BC CRC64;
     MANTYLLEVG VEEMPAHVVT PSIKQLHERV AKYLKEQRIT FDDIQEFATP RRMALLIHGL
     SDKQPDIDES VKGPAKKIAQ DADGNWTKAA IGFTRGQGAS VEDIEFKEVK GVEYVFVEKH
     IAGKTVAEVL QGLPAVITSM TFPTLMKWGY NNLQFIRPIR WLVSLLNDEV VPFNILDVEA
     GRETQGHRFL GHPVEIAKAD DYEETLNNDF VIADQTKRKN LIKDQITKII NENNWQVDWD
     EDLLEEVNNL VEWPTAFAGS FDEKYLALPD PVLITSMKDN QRFFCVRDGD GNLLSHFISV
     RNGNTDYLDN VIKGNERVLV PRLEDAQFFY QEDQKLTIDE YVERLKKVSF HDKISSMYDK
     MQRVAVIANV LGKQLNLSDE ELADLDRAAH IYKFDLTTQM VGEFAELQGI MGEIYAKLFG
     EKDDVATAIR EHYMPISAEG ELPQTKIGAV LAIADKLDSI MSFFAVDMIP SGSNDPYALR
     RQAFGIVRII ADRGWHLPLL SIQSEIAPAF ENAEINVSFD LNKNSDEVRS FFLDRIKQLF
     HGQKVRHDII DAATDTRQND IANILEAIQT IDDHKDDDNF KEDIEALTRV LRIAKKDKRP
     VSELVVDPNL FENPSEAKMH TAVSELIKEN QQTVSENFAA LRTLTPIISE YFDENMIMDK
     NEDIRNNRLA QLSILAHQAS LIGNLDNLIV K