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SYGB_LIMF3
ID   SYGB_LIMF3              Reviewed;         692 AA.
AC   B2GBZ7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=LAF_0843;
OS   Limosilactobacillus fermentum (strain NBRC 3956 / LMG 18251) (Lactobacillus
OS   fermentum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=334390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 3956 / LMG 18251;
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; AP008937; BAG27179.1; -; Genomic_DNA.
DR   RefSeq; WP_012391176.1; NC_010610.1.
DR   AlphaFoldDB; B2GBZ7; -.
DR   SMR; B2GBZ7; -.
DR   EnsemblBacteria; BAG27179; BAG27179; LAF_0843.
DR   GeneID; 61200414; -.
DR   KEGG; lfe:LAF_0843; -.
DR   PATRIC; fig|334390.5.peg.927; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000001697; 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..692
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101292"
SQ   SEQUENCE   692 AA;  77403 MW;  C819B1338817199B CRC64;
     MAHSYLLEVG LEEMPAHVVT PSIQQLKTRV ANYLTEERID FEDIQAYSTP RRLALLISGL
     ADKQPDVDES VKGPAKKIAQ DADGNWTKAA IGFTRGQGAT VDDIEFKEVK GVEYVYVEKH
     IQGKPVAEVL AGLNDVITAM NFPTLMRWGS FKLNFIRPIH WLVSLLDDQV VPFDILNVTA
     GRLTRGHRFL GHDVEIKSAT DYVAALKDDF VIVDAAERKA TIKDQIQAIV DQHNWVIDWD
     EELLEEVNNL VEWPTAFAGT FDQKYLELPE PVLITSMKDN QRFFCVRDHD GKLQPAFISV
     RNGNAVHLDN VIKGNERVLV PRLEDAKFFF DEDQKMTIDQ YVDRLKNVSF HDQISSMYDK
     MARTKALANL LGQQLGLSDQ ELADLARAAS IYKFDLTTQM VGEFAELQGI MGEIYAKRFG
     ENEAVAAAVR EHYMPISADG ALPQTTVGTV LAIADKLDSI YSFFAVDMIP SGSNDPYALR
     RQAYGIVRML ADRKWHLNLL DFQASAKQAV EQATPALGLD YAKNADAVTD FFIDRLKQLF
     SLDHLRHDIV DAVTDTHVTD PAAIVEAAHV LDAHKDDADL KDQVEALTRV IRLAAKGNLS
     EDDVKVDPSL FENPSEGQLD QAVQALIDAK EGRSLDQQFS ALLELEPVIS LYFEENMIMD
     KDEAVKNNRL SLLTILADQT AAFGNLDQLI VK
 
 
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