ID   SYGB_LEVBA              Reviewed;         691 AA.
AC   Q03SC5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=LVIS_0754;
OS   Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM
OS   1170 / LMG 11437 / NCIMB 947 / NCTC 947) (Lactobacillus brevis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Levilactobacillus.
OX   NCBI_TaxID=387344;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 / NCIMB
RC   947 / NCTC 947;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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; CP000416; ABJ63897.1; -; Genomic_DNA.
DR   RefSeq; WP_011667528.1; NC_008497.1.
DR   AlphaFoldDB; Q03SC5; -.
DR   SMR; Q03SC5; -.
DR   STRING; 387344.LVIS_0754; -.
DR   EnsemblBacteria; ABJ63897; ABJ63897; LVIS_0754.
DR   KEGG; lbr:LVIS_0754; -.
DR   PATRIC; fig|387344.15.peg.727; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000001652; 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..691
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101289"
SQ   SEQUENCE   691 AA;  75701 MW;  08EF7CEEF3B056D5 CRC64;
     MAHTFLLEIG LEEMPAHVVT PAIKQLVKRT ADYLKEERVD YDEIKPFSTP RRLAVLITGL
     ADKQRDISES VKGPAKKIAQ DAEGNWSKAA IGFTRGQGLT TDDITFKEIK GTEYVYVDKF
     IAGEPVATVL AGLKDVITAM TFPTMMKWST HHFQYIRPIR WLVALLDADV IPFSILDVTT
     DRNTRGHRFL GKDISIATAA DYEGDLTSEF VIADADKRKS MIKTQIDKLA ADHGWTVNVD
     AGLLEEVNNL VEWPTAFAGS FDEKYLTIPE EVLITSMRDH QRFFYARDAQ GQLLPTFISV
     RNGNDHDLQN VVSGNEKVLT ARLEDAMFFY TEDQKKTIAD YVERLKTVSF HDKISTMAEK
     MSRVKAIAGV LAKHVGLNDA QTKAVLRASE IYKFDLVTGM VGEFAELQGV MGEKYALLQG
     EDPAVAQAIR EHYEPISADG ALPASVPGAV LALADKFDSI LTFFAAGMIP SGSNDPYALR
     RQATGIVRIA QDQQWSLPVA DLAQAFVAAE TTANVAPKLD QAGQIDALVN FIKDRIRKIL
     RSAKQRHDII DAVTAGSSSD VLQIFTAADI LASHADDANF KDVIESLTRV IRLAQKAPAE
     VAATTVDPAL FENDSEGQLH QGVATVATAA KDGLTALYTA LADIQPVIAA YFDATMVMAK
     DDAVRNNRLA ELSRLADLAL ALGDLDQLVV K