ID   SYGB_LACP3              Reviewed;         689 AA.
AC   Q038U3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=LSEI_1503;
OS   Lacticaseibacillus paracasei (strain ATCC 334 / BCRC 17002 / CCUG 31169 /
OS   CIP 107868 / KCTC 3260 / NRRL B-441) (Lactobacillus paracasei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=321967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 334 / BCRC 17002 / CCUG 31169 / CIP 107868 / KCTC 3260 / NRRL
RC   B-441;
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; CP000423; ABJ70279.1; -; Genomic_DNA.
DR   RefSeq; WP_003660846.1; NC_008526.1.
DR   RefSeq; YP_806721.1; NC_008526.1.
DR   AlphaFoldDB; Q038U3; -.
DR   SMR; Q038U3; -.
DR   STRING; 321967.LSEI_1503; -.
DR   EnsemblBacteria; ABJ70279; ABJ70279; LSEI_1503.
DR   KEGG; lca:LSEI_1503; -.
DR   PATRIC; fig|321967.11.peg.1485; -.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000001651; 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..689
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101290"
SQ   SEQUENCE   689 AA;  76109 MW;  1AF287F8352F3B27 CRC64;
     MTHQYLIEIG LEDMPAHVVT PSLQQFHDKT VAFLKENHLD HGAIDQYATP RRLALLIHDL
     ADKQEDVEED 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