ID   SYGB_PEDPA              Reviewed;         690 AA.
AC   Q03F66;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=PEPE_1101;
OS   Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 /
OS   183-1w).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=278197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w;
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; CP000422; ABJ68156.1; -; Genomic_DNA.
DR   RefSeq; WP_011673491.1; NC_008525.1.
DR   AlphaFoldDB; Q03F66; -.
DR   SMR; Q03F66; -.
DR   STRING; 278197.PEPE_1101; -.
DR   PRIDE; Q03F66; -.
DR   EnsemblBacteria; ABJ68156; ABJ68156; PEPE_1101.
DR   GeneID; 33062734; -.
DR   KEGG; ppe:PEPE_1101; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000000773; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
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:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   PANTHER; PTHR30075; PTHR30075; 1.
DR   Pfam; PF05746; DALR_1; 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..690
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000006381"
SQ   SEQUENCE   690 AA;  78148 MW;  91842C7C26D2D467 CRC64;
     MAHNYLLEIG LEEIPAHVVT PSIKQLVQKV TAFLKENRLT YDSIDHFSTP RRLAIRINGL
     GDQQPDIEED AKGPARKIAQ DADGNWTKAA IGFTRGQGLT VDDITFKTIK GTDYVYVHKL
     IKGKMTKEIL TGLKEVVESI NFPTMMKWAN FDFKYVRPIR WLVSILDEEV LPFSILDVTA
     GRRTEGHRFL GEAVELANAE EYEAKLHDQF VIVDADERKQ LISNQIKAIA ESNRWNVTPN
     PGLLEEVNNL VEWPTAFNGG FDEKYLAIPE EVLITSMRDH QRFFFVRDQA GKLLPNFISV
     RNGNEEFIEN VVRGNEKVLT ARLEDAAFFY EEDQKHDINY YVDRLKKVSF HDKIGSMYEK
     LQRVNSIAKV IGNTLNLNQT ELDDIDRATM IYKFDLVTGM VGEFSELQGV MGEKYAQLNG
     ENQAVAQAIR EHYMPNSAEG DLPESVTGAV VALADKFDNI FSFFSAGMIP SGSNDPYALR
     RHAYGIVRIL NSRDWQLDLN QFKSQVKTEL AENGTAFGVD VDQNFDQVLN FFNDRIKQLL
     DHQKISHDIV ETVLTGNNHD VTEIIEAAQV LADAKASSTF KDDIEALTRV QRIATKNEES
     GELNVDPQLF NNASEGELFD QIIKIEAANN LTMSQLFAKL CELTPAISKY FDATMVMDKD
     ENIKRNRLNM MSRLANLILK IGDLTNVLVK