ID   SYGB_SINFN              Reviewed;         721 AA.
AC   C3MHD5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=NGR_c04670;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001389; ACP24263.1; -; Genomic_DNA.
DR   RefSeq; WP_012707048.1; NC_012587.1.
DR   RefSeq; YP_002825016.1; NC_012587.1.
DR   AlphaFoldDB; C3MHD5; -.
DR   SMR; C3MHD5; -.
DR   STRING; 394.NGR_c04670; -.
DR   EnsemblBacteria; ACP24263; ACP24263; NGR_c04670.
DR   KEGG; rhi:NGR_c04670; -.
DR   PATRIC; fig|394.7.peg.3275; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_1_5; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000001054; 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; 2.
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..721
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000197212"
SQ   SEQUENCE   721 AA;  79281 MW;  A18A6D2A5091231B CRC64;
     MPDLLIELRS EEIPARMQRK AAGDLKKLVT DALVEAGLTY EGAREYWTPR RLTLDIRGLN
     ARSADVREER KGPRTDANEK AIEGFLRAAG LSSIGDAHVH SDPKKGDFYV AHIVKPGRDA
     EDIVAEVMPA IIRDFPWPKS MRSGAASAKP GSLRWVRPLQ SIVCTFGAET EETRVIPFAV
     DGITASNITY GHRFHAPEAI MVRRFADYAD KLEKAKVVLD AERRKEIIGA DARNIAFANG
     LELVEDEGLL EEVTGLVEWP RVLMGSFEES YLEIPSEIIR LTIKTNQKCF VTRQPGAETL
     SNRFILVSNI EAKDGGKEIV HGNGKVVRAR LSDAAHFWKR DQGDLPDLET LKPSAEKFGL
     DLGKPLDQRM AKLDALNVTF HAKLGTQGER VARIRSIALA LAEVTGADQA LVERSVVLAK
     ADLRTEAVGE FPELQGIMGH KYAVLQGEDA AVANAIEDHY KPQGPSDRVP TDAVSAAVAL
     ADKLDTLAGF WAIDEKPTGS KDPYALRRAA LGVIRLILEG RTRLPLLPFF DVALKALRTQ
     RPDLTGDIAA DLLAFFHDRL KVYLRDLGAR YDLIDAVLTS EADDLLMIAR RVEALTAFIT
     AEEGKNLLAG TKRATQILAA EEKKGTEVAD QVDERLFRLD AERTLHASIK LASDDAREAI
     GKEDFRSAMA ALSKLREPVD VFFNDVLVND EDRAIRANRL ALLGLIRSAT GEVADFSKIS
     G