ID   SYGB_SHEFN              Reviewed;         694 AA.
AC   Q08A46;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=Sfri_0006;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000447; ABI69869.1; -; Genomic_DNA.
DR   RefSeq; WP_011635498.1; NC_008345.1.
DR   AlphaFoldDB; Q08A46; -.
DR   SMR; Q08A46; -.
DR   STRING; 318167.Sfri_0006; -.
DR   EnsemblBacteria; ABI69869; ABI69869; Sfri_0006.
DR   KEGG; sfr:Sfri_0006; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000000684; 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   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR30075; PTHR30075; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
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..694
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000006403"
SQ   SEQUENCE   694 AA;  75935 MW;  D87FECAF64569BB1 CRC64;
     MNFENLLIEV GTEELPPKAL RTLAESFLTS FTDELTKADL PFESAVWYAA PRRLAINVLG
     LALAQADKVV EKRGPAVSSA FDADGNPTKA AQGWARGNGI TVEQAERLVT DKGEWLVHQA
     KVVGVETKSL IADMAQRALD KLPIPKPMRW GNNKTQFIRP VHTVTMLLGS ELVAGELLGI
     TSNRIIRGHR FMGKASFELD HADNYLAALK EQGKVLADYE LRKSLIKADA EAAAAKLGGI
     ADIQDGLLEE VASLVEWPIV LTASFEEKFL NVPSEALVYT MKGDQKYFPV FDKAGKLLPN
     FIFVTNIESK DPQQIISGNE KVVRPRLADA EFFFNTDKKN TLESRIASLE TVVFQKQLGT
     LKARVERISE LAGFIATQMN NNGVETNSVD ASRAGLLSKT DLMTNMVMEF TDTQGTMGMH
     YARLDGETEA VAIALEEQYK PKFSGDTVPT ATVSCAVALA EKLDTLVGIF GIGQAPKGAA
     DPFALRRAAI GILRVIVENK LPLDLVELIA KAQALHATNI TNTNTSDDVL EFLLARFRAW
     YQDKGIQVDV ILAVLARRPT KPADFDSRVK AVSHFRGLEA STALAAANKR VSNILAKVEG
     ELPATINSAL LTEPAEKALA DKLVQLQPQL APLFADGNYQ QALTLLADLR ENVDQFFEDV
     MVMADDEALK NNRLALLTNL REQFLHVADI SLLQ