ID   SYGB_SHEON              Reviewed;         688 AA.
AC   Q8EKS6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 123.
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=SO_0014;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN53101.1; -; Genomic_DNA.
DR   RefSeq; NP_715656.1; NC_004347.2.
DR   RefSeq; WP_011070430.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EKS6; -.
DR   SMR; Q8EKS6; -.
DR   STRING; 211586.SO_0014; -.
DR   PaxDb; Q8EKS6; -.
DR   KEGG; son:SO_0014; -.
DR   PATRIC; fig|211586.12.peg.14; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   PhylomeDB; Q8EKS6; -.
DR   BioCyc; SONE211586:G1GMP-14-MON; -.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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   SMART; SM00836; DALR_1; 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..688
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000006405"
SQ   SEQUENCE   688 AA;  74936 MW;  B3BF14AE852D3532 CRC64;
     MNFENLLIEL GTEELPPKAL RKLAESFLAN FTEELTKADL AFKSAVWYAA PRRLALNITE
     LAIAQADKIV EKRGPAVSSA FDAGGKPTKA AEGWARGNGI TVDQAERLVT DKGEWLVYNA
     KVEGVETKSL VAAMAQRALD KLPIPKPMRW GSSKTQFIRP VHTATMLLGS ELIEGELLGI
     KSARNIRGHR FMGTGFELDH ADNYLTLLKE KGKVIADYES RKALIKADAE KAAAKIGGTA
     DIEDALLEEV TSLVEWPVVL TASFEEKFLS VPSEALVYTM KGDQKYFPVF DDAGKLLPNF
     IFVANIESKD PAQIISGNEK VVRPRLADAE FFFNTDKKHT LESRLPSLET VLFQQQLGTL
     KDKVTRISAL AAFIAEQTGA NAVDAARAGL LSKTDLMTNM VMEFTDTQGT MGMHYARLDG
     ETEAVALAME EQYKPKFSGD TVPTAAVSCA VALADKLDTL VGIFGIGQAP KGAADPFALR
     RAAIGVLRII VENKLPLDLV TLIAKAQELH GANLSNANAS EEVLEFLMAR FRAWYQDKGI
     NVDVILAVLA RRPTRPADFD SRINAVSHFR GLEASSALAA ANKRVSNILA KVEGELPSSV
     NVALLSEAAE QALAAKLAEL QPQLAPLFAN ADYQQALTLL ASLRESVDQF FEDVMVMADD
     AALRNNRLAL LNNLREQFLH VADISLLQ