ID   SYGB_SHESH              Reviewed;         689 AA.
AC   A8FP54;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Ssed_0014;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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; CP000821; ABV34627.1; -; Genomic_DNA.
DR   RefSeq; WP_012004153.1; NC_009831.1.
DR   AlphaFoldDB; A8FP54; -.
DR   SMR; A8FP54; -.
DR   STRING; 425104.Ssed_0014; -.
DR   PRIDE; A8FP54; -.
DR   EnsemblBacteria; ABV34627; ABV34627; Ssed_0014.
DR   KEGG; sse:Ssed_0014; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000002015; 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   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.
FT   CHAIN           1..689
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000078550"
SQ   SEQUENCE   689 AA;  75457 MW;  0B2F1FEDD632CC46 CRC64;
     MNFENLLIEV GTEELPPKSL RKLAESFLSN FTDELKKAEL SFESAVWHAA PRRLAICVNQ
     LALAQADKVV EKRGPAIAQA FDTDGNPTKA AMGWARGNGI TVEQAGRLKT DKGEWLLHQA
     KVVGVETKSL IAAMAQRSLD KLPIPKPMRW GNNTTQFIRP VHTVTMLLGS EVVEGELLGQ
     KSARIIRGHR FMGKASFELV HADNYLSALK EQGKVEANYE VRKALIKAGA EAAAAKIGGV
     ADLEDDLLEE VTSLVEWPVV LTANFEEKFL DVPAEALVYT MKGDQKYFPV FDKAGQLMPN
     FIFVTNIESK DPQQIIAGNE RVVRPRLADA EFFFETDKKD SLESRLTSLE TVIFQKQLGT
     IKDRVARISD MAGFIANSID ANADEAARAG LLSKSDLMTN MVMEFTDLQG TMGMHYARLN
     GETEAVALAL QEQYKPKFSG DTVPTAPVSV CVALAEKLDT LVGIFGIGQA PKGAADPFAL
     RRAAIGILRI CVENNLPLNL IDLIAKAQEL HGSNLTNDKA AEQVLEFFMG RFRAWYQDQG
     VSVDVILAVL ARRPTSPADF DSRIKAVSHF RSLEQASALA AANKRVSNIL AKVEGELPAA
     IDAGLLVENA EKVLAEKLNE LQPQLAPLFA AANYQEALAL LADLRESVDT FFEDVMVMAD
     DEALKNNRLA LLSSLREQFL HAADISLLQ