ID   SYGB_GEOSL              Reviewed;         687 AA.
AC   Q74FM7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 113.
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=GSU0579;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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; AE017180; AAR33910.1; -; Genomic_DNA.
DR   RefSeq; NP_951637.1; NC_002939.5.
DR   RefSeq; WP_010941242.1; NC_002939.5.
DR   AlphaFoldDB; Q74FM7; -.
DR   SMR; Q74FM7; -.
DR   STRING; 243231.GSU0579; -.
DR   PRIDE; Q74FM7; -.
DR   EnsemblBacteria; AAR33910; AAR33910; GSU0579.
DR   KEGG; gsu:GSU0579; -.
DR   PATRIC; fig|243231.5.peg.577; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_7; -.
DR   InParanoid; Q74FM7; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000000577; 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   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..687
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000006362"
SQ   SEQUENCE   687 AA;  74631 MW;  5AD7A10D6EFB2221 CRC64;
     MSKELFLEIG TEEIPAGFLP KAMADMEAIV TKELENARLA FGEVKTFATP RRLALVVKGL
     PTVQPDAEIT ALGPARNIAF GPDGTPSKAA EGFARGQGVD VASLTLVSTE KGEYVAAVRK
     ESGRPVPDLL AEILPRLVGG IPFRKSMRWA DLDVRFARPI HWIVALFDGV VVPFAFGNVQ
     SGNVSRGHRF MANQPFPVRD FAHYLDECER HFVIPDPERR KETIRREIHR VAKTAGGHLL
     PDEGLLDEVA YLVEYPSVVH GTFSPDFLKV PREVLITSMR SHQRYFSIVD DAGKLMPGFI
     TINNTLTEDP SVVVKGNERV LRARLSDARF FFEEDQKVKL ETRVESLKNV VYQQKLGTSY
     EKMERFRALA EGLADLLNPA VKAKTSRAAF LCKADLVSGM VGEFPEVQGI MGREYALLQG
     EDAEVAAAIA EHYLPTQAGG DLPASDIGAF VSIADKLDTI CGCFGVGLIP TGSADPYALR
     RSALGIINII LDRGCRLSLE GEIGKALELL SAKLTRPAAE VMADVLEFFR GRFVNLMADR
     YPADAVDAAI AAGFDDLVDA EARIGALAAF KGRPDFDSLA VAFKRVCNIV KDGVDQPVDA
     ALFQEPAEGA LFAAFQQVRA DVEARTASGD YLAALTGIAA LKGAVDDFFD KVMVMAEDER
     VRTNRLALLT GIARLFGGVA DFAKIAA