ID   SYGB_RUTMC              Reviewed;         678 AA.
AC   A1AWZ5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-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=Rmag_0721;
OS   Ruthia magnifica subsp. Calyptogena magnifica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC   Candidatus Ruthia.
OX   NCBI_TaxID=413404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17303757; DOI=10.1126/science.1138438;
RA   Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA   Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA   Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT   "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL   Science 315:998-1000(2007).
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; CP000488; ABL02452.1; -; Genomic_DNA.
DR   RefSeq; WP_011738077.1; NC_008610.1.
DR   AlphaFoldDB; A1AWZ5; -.
DR   SMR; A1AWZ5; -.
DR   STRING; 413404.Rmag_0721; -.
DR   EnsemblBacteria; ABL02452; ABL02452; Rmag_0721.
DR   KEGG; rma:Rmag_0721; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000002587; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   PANTHER; PTHR30075; PTHR30075; 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..678
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101330"
SQ   SEQUENCE   678 AA;  76074 MW;  D2D27FF951671018 CRC64;
     MNTKDFLLEL GCEELPPKCL QQLSNAFTHN LTTELDKLKL SYSSVESFAT PRRLAVLVSN
     LQLQQNDQII ERKGPSISAF DQDIEGFAKS CGVAKNVLVQ KTFGKTQYYF FTKQQKGLKT
     IDLLESTVDI AIQNISIIKP MRWSNLDTYF VRPTHWLIMM LGSDVVPASI MGLASGNTTR
     GLRFTGERIF DITCAKDYQK ILLERAQIEV DFNTRKEIIR KQVIQVAKNN NAIAVIDESL
     LDEVCALVEY PRAFSGNFSS KFLDVPEEAL ISAMKSHQKY FHMLDVDGNL MPVFISVANI
     ESSNLSVIID GNERVIRSRL ADSEFFWTQD KAHTLESRLD KLNQVLFMKS LGSMGDKIKR
     IEIFSGYIAT VIGANVKDSA RAGLLCKSDL VTDMVGEFAD LQGVMGGYYA LNDGENKAVA
     SAISEHYHPR FSGDSLPNTS EGLAVAIADK LDTVTGIIGI GQGPTGSKDP YALRRMALGL
     LRIMIESKLN LNLKELISKS LNENSSAVNI NSVDDIYQFM MRRLRAYYKE QKVNIQVFEA
     VLAVCPESPY DFHLRVEALN TFTNNQAFEN LIETNKRIAN ILKNYSNLLI KVDDSALVEV
     AEKALFKATK SLSKRILNST NYTKNIQELI AFKDIIDEFF DKVMVNTDDV VLRQARLNLI
     NWVRSLFLSV ADVSHLSL