ID   SYGB_DESAH              Reviewed;         689 AA.
AC   C0QJ89;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=HRM2_28130;
OS   Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS   HRM2) (Desulfobacterium autotrophicum).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulforapulum.
OX   NCBI_TaxID=177437;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43914 / DSM 3382 / VKM B-1955 / HRM2;
RX   PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA   Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA   Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA   Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA   Meyerdierks A., Gottschalk G., Amann R.;
RT   "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT   reducer oxidizing organic carbon completely to carbon dioxide.";
RL   Environ. Microbiol. 11:1038-1055(2009).
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; CP001087; ACN15902.1; -; Genomic_DNA.
DR   RefSeq; WP_015904665.1; NC_012108.1.
DR   AlphaFoldDB; C0QJ89; -.
DR   SMR; C0QJ89; -.
DR   STRING; 177437.HRM2_28130; -.
DR   EnsemblBacteria; ACN15902; ACN15902; HRM2_28130.
DR   KEGG; dat:HRM2_28130; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_7; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000000442; 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   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..689
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000204601"
SQ   SEQUENCE   689 AA;  75662 MW;  25A55CE9DDDF28CE CRC64;
     MNNLLIEIGA EEIPAGYILP ALTSFCDRVT AALTGARINH GKTAVFGTPR RLALMVEDVQ
     ACQAPQKTTL MGPPQRIGFD NEGKPTLAGV KFAEKAGIVP EEIIITDNGK GPYLSAVIEE
     SCLLTEAILE GVLPELIQAI PFPKSMHWGD LDVTFARPIV SLTALLGKTV LNFKIGNIAS
     ASFVFGHSFM APERFELESA DAYLDTLRKA GVVADIGERR TILKESIKAA ADKACATIIE
     DEELVDIVNN LVEYPYPVVG HFDEVFLELP DEVLITAMRE HQKYFALADT AGKLMPCFIA
     VNNTRARDMD VVAKGHGKVI RARLADAQFF YHVDLESTLD DFVEKLKAVT FQASLGSMYE
     KTGRLVVLVE FLAGLVNADQ ELQKKLMRAA RLSKADLVSQ MVIEFTKLQG IIGRVYAQKG
     GEDPEVAMAI EEHYRPVYSG GDLPRTDTGK ILAIADKTDT LCGCFSANLI PTGASDPYAL
     RRQSIGILQI MLEAGFDFSL RALVRRGVAQ YQTDPDKKNE ISTQILEFLK GRMTNMLVDQ
     GFSREAVNAA LSVSFYNVPD AFLRIKALDI LRQEPDFEPL STAFKRVVNI LKKAGGDAKT
     RVNVNLFNCD AEKALHQACG EVTERVDTCI KAGDYGAALK EISTLRPHVD RLFEDVMVMD
     DDVALRINRM ALLSSVAALF RNIADFSQI