ID   SYGB_MARN8              Reviewed;         693 AA.
AC   A1TWM6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=Maqu_0038;
OS   Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS   aquaeolei).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Marinobacteraceae; Marinobacter.
OX   NCBI_TaxID=351348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX   PubMed=21335390; DOI=10.1128/aem.01866-10;
RA   Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA   Edwards K.J.;
RT   "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT   'opportunitroph'.";
RL   Appl. Environ. Microbiol. 77:2763-2771(2011).
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; CP000514; ABM17145.1; -; Genomic_DNA.
DR   RefSeq; WP_011783618.1; NC_008740.1.
DR   AlphaFoldDB; A1TWM6; -.
DR   SMR; A1TWM6; -.
DR   STRING; 351348.Maqu_0038; -.
DR   EnsemblBacteria; ABM17145; ABM17145; Maqu_0038.
DR   KEGG; maq:Maqu_0038; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000000998; 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..693
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000006379"
FT   REGION          65..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   693 AA;  76675 MW;  42D89CC8E0C63CAA CRC64;
     MATQDFLVEL GTEELPPKAL KPLSDAFTQG IVKGLEEAGV AFGAVESFAA PRRLAVRIRD
     LADAQPDKSV EKRGPAVKAA FDDSGNPTRA LTGFATSLGI TPDQLDTMET DKGAWLVYRT
     VEKGKPTVEL MPDLVEKSLA ALPIPKRMRW GAWKTEFVRP VHWLILLYGN KVIEAPVMNL
     KPGNKTRGHR FHCPKELIVP TPADYEVVLK QEGYVLADFA ERREQIRAGV AALAEKEAGG
     KAVIDEDLLD EVTALNEWPV PLMGRFEDRF LEVPAEALIS SMKEHQKYFH VVDASDNMLP
     LFITVANLES KDPSQVISGN EKVIRPRLSD AAFFYETDRK TRLEDRIESL KPIVFQDKLG
     SIYDKSVRVA ALAKKIAEAI NSDPALAERA AMLAKTDLVT EMVLEFTDLQ GIMGQYYAAN
     DGEHEDVAKA LNEQYMPRFA GDDLPTTLTG CAVAIADRID SLVGLFGINQ PPSGTRDPFA
     LRRASLGVLR IIIERQLPLD LQTVCEWAEQ NFTVLTENNT ASTVVDYMLD RFRAHYDEQG
     ICAEVYLAVH ARRPTRPLDF DRRVKAVEAF RQLPEAQALA GANKRVSNIL TKQGGDSIGE
     TVDTALLQDA AEKTLAAKVE EQAQQVLPMF EQGDYASALT SLASLREPVD TFFDEVMVMA
     DDDAVRNNRL ALLNRLRNLF LRVADISLLP TAG