ID   SYGB_PSE14              Reviewed;         684 AA.
AC   Q48QJ1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=PSPPH_0011;
OS   Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS   (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1448A / Race 6;
RX   PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA   Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA   Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA   Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA   Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA   Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT   1448A reveals divergence among pathovars in genes involved in virulence and
RT   transposition.";
RL   J. Bacteriol. 187:6488-6498(2005).
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; CP000058; AAZ36340.1; -; Genomic_DNA.
DR   RefSeq; WP_002551325.1; NC_005773.3.
DR   AlphaFoldDB; Q48QJ1; -.
DR   SMR; Q48QJ1; -.
DR   STRING; 264730.PSPPH_0011; -.
DR   EnsemblBacteria; AAZ36340; AAZ36340; PSPPH_0011.
DR   GeneID; 61872715; -.
DR   KEGG; psp:PSPPH_0011; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000000551; 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.
FT   CHAIN           1..684
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000006385"
SQ   SEQUENCE   684 AA;  74853 MW;  7781A32A819BE3A2 CRC64;
     MSAQDFLVEL GTEELPPKTL VSLADAFLAG IEKGLSGAGL TYSAKQVYAA PRRLAVLITA
     LATQQPDRSV NLDGPPRQAA FDADGNPTQA ALGFAKKCGV DLSEIDQSGP KLRYSQTILG
     KPTTSLLPTI VEDSLNDLPI AKRMRWGARK EEFVRPTQWL VMLFGDQVVD CTILAQSAGR
     HSRGHRFHHP QDVRISSPAG YLSDLRAAHV LADFNERRQI ISKRVDELAT QQEGTAIVPP
     SLLDEVAGLV EWPVPLVCSF EERFLEVPQE ALITTMQDNQ KYFCLLDAEG KLLPRFITVA
     NIESKDPAQI VAGNEKVVRP RLTDAEFFFK QDKKQKLETF NDRLKNVVFQ AQLGSVFDKA
     ERVSKLAAYI APRIGGDAQR AARAGLLSKC DLSSEMVGEF PEMQGIAGYY YAKADGEPED
     VALALNEQYM PRGAGAELPT TLTGAAVAIA DKLDTLVGIF GIGMLPTGSK DPYALRRAAL
     GILRILIEKK LDLNLVETVK FAVTQFGAKI KPAGLAEQVL DFIFDRLRAR YEDEGVDVAV
     YLSVRALQPA SALDFDQRVQ AVQAFRKLPQ AAALAAVNKR VSNLLSKAEG SIAQTVEPKY
     FDNANEFSLY SAIQQADHAV QPMAAERQYS ESLARLAMLR EPVDAFFEAV MVNAEDANVR
     ANRYALLSRL RGLFLGVADI SLLG