ID   SYGB_PSEA8              Reviewed;         684 AA.
AC   B7V0P3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=PLES_00071;
OS   Pseudomonas aeruginosa (strain LESB58).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=557722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LESB58;
RX   PubMed=19047519; DOI=10.1101/gr.086082.108;
RA   Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA   Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA   Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA   Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT   "Newly introduced genomic prophage islands are critical determinants of in
RT   vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT   aeruginosa.";
RL   Genome Res. 19:12-23(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}.
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; FM209186; CAW24735.1; -; Genomic_DNA.
DR   RefSeq; WP_003120686.1; NC_011770.1.
DR   AlphaFoldDB; B7V0P3; -.
DR   SMR; B7V0P3; -.
DR   KEGG; pag:PLES_00071; -.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
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..684
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000197211"
SQ   SEQUENCE   684 AA;  73947 MW;  7410DF34DF904A3C CRC64;
     MSAKDFLVEL GTEELPPKAL NSLGEAFLSG IEKGLKAAGL SYAAARFYAA PRRLAVLVEQ
     LAVQQPDRTV NLDGPPLQAA FDASGNPTQA ALGFAKKCGV DLQQIDKSGP KLRFSQTIAG
     QPAAGLLPGI VEASLNELPI PKRMRWAARR EEFVRPTQWL VMLFGDDVVE CEILAQKAGR
     ESRGHRFHNP DNVRISSPAA YLEDLRGAHV LADFAERREL IAKRVAELAA EQQGSAIVPP
     SLLDEVTALV EWPVPLVCSF EERFLEVPQE ALITTMQDNQ KYFCLLDANG KLLPRFITVA
     NVESKAPENI VSGNEKVVRP RLTDAEFFFK QDKKQPLESF NERLRNVVFQ AQLGTVFEKA
     QRVSGLAAYI AERIGGNAQN ASRAGILSKC DLATEMVGEF PEMQGIAGYY YATHGGEAED
     VALALNEQYM PRGAGAELPS TLTGAAVAVA DKLDTLVGIF GIGMLPTGSK DPYALRRAAL
     GVLRILIEKQ LDLDLVAAVN AAVEQYGDKV KAAGLAEQVL DFVFDRLRAR YEDEGVDVAV
     YQSVRALKPS SPLDFDQRVQ AVQAFRQLPE AEALAAANKR VSNILAKSED EVPPNVDASL
     LVEAAEKALG SAVANAESEV APLAAARDYR AALARLAALR EPVDTFFADV MVNVDDAAVR
     ANRYALLAKL RGSFLGVADI SLLG