ID   SYGB_ERWT9              Reviewed;         689 AA.
AC   B2VCH1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=ETA_34130;
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
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; CU468135; CAO98459.1; -; Genomic_DNA.
DR   RefSeq; WP_012443082.1; NC_010694.1.
DR   AlphaFoldDB; B2VCH1; -.
DR   SMR; B2VCH1; -.
DR   STRING; 465817.ETA_34130; -.
DR   PRIDE; B2VCH1; -.
DR   EnsemblBacteria; CAO98459; CAO98459; ETA_34130.
DR   KEGG; eta:ETA_34130; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000001726; 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_1000101280"
SQ   SEQUENCE   689 AA;  76032 MW;  6E2745577E42D21A CRC64;
     MTDKTFLVEI GTEELPPKAL RSLAESFAAN LTAELDAAGL AHGEVSWFAA PRRLALKVAN
     LSAAQPDREV EKRGPAIQAA FDANGVATKA AEGWARGCGI TVDQAERLST DKGEWLMYRA
     RVTGERTQVL LPAMIATSLA KLPIPKLMRW GASEVQFVRP VHTVTLLLGD ELIPANILGI
     DSARIIRGHR FMGEPEFTID HADQYPQILL ERGKVQADYA ARKAIIKADA EAAAAKIGGV
     ADLSDSLLEE VTSLVEWPVV LTATFEEKFL AVPAEALVYT MKGDQKYFPV YDKAGKLLPN
     FIFVTNIESK DPQQIISGNE KVVRPRLADA EFFFNSDRKR RLEDNLPRLE TVLFQKELGT
     LRAKTDRIQA LAGWVAAQIG ADVNHATRAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
     GEAEDVAVAL NEQYQPRFAG DELPSNPVAC ALAIADKMDT LAGIFGIGQH PKGDKDPFAL
     RRAALGVLRI IVEKNLPLDL QTLTEEAVRL YGSKLSNAKA VDEVVDFMLG RFRTWYQEEG
     HSVDTLQAVL ARRPTRPADF DARMKAVSHF RTLEQAASLA AANKRVSNIL AKATEPLNDS
     VQASLLKENE EIKLATYVTA LSSKLQPFFA EGRYQDALIE LAQLREAVDN FFDKVMVNAE
     EKEVRINRLT LLAKLRELFL QVADISLLQ