ID   SYGB_ECO55              Reviewed;         689 AA.
AC   B7L6X3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-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};
GN   OrderedLocusNames=EC55989_4013;
OS   Escherichia coli (strain 55989 / EAEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=55989 / EAEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(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; CU928145; CAV00497.1; -; Genomic_DNA.
DR   RefSeq; WP_001291771.1; NC_011748.1.
DR   AlphaFoldDB; B7L6X3; -.
DR   SMR; B7L6X3; -.
DR   PRIDE; B7L6X3; -.
DR   EnsemblBacteria; CAV00497; CAV00497; EC55989_4013.
DR   KEGG; eck:EC55989_4013; -.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000000746; 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..689
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000197186"
SQ   SEQUENCE   689 AA;  76783 MW;  0176D52E30BAF729 CRC64;
     MSEKTFLVEI GTEELPPKAL RSLAESFAAN FTAELDNAGL AHGTVQWFAA PRRLALKVAN
     LAEAQPDREI EKRGPAIAQA FDAEGKPSKA AEGWARGCGI TVDQAERLTT DKGEWLLYRA
     HVKGESTEAL LPNMVATSLA KLPIPKLMRW GASDVHFVRP VHTVTLLLGD KVIPATILGI
     QSDRVIRGHR FMGEPEFTID NADQYPEILR ERGKVIADYE ERKAKIKADA EEAARKIGGN
     ADLSESLLEE VASLVEWPVV LTAKFEEKFL AVPAEALVYT MKGDQKYFPV YANDGKLLPN
     FIFVANIESK DPQQIISGNE KVVRPRLADA EFFFNTDRKK RLEDNLPRLQ TVLFQQQLGT
     LRDKTDRIQA LAGWIAEQIG ADVNHATRAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
     GEAEDVAVAL NEQYQPRFAG DDLPSNPVAC ALAIADKMDT LAGIFGIGQH PKGDKDPFAL
     RRAALGVLRI IVEKNLNLDL QTLTEEAVRL YGDKLTNANV VDDVIDFMLG RFRAWYQDEG
     YTVDTIQAVL ARRPTRPADF DARMKAVSHF RTLDAAAALA AANKRVSNIL AKSDEVLSDR
     VNASTLKEPE EIKLAMQVVV LRDKLEPYFA EGRYQDALVE LAELREPVDA FFDKVMVMVD
     DKELRLNRLT MLEKLRELFL RVADISLLQ