ID   SYGB_PROMH              Reviewed;         690 AA.
AC   B4EZ95;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=PMI2855;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(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; AM942759; CAR45626.1; -; Genomic_DNA.
DR   RefSeq; WP_012368525.1; NC_010554.1.
DR   AlphaFoldDB; B4EZ95; -.
DR   SMR; B4EZ95; -.
DR   STRING; 529507.PMI2855; -.
DR   DNASU; 6802649; -.
DR   EnsemblBacteria; CAR45626; CAR45626; PMI2855.
DR   GeneID; 6802649; -.
DR   KEGG; pmr:PMI2855; -.
DR   PATRIC; fig|529507.6.peg.2786; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000008319; 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..690
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101316"
SQ   SEQUENCE   690 AA;  76917 MW;  BBB6AE04BED470E3 CRC64;
     MTTETFLVEI GTEELPPKAL RSLAESFATH FTAELDNANI THGDVSWFAA PRRLAIKVAN
     MAKSQADRIV EKRGPAIAQA FDAEGKPTKA AEGWARGNGI TVDQAERLST DKGEWLFYRA
     EVKGEAVNQL LAGMVSNALA KLPIPKLMRW GDKETHFVRP VHTVTLLLGD TLIDGEILGV
     QSARIIRGHR FMGEAEFTID NADQYPEILY ERGKVIADYE NRKSIILHDA RLAAEKLGGV
     ADLSDSLVEE VTSLVEWPVV LTAKFEEKFL EVPAEALVYT MKGDQKYFPV YDKQGALLPH
     FIFVSNIESS DPQQIISGNE KVVRPRLADA EFFFKTDRKQ RLEDNLPRLE TVLFQKNLGS
     LRDKTDRIQA LAGFIAEKMG ADVNKATRAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
     GEDEEVAVAL KEQYQPRFAG DALPSNPVAS AVAIAEKMDT LAGIFGIGQH PKGDKDPFAL
     RRAALGVLRI IVEQDLPLDI EELTQEAARL YGDKLTNQNV VSDVVEFMLG RFRAWYQELG
     YSIDTIQAVL ARRPTQPADF NARVKAVTYF RTLEEAAALA EANKRVSNIL AKSADVKLND
     KVLASVLKAP EEVQLAANLS VLQDKLAPLF AERKYQEALV ELASLRDVVN NFFDKVMVMD
     KDEEIRVNRL TMLHELRELF LKVADISVLQ