ID   SYGB_SALTI              Reviewed;         689 AA.
AC   Q8Z2B3;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 123.
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=STY4144, t3864;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD07973.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO71343.1; -; Genomic_DNA.
DR   RefSeq; NP_458271.1; NC_003198.1.
DR   RefSeq; WP_001291805.1; NZ_WSUR01000001.1.
DR   AlphaFoldDB; Q8Z2B3; -.
DR   SMR; Q8Z2B3; -.
DR   STRING; 220341.16504960; -.
DR   EnsemblBacteria; AAO71343; AAO71343; t3864.
DR   KEGG; stt:t3864; -.
DR   KEGG; sty:STY4144; -.
DR   PATRIC; fig|220341.7.peg.4234; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..689
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_0000072925"
SQ   SEQUENCE   689 AA;  76646 MW;  A93CC239351028D9 CRC64;
     MSEKTFLVEI GTEELPPKAL RSLAESFAAN FTAELDNAGL AHGTVQWFAA PRRLALKVAN
     LAEAQPDREI EKRGPAIAQA FDAEGKPSKA AEGWARGCGI TVDQAERLTT DKGEWLLYRA
     YVKGESTEAL LPNMVATSLA KLPIPKLMRW GASDVHFVRP VHTVTLLLGD KVIPATILGI
     QSDRVIRGHR FMGEPEFTID NADQYPEILR ERGKVIADYE ERKAKIKADA EEAARKIGGN
     ADLSESLLEE VASLVEWPVV LTAKFEEKFL AVPSEALVYT MKGDQKYFPV YANDGKLLPN
     FIFVANIESK DPQQIISGNE KVVRPRLADA EFFFNTDRKK RLEDNLPRLQ TVLFQQQLGT
     LRDKTDRIQA LAGWIAEQIG ADVNHATRAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
     GEAEDVAVAL NEQYQPRFAG DDLPSNPVAC ALAIADKMDT LAGIFGIGQH PKGDKDPFAL
     RRAALGVLRI IVEKNLNLDL QTLTEEAVRL YGDKLTNASV VDDVIDFMLG RFRAWYQDEG
     YSVDTIQAVL ARRPTRPADF DARMKAVSHF RTLEEASALA AANKRVSNIL AKATEPLNDI
     VHASVLKEAA EIELARHLVV LRDKLQPYFA DGRYQEALIE LAALRAPVDE FFENVMVNAE
     EKDIRINRLT LLSKLRELFL QVADISLLQ