ID   SYGB_CROS8              Reviewed;         689 AA.
AC   A7MKS3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=ESA_04169;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU79350.1; -; Genomic_DNA.
DR   RefSeq; WP_012126294.1; NC_009778.1.
DR   AlphaFoldDB; A7MKS3; -.
DR   SMR; A7MKS3; -.
DR   EnsemblBacteria; ABU79350; ABU79350; ESA_04169.
DR   KEGG; esa:ESA_04169; -.
DR   PATRIC; fig|290339.8.peg.3708; -.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000000260; 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_1000006359"
SQ   SEQUENCE   689 AA;  76138 MW;  58C8AD0F48894083 CRC64;
     MSEKTFLVEI GTEELPPKAL RSLAESFAAN FTAELDAAGL AHGVVSWFAA PRRLALKVAN
     LAASQPDREV EKRGPAVSAA FDAEGNPSKA AEGWARGCGI TVDQAERLVT DKGEWLMYRA
     HVKGESAQAL LPNMVSTALS KLPIPKLMRW GASDVQFVRP VHTVTLLLDD EVLPATILGI
     QSDRVIRGHR FMGEPEFTID HADQYPQILL ERGKVIADYN ARKAKIQQDA EAAAAKIGGN
     ADLSDSLLEE VTSLVEWPVV LTAKFEEKFL AVPAEALVYT MKGDQKYFPV YGTDGKLLPN
     FIFVANIESK DPRQIISGNE KVVRPRLADA EFFFNTDRKK RLEDHLPRLE TVLFQQQLGT
     LRDKTDRIQA LSGWIASQIG ADVNHATRAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
     GESEDVAVAL NEQYMPRFAG DALPSSLVAC AVAIADKMDT LAGIFGIGQH PKGDKDPFAL
     RRAALGVLRI IVEKNLPLDL QTLTEEAVRL YGSKLTNAKV VDDVVDFMLG RFRAWYQDEG
     YSVDTIQAVL ANRPTRPADF DARMKAVSHF RTLDEAVALA AANKRVSNIL AKATEPLNDE
     VHASVLKEDP EIRLALQVAV MRDKLQPLFA EGRYQEALVE LAQLREPVDE FFEKVMVNAD
     DAQVRINRLT LLSKLRALFL QVADISLLQ