ID   SYGB_SHEPC              Reviewed;         689 AA.
AC   A4Y1A9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Sputcn32_0006;
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 / ATCC BAA-453;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000681; ABP73742.1; -; Genomic_DNA.
DR   RefSeq; WP_011918264.1; NC_009438.1.
DR   AlphaFoldDB; A4Y1A9; -.
DR   SMR; A4Y1A9; -.
DR   STRING; 319224.Sputcn32_0006; -.
DR   GeneID; 45040443; -.
DR   KEGG; spc:Sputcn32_0006; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
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   SMART; SM00836; DALR_1; 1.
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_1000006406"
SQ   SEQUENCE   689 AA;  75096 MW;  DCEE698740A4B841 CRC64;
     MNFENLLIEL GTEELPPKSL RKLAESFLAN FTEELTKADL AFSSAVWYAA PRRLAINVTE
     LALAQADKVV EKRGPAVSSA FDAEGKPTKA AEGWARGNGI TVEQAERLVT DKGEWLVHNA
     KVEGVETKSL IAAMAQRALD KLPIPKPMRW GNNKTQFIRP VHTATILLGS ELIEGELLGI
     KSARTVRGHR FMGLKQFELA HADHYLADLK EKGKVIADYE SRKALIKADA EKAAAKIGGT
     ADIEDSLLEE VASLVEWPVV LTASFEEKFL SVPSEALVYT MKGDQKYFPV FDNAGKLLPN
     FIFVANIESK DPAQIISGNE KVVRPRLADA EFFFNTDKKH TLESRLPSLE TVLFQQQLGT
     LKDKVNRISA LAAFIAEQTG ANAVDAARAG LLSKTDLMTN MVMEFTDTQG TMGMHYARLD
     GETEAVAVAM EEQYKPKFSG DTVPSAGVSC AVALADKLDT LVGIFGIGQA PKGAADPFAL
     RRAAIGVLRI IVENKLPLDL VTLIAKAQEL HGTHLSNANA SDEVLEFLMA RFRAWYQDKG
     IGVDVILAVL ARRPTRPADF DSRINAVSHF RSLEASGALA AANKRVSNIL AKVEGALPTT
     IDASLLTEAA EQALAAKLNE LQPQLAPLFA NADYQQALTL LAGLRESVDQ FFEDVMVMAD
     DEALKNNRLA LLNNLREQFL HVADISLLQ