ID   SYGB_SHEHH              Reviewed;         689 AA.
AC   B0TLA9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=Shal_0006;
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) 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; CP000931; ABZ74582.1; -; Genomic_DNA.
DR   RefSeq; WP_012275140.1; NC_010334.1.
DR   AlphaFoldDB; B0TLA9; -.
DR   SMR; B0TLA9; -.
DR   STRING; 458817.Shal_0006; -.
DR   EnsemblBacteria; ABZ74582; ABZ74582; Shal_0006.
DR   KEGG; shl:Shal_0006; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000001317; 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   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_1000078548"
SQ   SEQUENCE   689 AA;  75525 MW;  DD2C0CD7B30372DF CRC64;
     MNFENLLIEV GTEELPPKSL RKLAESFLAN FTEELTKAEL SFDSAVWHAS PRRLAICINQ
     LALAQADKVV EKRGPAIAQA FDADGNPTKA AQGWARGNGI SVEQAERLKT DKGEWLLHQA
     RVVGVETKSL IADMAQRSLD KLPIPKPMRW GSNTTQFIRP VHTVTMLLGS EVVEGELLGI
     KSDRVIRGHR FMGESSFELD HADNYLVALK EKGKVLADYQ ARKAIIKTDA EAAAAKIGGV
     ADLEDDLLEE VTSLVEWPVV LTASFEEKFL DVPAEALVYT MKGDQKYFPV FDNAGQLLPN
     FIFVTNIESK DPQQIISGNE KVVRPRLADA EFFFETDKKE SLEARLASLE TVVFQKQLGT
     IKQRVERISA LAGYIATSIN ANSEEAARAG LLSKSDLMTN MVMEFTDLQG TMGMHYARLN
     GETEAVAVAL AEQYKPKFSG DTVPTAPISI CVALAEKLDT LVGIFGIGQA PKGAADPFAL
     RRAAIGVLRI CLENNLPLDL VDLIAKAQEL HGENLTNENV AEQVLEFFMG RFRAWYQDQG
     VSVDVILAVL ARRPTAPADF ESRIKAVAHF RTLEQASALA AANKRVSNIL AKVEGELPAA
     IDDKLLVEEA EKALAAKLAE LQPQLAPLFA AANYQEALAL LASLRESVDT FFEDVMVMAD
     DEALKNNRLA LLSSLREQFL HAADISLLQ