ID   SYGB_VIBC3              Reviewed;         688 AA.
AC   A5F487; C3M308;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, 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};
GN   OrderedLocusNames=VC0395_A2499, VC395_0160;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(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; CP000627; ABQ21154.1; -; Genomic_DNA.
DR   EMBL; CP001235; ACP08187.1; -; Genomic_DNA.
DR   RefSeq; WP_001040221.1; NZ_JAACZH010000018.1.
DR   AlphaFoldDB; A5F487; -.
DR   SMR; A5F487; -.
DR   STRING; 345073.VC395_0160; -.
DR   EnsemblBacteria; ABQ21154; ABQ21154; VC0395_A2499.
DR   GeneID; 57741478; -.
DR   KEGG; vco:VC0395_A2499; -.
DR   KEGG; vcr:VC395_0160; -.
DR   PATRIC; fig|345073.21.peg.151; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000000249; Chromosome 2.
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..688
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000071880"
SQ   SEQUENCE   688 AA;  75925 MW;  9B6A9A21715D2B39 CRC64;
     MAKEFLIELG TEELPPKQLR TLAEAFAANF AAELATADIA HEGVTWFATP RRLALKVANL
     AESQPDRVVE KRGPAVNVAF DADGKPTKAA EGWARGNGIT VEQAERLVTD KGEWLLFKEQ
     VQGQQTASVV VEMAAKALAN LPIAKPMRWG DKETQFIRPV KTLTILFGSE LIQGEILGVA
     SARTLRGHRF MGEAEFTIES AEQYPAILEE RGKVIADYAT RKAMIIEGSQ QAAQQLGGIA
     DLEDALVEEV TSLVEWPVVM TAKFEEKFLK VPAEALVYTM KGDQKYFPVY DASKKLLPNF
     IFVSNIESKE PRHIVEGNEK VVRPRLADAE FFFNTDRKRP LVDRLPLLEN AIFQQQLGTI
     KDKTDRITEL AGYIAEQIGA DVEKSKRAGL LAKCDLMTSM VFEFTDTQGV MGMHYARHDG
     EAEEVAVALN EQYMPRFAGD ELPSRGVSAA VAMADKLDTI VGIFGIGQAP KGSDPFALRR
     ASLGVLRILV EYGYQLDLVD LIAKAKSLFG DRLTNANVEQ EVIEFMLGRF PTWYQDAGFS
     IDIIQAVLAR NPTKPADFDQ RVKAVSHFRA LEEAEALAAA NKRVGNILAK YDGELGEEID
     LALLQEDAEK ALAEAVEIMA EALEPAFATG NYQEALSKLA GLRAPVDAFF DNVMVMADDE
     ALKKNRLTLL NKLRNLFLQI ADISLLQK