ID   SYGB_MORCA              Reviewed;         266 AA.
AC   P77891;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Glycine--tRNA ligase beta subunit;
DE            EC=6.1.1.14;
DE   AltName: Full=Glycyl-tRNA synthetase beta subunit;
DE            Short=GlyRS;
DE   Flags: Fragment;
GN   Name=glyS;
OS   Moraxella catarrhalis (Branhamella catarrhalis).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25238 / DSM 9143 / BCRC 10629 / CIP 73.21 / NCTC 11020 / Ne 11;
RA   Walker E.S., Preston R.A., Post J.C., Ehrlich G.D., Klingman K.L.;
RL   Submitted (NOV-1996) 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;
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; U73324; AAB18210.1; -; Genomic_DNA.
DR   AlphaFoldDB; P77891; -.
DR   SMR; P77891; -.
DR   STRING; 857571.EA1_07730; -.
DR   eggNOG; COG0751; Bacteria.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   PANTHER; PTHR30075; PTHR30075; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..>266
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_0000072913"
FT   NON_TER         266
SQ   SEQUENCE   266 AA;  29491 MW;  8614880E16827072 CRC64;
     MTTILFELGT EELPPKNLKT LRDALKNSVG TLLNDQNISF DDIHAFAAPR RLALTITGVG
     EFQPDRIETK KGPSVKAAFD DAGNLTRAGQ GFLQGLNATG RNLSVKDLGR IADKKGEYIA
     YDLTIKGEKI TDLMPNILQK ALDDLPIAKR MRSGIDRHEF IRPVHWIVLM SDDVVIEATI
     QGHKTGNQSR GHRYHSPDFF AIDHADHYEN LLKNHHVIAD FDQRQADILA QVKTLADDVN
     GTAIMPQELL DEVTALVDLP VALRAS