ID   SYGB_LISMC              Reviewed;         688 AA.
AC   C1KVA5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=Lm4b_01468;
OS   Listeria monocytogenes serotype 4b (strain CLIP80459).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=568819;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIP80459;
RX   PubMed=22530965; DOI=10.1186/1471-2164-13-144;
RA   Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B.,
RA   Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A.,
RA   Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P.,
RA   Rusniok C., Buchrieser C., Goebel W., Chakraborty T.;
RT   "Comparative genomics and transcriptomics of lineages I, II, and III
RT   strains of Listeria monocytogenes.";
RL   BMC Genomics 13:144-144(2012).
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; FM242711; CAS05230.1; -; Genomic_DNA.
DR   RefSeq; WP_003726011.1; NC_012488.1.
DR   AlphaFoldDB; C1KVA5; -.
DR   SMR; C1KVA5; -.
DR   KEGG; lmc:Lm4b_01468; -.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   BioCyc; LMON568819:LM4B_RS07320-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   PANTHER; PTHR30075; PTHR30075; 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_1000204607"
SQ   SEQUENCE   688 AA;  78502 MW;  D377F42EF4AF3A62 CRC64;
     MSKDFLLEIG LEEMPAKYVT SSVLQLEKRV TDWLKDNQIE FKEIKTYSTP RRLTVLVEEM
     AEEQANRVEE AKGPAKKIAL DDEGNWSKAA LGFAKSQKVA PEDLTFREIK GVEYIYIKKE
     VIGEKTTALL PSLEKVVTSM TFPVSMHWGS NDLRYIRPIK WLIAMFGEEI IPFEITGVST
     SNTSRGHRFL GKTATINQPS DYPNALLEQF VVVNASERKQ AIVEQLRELE TMENWQIRED
     DDLLEEVTNL VEYPTVLAGN FEKEYLELPE EVLITTMKEH QRYFPVFSQE GELLPHFVTV
     RNGNHENLDT VARGNEKVLR ARLSDADFFY QEDLKITIDE AVAKLQNIVF HEKLGTLTEK
     MKRVQKVALM LADYLNWQEE DKQDIIRLTN IYKFDLVTNI VGEFPELQGL MGEKYALLQG
     EKPAIATAIR EHYLPSSAEG DLPQTDLGSL IAIADKLETL IGFFCVNIAP TGSADPFGLR
     RSAFGAVRII QANGWDIPML EVVSRIVDME RAEGATELPS SDVIKEVQTF LKNRLRVILQ
     GHHIRHDIID AVIGGDPNMI PQLIDRAQIL NKHADAEWFR PTIEALTRVV NISKKYEDGV
     EVDPSLFENE YEQALFDKLE KLKFDFAGLK IVDRLKAFAD LRTTIDAYFD NTLVMTDNDE
     LKNNRLALLF ELASFIKEFA QMDEINVK