ID   SYGB_LISMH              Reviewed;         688 AA.
AC   B8DE53;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=LMHCC_1112;
OS   Listeria monocytogenes serotype 4a (strain HCC23).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=552536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCC23;
RX   PubMed=21602330; DOI=10.1128/jb.05236-11;
RA   Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA   Lawrence M.L.;
RT   "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL   J. Bacteriol. 193:3679-3680(2011).
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; CP001175; ACK39460.1; -; Genomic_DNA.
DR   RefSeq; WP_012581310.1; NC_011660.1.
DR   AlphaFoldDB; B8DE53; -.
DR   SMR; B8DE53; -.
DR   KEGG; lmh:LMHCC_1112; -.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
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_1000197205"
SQ   SEQUENCE   688 AA;  78376 MW;  2F7B21D3B6811281 CRC64;
     MSKDFLLEIG LEEMPAQYVT SSVLQLEKRV TDWLTENKIE FGEIKTYSTP RRLTVLVEGM
     AEEQANRVEE AKGPAKKIAL DDEGNWSKAA LGFAKSQKVD PADLTFRDIK GVEYIYIKKE
     VIGEKTSTLL PNLEKVVTSM TFPVSMHWGS NDLRYIRPIK WLIAMFGEEI IPFEITGVTT
     SNTSRGHRFL GKSATIKQPS DYPNALLEQF VVVNAEERKQ AIVEQLRELE SMENWQIKED
     DDLLEEVTNL VEYPTVLSGN FEKEYLELPE EVLITTMKEH QRYFPVFSQA GELLPHFVTV
     RNGNHENLDT VARGNEKVLR ARLSDADFFY QEDLKMTIDE AVAKLQNIVF HEKLGTLTEK
     MKRVQKVALM LADYLDWQEE DKQDIIRLTN IYKFDLVTNI VGEFPELQGL MGEKYALLQG
     EKPAIATAIR EHYLPNSAEG ELPQTDLGSL IAIADKLETL IGFFCVNIVP TGSADPFGLR
     RSAFGAMRII QANGWDIPML EVISRIVDME RAEGSAELPG ADVKKEVQTF LKNRLRVILQ
     GHHIRHDIID AVIGGDPNVI PQLIDRAQIL NEHAEAEWFR PTIEALSRVV KIAKKYEDGV
     EVDPALFENE YEQALFDKLE KLKFDYAGLT IIERLKAFAD LRTTIDAYFD NTLVMSDNDE
     LKNNRLALLF ELASFIKEFA QMDEINVK