ID   SYGB_LISIN              Reviewed;         688 AA.
AC   Q92BQ2;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 103.
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=lin1495;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL596168; CAC96726.1; -; Genomic_DNA.
DR   PIR; AF1619; AF1619.
DR   RefSeq; WP_010991561.1; NC_003212.1.
DR   AlphaFoldDB; Q92BQ2; -.
DR   SMR; Q92BQ2; -.
DR   STRING; 272626.lin1495; -.
DR   EnsemblBacteria; CAC96726; CAC96726; CAC96726.
DR   KEGG; lin:glyS; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000002513; Chromosome.
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_0000072910"
SQ   SEQUENCE   688 AA;  78641 MW;  9C42FAD805648429 CRC64;
     MSKDFLLEIG LEEMPAKYVT SSVLQLEKRV TDWLKDNQIE FKEIKTYSTP RRLTVLVEEM
     AEEQANRVEE AKGPAKKIAL DDEGNWSKAA LGFAKSQKVA PEDLTFREIK GVEYIYIKKE
     VIGEKTTALL PSLEKVVTSM TFPVSMHWGS NDLRYIRPIK WLIAMFGEEI IPFEITGVST
     SNTSRGHRFL GKTATINQPS DYPHALLEQF VVVNASERKQ AIVEQLRELE TMENWQIRED
     DDLLEEVTNL VEYPTVLAGN FEKEYLELPE EVLITTMKEH QRYFPVFSQE GELLPHFVTV
     RNGNHENLDT VARGNEKVLR ARLSDADFFY QEDLKITIDE AVAKLQNIVF HEKLGTLTEK
     MERVQKVALM LADYLNWQEE DKQDIIRLTN IYKFDLVTNI VGEFPELQGL MGEKYALLQG
     EKPAIATAIR EHYLPSSAEG VLPQTDLGSL IAIADKLETL IGFFCVNIVP TGSADPFGLR
     RSAFGAMRII QANGWDIPML EVISRIVDME RAEGATELPS ADVKKEVQTF LKNRLRVILQ
     GHHIRHDIID AVIGGDPNVI PQLIDRAQIL NKHADAEWFR PTIEALTRVV KISKKYEDGV
     EVDPNLFENE YEQELFDKLE KLKYDYAGLT IVDRLKAFAD LRTTIDGYFD NTLVMTDNDE
     LKNNRLALLF ELASFIKEFA QMDEINVK