ID   SYGB_LISMO              Reviewed;         688 AA.
AC   Q8Y754;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=lmo1458;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
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; AL591979; CAC99536.1; -; Genomic_DNA.
DR   PIR; AB1257; AB1257.
DR   RefSeq; NP_464983.1; NC_003210.1.
DR   RefSeq; WP_010990131.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y754; -.
DR   SMR; Q8Y754; -.
DR   STRING; 169963.lmo1458; -.
DR   PaxDb; Q8Y754; -.
DR   EnsemblBacteria; CAC99536; CAC99536; CAC99536.
DR   GeneID; 987668; -.
DR   KEGG; lmo:lmo1458; -.
DR   PATRIC; fig|169963.11.peg.1497; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OMA; LPIPKRM; -.
DR   PhylomeDB; Q8Y754; -.
DR   BioCyc; LMON169963:LMO1458-MON; -.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..688
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_0000072912"
SQ   SEQUENCE   688 AA;  78508 MW;  86A89F8457937A70 CRC64;
     MSKDFLLEIG LEEMPAQYVT SSVLQLEKRV TDWLTENKIE FGEIKTYSTP RRLTVLVEGM
     AEEQANRVEE AKGPAKKIAL DEEGNWSKAA LGFAKSQKVD PADLTFRDIK GVEYIYIKKE
     VIGEKTSTLL PSLEKVVTSM TFPVSMHWGS NDLRYIRPIK WLIAMFDEEI 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 QANGWNIPML EVISRIVDME RAEGSTELPD ADVKKEVQTF LKNRLRVILQ
     GHHIRHDIID AVIGGDPNVI PQLIDRAQIL NEHAEAEWFR PTIEALSRVV KIAKKYEDGV
     EVDPALFENE YEQALFDKLE KLKFDYAGLT IIERLKAFAD LRTTIDAYFD NTLVMSDNDE
     LKNNRLALLF ELASFIKEFA QMDEINVK