ID   SYGB_COXBN              Reviewed;         689 AA.
AC   A9KBT7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=CBUD_0207;
OS   Coxiella burnetii (strain Dugway 5J108-111).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=434922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dugway 5J108-111;
RX   PubMed=19047403; DOI=10.1128/iai.01141-08;
RA   Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA   Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA   Heinzen R.A.;
RT   "Comparative genomics reveal extensive transposon-mediated genomic
RT   plasticity and diversity among potential effector proteins within the genus
RT   Coxiella.";
RL   Infect. Immun. 77:642-656(2009).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABS77223.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000733; ABS77223.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_043880992.1; NC_009727.1.
DR   AlphaFoldDB; A9KBT7; -.
DR   SMR; A9KBT7; -.
DR   EnsemblBacteria; ABS77223; ABS77223; CBUD_0207.
DR   KEGG; cbd:CBUD_0207; -.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000008555; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
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:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   PANTHER; PTHR30075; PTHR30075; 1.
DR   Pfam; PF05746; DALR_1; 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..689
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000078539"
SQ   SEQUENCE   689 AA;  77877 MW;  E46AC1A75576E9F1 CRC64;
     MTTQDFLLEI GCEELPPRRL NQLSQALSQT IKSELEKADL SFENIHRYAT PRRLAVLVNN
     LALQQPQRKI ERQGPSVKAA FDKDQTPTLA CFGFAQSCGV STAQLKVKKT KKGEFIYCEI
     EQPGQNTLDL LPNIIQSALK QLPTPKAMRW GDHKEFFVRP VHWIILMLGK DLVPATLLGK
     MASCETRGHR FHHPKNILVT KPDDYQKLLL THGMVIADFE KRREKIRDLI QKAASEKGEA
     IIDEGLLEEV TGMVEWPVIL VGNFKAEFLE LPPEVLITTM KVHQRTFPIK NKNGDLLPYF
     IIVSNIESKN PKRVIVGNER VINARLADAS FFYDNDLRTS LENRLPKLGD VIFQRQLGTL
     ADKARRIEKL AAFIAKQINI DEQLAARAGL LSKCDLVSEM VYEFPTLQGI MGYYYAFHDK
     EPPLVAEAIK EHYLPRFSGD QLPRNLLSAC VAVADRIDTI IGIIGINKSP TGDKDPFALR
     RAALGILRIL IEKELSLDLF ALLNEAKNNY AVELPNVNVA NQSFDFIIER LRAWYLEKEV
     PASVFMAVLA SHPADPLDFD RRIKAVQHFQ TLPEADALAA ANKRVSNILK KQAAELKSKT
     IDHSLFDSDA EHLLADQLKE RAELVNNLYK KADYTKALSE LASLKEPIDI FFDKVMVMVD
     DKEKRENRLA LLSSLQQLFS QIADISLLS