ID   SYGB_CITBB              Reviewed;         687 AA.
AC   B5ED84;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=Gbem_0642;
OS   Citrifermentans bemidjiense (strain ATCC BAA-1014 / DSM 16622 / JCM 12645 /
OS   Bem) (Geobacter bemidjiensis).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Citrifermentans.
OX   NCBI_TaxID=404380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter bemidjiensis BEM.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001124; ACH37670.1; -; Genomic_DNA.
DR   RefSeq; WP_012529078.1; NC_011146.1.
DR   AlphaFoldDB; B5ED84; -.
DR   SMR; B5ED84; -.
DR   STRING; 404380.Gbem_0642; -.
DR   EnsemblBacteria; ACH37670; ACH37670; Gbem_0642.
DR   KEGG; gbm:Gbem_0642; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_7; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000008825; 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; Reference proteome.
FT   CHAIN           1..687
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101281"
SQ   SEQUENCE   687 AA;  75710 MW;  F46093145AC0006B CRC64;
     MAKDLFLEIG CEEIPAGFVP KAMADMELLI KKEFDSARIE YGEIVTLGTP RRLVLAVKGV
     AERQPDAELT AMGPAKSHAY DADGNPTKAA QGFARGQGID VSQLKLVTTE KGEYLAAVKS
     EIGRATAELL PELLPRLIGN IPFKKSMRWA DFDVRFARPI HWIVALFDGK VVPFSFGNID
     SGSASRGHRF MANTSFPVRD LAHYLEECER HFVIPDPNKR KEIIRAEIER VAKQAKGNVL
     PDEALLEQVS YLVEYPSAVH GTFSPDFLVV PREVLITSMR EHQRYFSLVD DEGKLLPGFI
     TINNTITEDP QVVVKGNERV LRARLSDARF FFDEDHKVRL EARVESLKSV VYQAKLGTSY
     EKMERFRELG KRLAQRLNPA VTKEVERAAT LCKADLVSGM VGEFPEVQGI MGREYALHDG
     EEKAVANAIA EHYLPTQAGG ELPASDIGAF VSLADKMDTI CGCFSVGLIP TGSADPYALR
     RSALGIINII LDKGYREPLS DFVKASLDLL SAKATRPLAE VQKDVLDFFR GRFVNLMADR
     FPSDAVEAVV SVSFDDLVEA AAKIEALAGF RNRDDFGPLA VAFKRVCNIV KDGVDTPVST
     ELFQDAAEGE LHQALTQVSG KVAAALKKAD YLAALTEIAT LKPAVDLFFE KVMVMAEDER
     VRQNRLALLT GIARLFGSLA DFSRLSP