SYGB_RHIEC
ID SYGB_RHIEC Reviewed; 704 AA.
AC Q2KBT5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 112.
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=RHE_CH00890;
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251;
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; CP000133; ABC89701.1; -; Genomic_DNA.
DR RefSeq; WP_011424238.1; NC_007761.1.
DR AlphaFoldDB; Q2KBT5; -.
DR SMR; Q2KBT5; -.
DR STRING; 347834.RHE_CH00890; -.
DR EnsemblBacteria; ABC89701; ABC89701; RHE_CH00890.
DR KEGG; ret:RHE_CH00890; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_1_5; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000001936; 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; 2.
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..704
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101320"
SQ SEQUENCE 704 AA; 77046 MW; 394BA1F580C7D556 CRC64;
MPNLLLELRS EEIPARMQRK AAGDLKKLVT DALVEAGLSY EGAREYWTPR RLALDIHGLT
ARSADVREER KGPRTDANEK AIEGFLRGAG LSSISEAQVV NDPKKGDFYV AVISKPGRAT
EEIVAEVMPG IIRDFPWPKS MRWGKASSAP GALRWVRPLQ SIVCTFGPEH EETTVIPFEI
DGITASNITY GHRFHAPEAI MVRRFDDYAA SLERAKVILD AERRKDIILH DARDIAFANG
LELVEDEGLL EEVSGLVEWP QVLMGSFEED YLSIPSEIIR LTIKTNQKCF VTRKQGEDTL
SNRFILVSNI EASDGGKEIV HGNGKVVRAR LSDALHFWKR DQGNLPDLET LAASAAKFGL
DLQKPLDQRM AKLDALDVTF HAKLGTQGAR VARIRALAQK LAAVTGADAA LTDRAAVLAK
ADLRTEAVGE FPELQGLMGR KYAALQGENA SVAAAIEDHY KPQGPSDRVP EDKVAITLAL
ADKLDTLTGF WAIDEKPTGS KDPFALRRAA LGVVRILLER GIRLPLLATT RDGDLLSFFH
DRLKVYLRDQ GARHDLIDAV LTPEADDLLM VARRVEALTA FITSEDGKNL LAGTKRATQL
LAAEEKKGTV IADGVSPALF KLDAEKELFA AISSASKDAA NAVAGEDFRS AMEALSKLRG
PVDRFFEDVL VNDEDAAIRA NRLALLRLIR EATGTVADFS KISG