SYG_BORAP
ID SYG_BORAP Reviewed; 445 AA.
AC Q0SNE2; G0IS15;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Glycine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00253};
DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00253};
DE AltName: Full=Glycyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00253};
DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00253};
GN Name=glyQS {ECO:0000255|HAMAP-Rule:MF_00253};
GN OrderedLocusNames=BAPKO_0380, BafPKo_0370;
OS Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=390236;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo;
RX PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA Wilske B., Platzer M.;
RT "Comparative genome analysis: selection pressure on the Borrelia vls
RT cassettes is essential for infectivity.";
RL BMC Genomics 7:211-211(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo;
RX PubMed=22123755; DOI=10.1128/jb.05951-11;
RA Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA Fraser-Liggett C.M., Schutzer S.E.;
RT "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT Lyme disease agent isolates.";
RL J. Bacteriol. 193:6995-6996(2011).
CC -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly).
CC {ECO:0000255|HAMAP-Rule:MF_00253}.
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_00253};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00253}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00253}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00253}.
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DR EMBL; CP000395; ABH01636.1; -; Genomic_DNA.
DR EMBL; CP002933; AEL69596.1; -; Genomic_DNA.
DR RefSeq; WP_011600985.1; NC_017238.1.
DR AlphaFoldDB; Q0SNE2; -.
DR SMR; Q0SNE2; -.
DR STRING; 390236.BafPKo_0370; -.
DR EnsemblBacteria; AEL69596; AEL69596; BafPKo_0370.
DR KEGG; baf:BAPKO_0380; -.
DR KEGG; bafz:BafPKo_0370; -.
DR PATRIC; fig|390236.22.peg.363; -.
DR eggNOG; COG0423; Bacteria.
DR HOGENOM; CLU_015515_2_1_12; -.
DR OMA; EPSYGID; -.
DR OrthoDB; 626850at2; -.
DR Proteomes; UP000005216; 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; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00774; GlyRS-like_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_00253_B; Gly_tRNA_synth_B; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR027031; Gly-tRNA_synthase/POLG2.
DR InterPro; IPR022961; Gly_tRNA_ligase_bac.
DR InterPro; IPR033731; GlyRS-like_core.
DR InterPro; IPR002315; tRNA-synt_gly.
DR PANTHER; PTHR10745; PTHR10745; 4.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01043; TRNASYNTHGLY.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00389; glyS_dimeric; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..445
FT /note="Glycine--tRNA ligase"
FT /id="PRO_1000047371"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 177..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 187..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 192..196
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 262..263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 304..308
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 308..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
SQ SEQUENCE 445 AA; 52256 MW; 6D5F64579D49549A CRC64;
MVRMEDIISL AKRKGFVFQS SEVYGGLSGV WDYGPLGIEL KENIKREWWK SMVYLHENIV
GLDSAIFMRS EIWKASGHID GFSDSMVDCK DCKSRFRADF VDLSKNCPNC KVGNNFTSPR
NFNLMFKTHI GVVEDSSSEI YLRPETAQGI FVNFRNVLDS SRLKIPFGIA QVGKAFRNEI
VAKNFIFRTC EFEQMEMQFF VHPKQIDEWF CYWQQNRMNF FIETLKIRPD RLRLKAHNST
ELAHYAKSAF DIEYEFPFGF QEIEGIHNRG NYDLTQHSKF SNNSKVFEYH DLLTKERYVP
YVIETSAGLT RSVLMTLCDA YSEEELSDGD KRIVLRLHPK LAPYKIAIFP LVKKVELVEV
ARRIYVELCD DFHIFYDDSG TIGKRYRRQD EIGTPYCVTV DYNTIEDETV TVRERNNMTQ
KRIFINDLYS YIKTEILNYK EDVNK
