SYGB_YERPB
ID SYGB_YERPB Reviewed; 689 AA.
AC B2K7F8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=YPTS_4134;
OS Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502801;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB1/+;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL Submitted (APR-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}.
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DR EMBL; CP001048; ACC91080.1; -; Genomic_DNA.
DR RefSeq; WP_002209623.1; NZ_CP009780.1.
DR AlphaFoldDB; B2K7F8; -.
DR SMR; B2K7F8; -.
DR GeneID; 66843665; -.
DR KEGG; ypb:YPTS_4134; -.
DR PATRIC; fig|502801.10.peg.3609; -.
DR OMA; LPIPKRM; -.
DR BioCyc; YPSE502801:YPTS_RS20825-MON; -.
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_1000101374"
SQ SEQUENCE 689 AA; 76204 MW; 715AF2AE0D639397 CRC64;
MTQQTFLVEI GTEELPPKAL RSLAESFAAN FTAELDNANL SHGEVSWYAA PRRLAVKVAN
LSAAQADREV EKRGPAIAQA FDAEGKPSKA AEGWARGCGI TVDQAERLVT DKGEWLLYRA
HVKGQPAQLL LAGMVNTALS KLPIPKLMRW GDKETQFVRP VHTVTLLLGT EVIPGTVLGI
NSDRVIRGHR FMGEAEFTID SADQYPQILL ERGKVIADYE LRKSIIKRDA EQAAQQIGGV
ADLSESLLEE VASLVEWPVV LTAKFEEKFL AVPAEALVYT MKGDQKYFPV YDTAGHLMPH
FIFVANIESK DPQQIISGNE KVVRPRLADA EFFFKTDRKK RLEDNLPRLE TVLFQQQLGT
LRDKTDRIQA LAGWVAAQIG ADVNHATRAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
GEAEDVAVAL NEQYQPRFAG DDLPSNPVAC ALAIADKMDT LAGIFGIGQH PKGDKDPFAL
RRAALGVLRI IVEKNLSLDL QTLTEEAVRL YGSKLTNAKV VDDVIEFMLG RFRAWYQDEG
HSVDTIQAVL ARRPTKPADF DARVKAVTYF RTLDAAAALA AANKRVSNIL AKSTDTLNDH
VHASILKEPA ELKLATHLVV LRDQLEPVFA AGQYKEALVE LAALRETVDE FFESVMVMAE
DDAVRVNRLT LLSKLRELFL QVADISLLQ