SYGB_RICPU
ID SYGB_RICPU Reviewed; 664 AA.
AC C4K2V3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 63.
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=RPR_07440;
OS Rickettsia peacockii (strain Rustic).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=562019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rustic;
RX PubMed=20027221; DOI=10.1371/journal.pone.0008361;
RA Felsheim R.F., Kurtti T.J., Munderloh U.G.;
RT "Genome sequence of the endosymbiont Rickettsia peacockii and comparison
RT with virulent Rickettsia rickettsii: identification of virulence factors.";
RL PLoS ONE 4:E8361-E8361(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}.
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DR EMBL; CP001227; ACR47898.1; -; Genomic_DNA.
DR AlphaFoldDB; C4K2V3; -.
DR SMR; C4K2V3; -.
DR PRIDE; C4K2V3; -.
DR EnsemblBacteria; ACR47898; ACR47898; RPR_07440.
DR KEGG; rpk:RPR_07440; -.
DR HOGENOM; CLU_007220_2_1_5; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000005015; 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..664
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000204611"
SQ SEQUENCE 664 AA; 75802 MW; E1C43206F9659088 CRC64;
MSELLLELFS EEIPAFMQKN AEEGYLNIFT KIFEENEIFA KVQVFAGPRR ITLHATHLPK
ITLPKEEEIK GPSIEAPETA INGFCKAHNV SKLELPTKLI SNQLYYFFVK KTEEREIKEI
LPEIIIEAIN KYSWAKSMFW GDYKIKWIRP LRNILCIFNG EILPMQFGHL TANNITYGHR
LTDNKKLEVT DFEDYRNKLL ENHVILERAK REAIIKTGLL ELANSHELII KEDNRLVEEV
VGLSEFPIVL LGKIPQKFLE LPKEVLISSM RTHQKYFCLF DKTGNFTPYF LFVSNGRFTN
AELVIQGNEK VLSARLSDAL YFCKQDIAKT LESRLGQLEA VTFHAKLGNL REKIERITDI
CNYIAPNNKD LITAARLCKS DLVSEMVWEF PDLQGIMGYY YAKHEGLNAE IAAAIKDHYK
PQGLSDNVPS GNAALLALAD KLDSLVGLMI AGETPTGSGD PYALRRQALG IIRIILENKL
ELNFNDLINF SINLYKDSSD ENKNLIISFF EERAKFYFKN DYDIALINAV LDLNLIDTNF
KLDELKEFLI EDAGKQLLNA YKRASNIIGD QKITGLVDAS LFSTQPEKEL FEVIQKISPE
IIDSIADKDY KKALNLLSSL LTPITSFFDN ILVNDSDPKI AQNRLSLLQN ICELFDKVAK
FNRL