SYGB_SHEPW
ID SYGB_SHEPW Reviewed; 689 AA.
AC B8CH76;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
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=swp_0020;
OS Shewanella piezotolerans (strain WP3 / JCM 13877).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=225849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP3 / JCM 13877;
RX PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA Bartlett D.H., Yu J., Hu S., Xiao X.;
RT "Environmental adaptation: genomic analysis of the piezotolerant and
RT psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT WP3.";
RL PLoS ONE 3:E1937-E1937(2008).
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; CP000472; ACJ26868.1; -; Genomic_DNA.
DR RefSeq; WP_020910252.1; NC_011566.1.
DR AlphaFoldDB; B8CH76; -.
DR SMR; B8CH76; -.
DR STRING; 225849.swp_0020; -.
DR EnsemblBacteria; ACJ26868; ACJ26868; swp_0020.
DR KEGG; swp:swp_0020; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000000753; 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 SMART; SM00836; DALR_1; 1.
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_1000197216"
SQ SEQUENCE 689 AA; 75447 MW; AFC79C7CC7519353 CRC64;
MNFENLLIEV GTEELPPKSL RKLAESFLNN FTDELKKAEL TFESAVWHAA PRRLAINVNQ
LALAQADKVV EKRGPAVAQA FDADGNPTKA AMGWARGNGI TVEQADRLKT DKGEWLLHQA
KVVGVETKSL IAAMAQRSLD KLPIPKPMRW GSNTTQFIRP VHTVTMLLGS EVVEGELLGI
KSDRIIRGHR FMGKPSIELD HADNYLSVLK EQGKVDANYE ARKAQIKADA EAAAAKLGGV
ADLEDDLLEE VTSLVEWPVV LTASFEEKFL DVPAEALVYT MKGDQKYFPV FDDAGQLLPN
FIFVTNIESK DPQQIISGNE KVVRPRLADA EFFFETDKKN SLESRLSSLE TVVFQKQLGT
IKQRVERISA MAAYIATSIG ANSEEAARAG LLSKSDLMTN MVMEFTDLQG TMGMHYARLN
GETEAVAVAL SEQYKPKFSG DTVPTAPVSI CVALAEKLDT LVGIFGIGQA PKGAADPFAL
RRAAIGVLRI CLENNLPLDL VDLIAKAQEL HGENLTNDKA PEQVLEFFMG RFRAWYQDQG
ISVDVILAVL ARRPTAPADF ESRIKAVAHF RTLEQALALA AANKRVSNIL AKVEGELPAT
IDEALLVEAA EKALAAKLAE LQPQLAPLFA AANYQEALAL LASLRESVDT FFEDVMVMAD
DEALKNNRLA LLSSLRDQFL HAADISLLQ