SYGB_ECOLI
ID SYGB_ECOLI Reviewed; 689 AA.
AC P00961; Q2M7M1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Glycine--tRNA ligase beta subunit;
DE EC=6.1.1.14;
DE AltName: Full=Glycyl-tRNA synthetase beta subunit;
DE Short=GlyRS;
GN Name=glyS; Synonyms=glyS(B); OrderedLocusNames=b3559, JW3530;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6309809; DOI=10.1016/s0021-9258(17)44504-2;
RA Webster T.A., Gibson B.W., Keng T., Biemann K., Schimmel P.;
RT "Primary structures of both subunits of Escherichia coli glycyl-tRNA
RT synthetase.";
RL J. Biol. Chem. 258:10637-10641(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RX PubMed=6290471; DOI=10.1016/s0021-9258(18)33539-7;
RA Keng T., Webster T.A., Sauer R.T., Schimmel P.;
RT "Gene for Escherichia coli glycyl-tRNA synthetase has tandem subunit coding
RT regions in the same reading frame.";
RL J. Biol. Chem. 257:12503-12508(1982).
RN [6]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
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;
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC -!- INTERACTION:
CC P00961; P00960: glyQ; NbExp=3; IntAct=EBI-551400, EBI-551191;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; J01622; AAA23915.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18536.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76583.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77735.1; -; Genomic_DNA.
DR EMBL; J01623; AAA23917.1; -; Genomic_DNA.
DR PIR; S47780; SYECGB.
DR RefSeq; NP_418016.1; NC_000913.3.
DR RefSeq; WP_001291772.1; NZ_SSZK01000041.1.
DR PDB; 7EIV; X-ray; 2.68 A; C/D=1-575.
DR PDBsum; 7EIV; -.
DR AlphaFoldDB; P00961; -.
DR SMR; P00961; -.
DR BioGRID; 4259716; 23.
DR BioGRID; 852388; 1.
DR ComplexPortal; CPX-5201; Glycyl-tRNA synthetase complex.
DR DIP; DIP-6880N; -.
DR IntAct; P00961; 11.
DR STRING; 511145.b3559; -.
DR jPOST; P00961; -.
DR PaxDb; P00961; -.
DR PRIDE; P00961; -.
DR EnsemblBacteria; AAC76583; AAC76583; b3559.
DR EnsemblBacteria; BAE77735; BAE77735; BAE77735.
DR GeneID; 948080; -.
DR KEGG; ecj:JW3530; -.
DR KEGG; eco:b3559; -.
DR PATRIC; fig|1411691.4.peg.3154; -.
DR EchoBASE; EB0405; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
DR InParanoid; P00961; -.
DR OMA; LPIPKRM; -.
DR PhylomeDB; P00961; -.
DR BioCyc; EcoCyc:GLYS-MON; -.
DR BioCyc; MetaCyc:GLYS-MON; -.
DR PRO; PR:P00961; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009345; C:glycine-tRNA ligase complex; IPI:ComplexPortal.
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; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Ligase; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..689
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_0000072899"
FT CONFLICT 2
FT /note="S -> Q (in Ref. 1; AAA23915)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="A -> P (in Ref. 1; AAA23915)"
FT /evidence="ECO:0000305"
FT CONFLICT 154..156
FT /note="DVH -> AAA (in Ref. 1; AAA23915)"
FT /evidence="ECO:0000305"
FT CONFLICT 211..212
FT /note="ER -> DG (in Ref. 1; AAA23915)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="L -> D (in Ref. 1; AAA23915)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="L -> V (in Ref. 1; AAA23915)"
FT /evidence="ECO:0000305"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 20..36
FT /evidence="ECO:0007829|PDB:7EIV"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:7EIV"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:7EIV"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:7EIV"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:7EIV"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:7EIV"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:7EIV"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 127..140
FT /evidence="ECO:0007829|PDB:7EIV"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:7EIV"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:7EIV"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:7EIV"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:7EIV"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 219..237
FT /evidence="ECO:0007829|PDB:7EIV"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 245..252
FT /evidence="ECO:0007829|PDB:7EIV"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 267..271
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:7EIV"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:7EIV"
FT STRAND 297..307
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 313..337
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 361..378
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 383..391
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 400..404
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 409..420
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 424..432
FT /evidence="ECO:0007829|PDB:7EIV"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 447..467
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 480..493
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 500..509
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 520..538
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 543..551
FT /evidence="ECO:0007829|PDB:7EIV"
FT HELIX 557..569
FT /evidence="ECO:0007829|PDB:7EIV"
SQ SEQUENCE 689 AA; 76813 MW; F123D53B25BAE23A CRC64;
MSEKTFLVEI GTEELPPKAL RSLAESFAAN FTAELDNAGL AHGTVQWFAA PRRLALKVAN
LAEAQPDREI EKRGPAIAQA FDAEGKPSKA AEGWARGCGI TVDQAERLTT DKGEWLLYRA
HVKGESTEAL LPNMVATSLA KLPIPKLMRW GASDVHFVRP VHTVTLLLGD KVIPATILGI
QSDRVIRGHR FMGEPEFTID NADQYPEILR ERGKVIADYE ERKAKIKADA EEAARKIGGN
ADLSESLLEE VASLVEWPVV LTAKFEEKFL AVPAEALVYT MKGDQKYFPV YANDGKLLPN
FIFVANIESK DPQQIISGNE KVVRPRLADA EFFFNTDRKK RLEDNLPRLQ TVLFQQQLGT
LRDKTDRIQA LAGWIAEQIG ADVNHATRAG LLSKCDLMTN MVFEFTDTQG VMGMHYARHD
GEAEDVAVAL NEQYQPRFAG DDLPSNPVAC ALAIADKMDT LAGIFGIGQH PKGDKDPFAL
RRAALGVLRI IVEKNLNLDL QTLTEEAVRL YGDKLTNANV VDDVIDFMLG RFRAWYQDEG
YTVDTIQAVL ARRPTRPADF DARMKAVSHF RTLDAAAALA AANKRVSNIL AKSDEVLSDR
VNASTLKEPE EIKLAMQVVV LRDKLEPYFT EGRYQDALVE LAELREPVDA FFDKVMVMVD
DKELRINRLT MLEKLRELFL RVADISLLQ
