SYGA_CAMJE
ID SYGA_CAMJE Reviewed; 287 AA.
AC Q9PPK3; Q0PAH5;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00254};
DE AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00254};
GN Name=glyQ {ECO:0000255|HAMAP-Rule:MF_00254}; OrderedLocusNames=Cj0704;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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_00254};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00254}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00254}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00254}.
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DR EMBL; AL111168; CAL34841.1; -; Genomic_DNA.
DR PIR; C81341; C81341.
DR RefSeq; WP_002852069.1; NC_002163.1.
DR RefSeq; YP_002344122.1; NC_002163.1.
DR PDB; 3RGL; X-ray; 2.45 A; A/B=1-287.
DR PDB; 3UFG; X-ray; 2.55 A; A/B=1-287.
DR PDBsum; 3RGL; -.
DR PDBsum; 3UFG; -.
DR AlphaFoldDB; Q9PPK3; -.
DR SMR; Q9PPK3; -.
DR IntAct; Q9PPK3; 4.
DR STRING; 192222.Cj0704; -.
DR PaxDb; Q9PPK3; -.
DR PRIDE; Q9PPK3; -.
DR EnsemblBacteria; CAL34841; CAL34841; Cj0704.
DR GeneID; 905023; -.
DR KEGG; cje:Cj0704; -.
DR PATRIC; fig|192222.6.peg.696; -.
DR eggNOG; COG0752; Bacteria.
DR HOGENOM; CLU_057066_1_0_7; -.
DR OMA; SYYQFQV; -.
DR BRENDA; 6.1.1.14; 13746.
DR Proteomes; UP000000799; 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; IEA:UniProtKB-UniRule.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00733; GlyRS_alpha_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR Pfam; PF02091; tRNA-synt_2e; 1.
DR PRINTS; PR01044; TRNASYNTHGA.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00388; glyQ; 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; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..287
FT /note="Glycine--tRNA ligase alpha subunit"
FT /id="PRO_0000072833"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:3RGL"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:3RGL"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:3RGL"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:3RGL"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:3RGL"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:3RGL"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:3RGL"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3RGL"
FT STRAND 72..83
FT /evidence="ECO:0007829|PDB:3RGL"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:3RGL"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:3RGL"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:3RGL"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:3RGL"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3RGL"
FT STRAND 122..145
FT /evidence="ECO:0007829|PDB:3RGL"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:3RGL"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:3RGL"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:3RGL"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:3RGL"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:3RGL"
FT HELIX 189..206
FT /evidence="ECO:0007829|PDB:3RGL"
FT HELIX 210..229
FT /evidence="ECO:0007829|PDB:3RGL"
FT HELIX 233..253
FT /evidence="ECO:0007829|PDB:3RGL"
FT HELIX 258..281
FT /evidence="ECO:0007829|PDB:3RGL"
SQ SEQUENCE 287 AA; 33058 MW; 3ED6803DD5B72908 CRC64;
MTFSQMILNL QNYWQEQGCA IMQPYDMPAG AGTFHPATFL RSLGKKPWAA AYVAPSRRPT
DGRYGENPNR LGAYYQFQVL IKPSPDNIQE LYLKSLENLG FDLKSHDIRF VEDNWESPSL
GAWGLGWEVW LDGMEVTQFT YFQQVGGIAV DLVSAEITYG LERIAMYLQN VDNVYDIVWS
EFNGEKIKYA DVHKQSEYEF SKYNFEVSDV KILNEQFENS YKECKNILEQ GLALPAYDYC
MLAAHTFNLL DARGAISVAQ RQDYMLKIRE LSKNCAEIYK KNLNEAE
