SYGB_ACIBS
ID SYGB_ACIBS Reviewed; 689 AA.
AC B0VQA1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=ABSDF0371;
OS Acinetobacter baumannii (strain SDF).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509170;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDF;
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(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; CU468230; CAO99765.1; -; Genomic_DNA.
DR AlphaFoldDB; B0VQA1; -.
DR SMR; B0VQA1; -.
DR EnsemblBacteria; CAO99765; CAO99765; ABSDF0371.
DR KEGG; abm:ABSDF0371; -.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000001741; 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..689
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101254"
SQ SEQUENCE 689 AA; 75142 MW; 0B312ABA8B49A189 CRC64;
MSKHTVLFEL GCEELPPKSL KTLRDALQVE TVKGLNEAGL NFASVEAYAA PRRLALKIVD
VDAAQADTQK RFDGPAVQAA YDAEGKPTKA LEGFMRGQGI TVEQLSTFQA GKVEKVCYLK
DVKGQSLDAL LPQILQTALD NLPIAKRMRS AASRTEFVRP VKWVVLLKDD QVIEATIQDH
KAGNVTYGHR FHAPEAVTLA HANDYLAALE KAYVVANFEK RQATIQEQVK KLADEVNATA
IVPADLLDEV TSLVEWPVAL RATFEERYLA VPQEALITTM QDNQKYFCLI NAEGKLQPYF
ITVSNIESKD PTQIIEGNEK VVRPRLSDAE FFFLQDQKQP LASRKEKLTN MVFQAQLGTL
WDKSTRIAKL AVALSSITGA NPADAEKAAL LAKCDLTSEL VGEFPELQGI AGTYYARIEG
ENTEVSEALG EQYLPKFAGD VLPKTKTGTT IALADRLDTL VGIFGIGQAP TGSKDPFALR
RSAIGILRLI IENELDVTIE ELVNLALQSY GDIVKDHDKT RADAVAFLEG RYRAKYEDQG
VAVDVLQAVQ ALAPKSPLDF DKRVNAVNHF RTLPEAAALA AANKRVANIL AKEAASEGSV
VEANLVEDAE KALFAELQAV TPVVEPLLTA KDYTAALSKL AALRAPIDAF FDGVMVMADD
ADLKANRLRL LAQLRNLFTA VADVSVLQG