SYGB_ACIB3
ID SYGB_ACIB3 Reviewed; 689 AA.
AC B7GVW2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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};
GN OrderedLocusNames=ABBFA_000392;
OS Acinetobacter baumannii (strain AB307-0294).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=557600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB307-0294;
RX PubMed=18931120; DOI=10.1128/jb.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT baumannii.";
RL J. Bacteriol. 190:8053-8064(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; CP001172; ACJ58770.1; -; Genomic_DNA.
DR RefSeq; WP_000033906.1; NZ_CP001172.1.
DR AlphaFoldDB; B7GVW2; -.
DR SMR; B7GVW2; -.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000006924; 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_1000197165"
SQ SEQUENCE 689 AA; 75052 MW; B68DFFC3704FB06F CRC64;
MSKHTVLFEL GCEELPPKSL KTLRDALQAE TVKGLNEAGL NFASVEAYAA PRRLALKIVD
VDAAQADTQK RFDGPAVQAA YDAEGKPTKA LEGFMRGQGI TVEQLSTFQA GKVEKVCYLK
DVKGQSLDTL LPQILQTALD NLPIAKRMRS AASRTEFVRP VKWVVLLKDD QVIEATIQDH
KAGNVTYGHR FHAPEAVTLA HANDYLAALE KAYVVANFEK RQATIQEQVK KLADEVNATA
IVPADLLDEV TSLVEWPVAL RATFEERYLA VPQEALITTM QDNQKYFCLI NAEGKLQPYF
ITVSNIESKD PTQIIEGNEK VVRPRLSDAE FFFLQDQKQP LASRKEKLAN MVFQAQLGTL
WDKSTRIAKL AVALSSITGA NPADAEKAAL LAKCDLTSEL VGEFPELQGI AGTYYARIEG
ENTEVSEALG EQYLPKFAGD VLPKTKTGTT IALSDRLDTL VGIFGIGQAP TGSKDPFALR
RSAIGILRLI IENELDVTIE ELVNLALQGY GDIVKDHDKT RADAVAFLEG RYRAKYEDQG
VAVDVLQAVQ ALAPKSPLDF DKRVNAVNHF RTLPEAAALA AANKRVANIL AKEATPEGSV
VEANLVEDAE KALFAELQAV TPVVEPLLAA KDYTAALSKL AALRAPIDAF FDGVMVMADD
AGLKANRLRL LAQLRNLFTA VADVSVLQG