ID   SYGB_ACIBY              Reviewed;         689 AA.
AC   B0V7W2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=ABAYE0367;
OS   Acinetobacter baumannii (strain AYE).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509173;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AYE;
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; CU459141; CAM85343.1; -; Genomic_DNA.
DR   RefSeq; WP_000033906.1; NC_010410.1.
DR   AlphaFoldDB; B0V7W2; -.
DR   SMR; B0V7W2; -.
DR   EnsemblBacteria; CAM85343; CAM85343; ABAYE0367.
DR   KEGG; aby:ABAYE0367; -.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000002446; 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_1000101256"
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