ID   SYGB_ACIBC              Reviewed;         689 AA.
AC   B2HZR3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-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}; OrderedLocusNames=ACICU_03321;
OS   Acinetobacter baumannii (strain ACICU).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=405416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACICU;
RX   PubMed=18411315; DOI=10.1128/aac.01643-07;
RA   Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J.,
RA   Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.;
RT   "Whole-genome pyrosequencing of an epidemic multidrug-resistant
RT   Acinetobacter baumannii strain belonging to the European clone II group.";
RL   Antimicrob. Agents Chemother. 52:2616-2625(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; CP000863; ACC58631.1; -; Genomic_DNA.
DR   RefSeq; WP_000033889.1; NZ_CP031380.1.
DR   AlphaFoldDB; B2HZR3; -.
DR   SMR; B2HZR3; -.
DR   KEGG; abc:ACICU_03321; -.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000008839; 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_1000101253"
SQ   SEQUENCE   689 AA;  75035 MW;  63FDBE3B02302E21 CRC64;
     MSKHTVLFEL GCEELPPKSL KTLRDALQAE TVKGLNEAGL DFASVEAYAA PRRLALKIVD
     VDAAQADTQK RFDGPAVQAA YDAEGKPTKA LEGFMRGQGI TVDQLSTFQA GKVEKVCYLK
     DVKGQSLDAL 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 IALADRLDTL VGIFGIGQAP TGSKDPFALR
     RSAIGILRLI IENELDVTIE ELVNLALQGY GDIVKDHDKT RADAVAFLEG RYRAKYEDQG
     VAVDVLQAVQ ALAPKSPLDF DKRVNAVNHF RTLPEAAALA AANKRVANIL AKEAAPEGSV
     IEANLVEDAE KALFAELQAV TPVVEPLLAA KDYTAALSKL AALRAPIDAF FDGVMVMADD
     ADLKANRLRL LAQLRNLFTA VADVSVLQG