ID   SYGB_ACIBT              Reviewed;         689 AA.
AC   A3M9C2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
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=A1S_3119;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS   KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT   density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
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; CP000521; ABO13516.2; -; Genomic_DNA.
DR   RefSeq; WP_000033892.1; NZ_CP053098.1.
DR   AlphaFoldDB; A3M9C2; -.
DR   SMR; A3M9C2; -.
DR   KEGG; acb:A1S_3119; -.
DR   HOGENOM; CLU_007220_2_2_6; -.
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_1000101255"
SQ   SEQUENCE   689 AA;  75025 MW;  625F2E4993E02EEE 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 STQIIEGNEK 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