ID   SYGB_ACIC5              Reviewed;         706 AA.
AC   C1F1J0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, 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=ACP_0591;
OS   Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM
OS   7670 / NBRC 15755 / NCIMB 13165 / 161).
OC   Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC   Acidobacterium.
OX   NCBI_TaxID=240015;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 / NCIMB
RC   13165 / 161;
RX   PubMed=19201974; DOI=10.1128/aem.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP001472; ACO32145.1; -; Genomic_DNA.
DR   RefSeq; WP_015895776.1; NC_012483.1.
DR   AlphaFoldDB; C1F1J0; -.
DR   SMR; C1F1J0; -.
DR   STRING; 240015.ACP_0591; -.
DR   PRIDE; C1F1J0; -.
DR   EnsemblBacteria; ACO32145; ACO32145; ACP_0591.
DR   KEGG; aca:ACP_0591; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_0; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000002207; 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   SMART; SM00836; DALR_1; 1.
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; Reference proteome.
FT   CHAIN           1..706
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000197163"
SQ   SEQUENCE   706 AA;  77535 MW;  8F332E62EF1F1206 CRC64;
     MAEFLFEIGL EEIPARMIAA AESELARRVA ELLQREDLLA EGHAVTRYST PRRLAVLVTG
     VKAAQADREE QLTGPAWSIA FKDGQPTPAA QAFAKKAGVE VAALQKVTTP KGEYVGASSV
     RKGRAANEIL LEALPKEIAA IYWPKNMYWR AGKPERFVRP VQWMVALLGE QVIPVEFAGV
     TAANVTYGHR ILHGDAPVAI PAPMEYAATL EAAKVQADVE ARRHRIRKAL DHVTRTVPGA
     RWREDEALVD AVTHLTEWPS VLLGSFETEF LALPEEVLVT VMRDHQKYFA VEDAAGKLAP
     HFLTALNTEP SDQAAAIIRH GNERVLRARF NDARFFWTVD QKISLANRLE MLQSVTFHKE
     LGSYHQKTHT TREIAVKLSA QVRHAGTSVD EAALLRAVEL AKTDLTTELV KEFTELQGIV
     GGLYARAQGE GEAVAQAIYW QYSPASMDDP IPPTLEGQLL GLADRIGTIV EMFAIGLEPT
     GSKDPFALRR AANAVVKILA EGKLPVTLDR LLNAAEESSK VENAAASREK VMAFLKERLE
     FYMREVLGYR YDVVNAVLAA GAHDVVDTIA RAEALSAVRG SEDFAAIAAA FKRSKNILRQ
     AAEKAGVAED SLSADVDAAL LPEPAEKQLH EAAAKLAPVV EELRAKNDYR AALEQIATLR
     PQVDLFFDKV MVMVEDDLLR HNRLALIQYV LRSFSSIADF SEIVAS