ID   SYGB_SYNP2              Reviewed;         713 AA.
AC   B1XK79;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=SYNPCC7002_A2456;
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA   Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000951; ACB00434.1; -; Genomic_DNA.
DR   RefSeq; WP_012308052.1; NC_010475.1.
DR   AlphaFoldDB; B1XK79; -.
DR   SMR; B1XK79; -.
DR   STRING; 32049.SYNPCC7002_A2456; -.
DR   EnsemblBacteria; ACB00434; ACB00434; SYNPCC7002_A2456.
DR   KEGG; syp:SYNPCC7002_A2456; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_3; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000001688; 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; Reference proteome.
FT   CHAIN           1..713
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101363"
SQ   SEQUENCE   713 AA;  78310 MW;  45DB1F51428DF4F1 CRC64;
     MATYLIEVGT EELPADFVAA AIAQLKDRVS HSLTEYFLTP DGIEVYGTPR RLAVLIQGLP
     DQQADREEEI KGPPAAAAFK EGQPTKAAEG FARKQGVELS ALEVRPTEKG DFVFVQKKTL
     GRPTPEILQE LVLGWFTALE GRRFMRWADG DLRFPRPIRW LVSLWNDAVL PLELVNGSGK
     LEAGRISRGH RILHQGDVTL NNAADYVVTL QQAFVEVNPQ VREEKIVAGV KAAAAEIGGE
     AEMPADLLAE VVNLVEYPTA VVGDIEAEFL ELPTEVITTV MVTHQRYFAV RDRQDKTKLL
     PKFITISNGD PKKSEIIAAG NGRVIRARLA DGQFFYRADC DEHLETYLPQ LEAVTFQEEL
     GTMRDKVDRI MEISQQIAEQ LGLSEADKEI IASTAMLCKA DLVTQMVYEF PELQGIMGQK
     YALVSGEAPA VAEGIFEHYL PRNADDILPQ TLAGQVVGMG DRLDTLVSIF GLGMIPSGSS
     DPFALRRAAN AIITVAWDAG LEIDLGELLA QGAKDFVTAH PDKTSPLEAL QSFFIQRIQT
     LLQDEKGIDY DLVNAVLGDD AEYTERALTD LLDVGDRAAF LQSIRDDGQL AKIYATVNRS
     AKLAAKGNLS TDSLDPTGVI NPEKFAQNSE RDLYAGLVEL VPTTEVARTE RDYQKLIDGL
     AALAPTVERF FDGEDSVLVM AEDPAVRENR LNLLGLLRNH ARVLADFGAI VKQ