ID   SYGB_ACIF5              Reviewed;         694 AA.
AC   B5EMS4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-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=Lferr_2210;
OS   Acidithiobacillus ferrooxidans (strain ATCC 53993 / BNL-5-31)
OS   (Leptospirillum ferrooxidans (ATCC 53993)).
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=380394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53993 / BNL-5-31;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Borole A.P.;
RT   "Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993.";
RL   Submitted (AUG-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; CP001132; ACH84413.1; -; Genomic_DNA.
DR   RefSeq; WP_012537273.1; NC_011206.1.
DR   AlphaFoldDB; B5EMS4; -.
DR   SMR; B5EMS4; -.
DR   GeneID; 66433541; -.
DR   KEGG; afe:Lferr_2210; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OMA; LPIPKRM; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   PANTHER; PTHR30075; PTHR30075; 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..694
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101257"
SQ   SEQUENCE   694 AA;  76429 MW;  6657A849EB47712D CRC64;
     MSAPEDLLLE LGCEELPARE QMPLQDAATG IIGQLLDAAG LQFGSIHGYV TPRRLALWIK
     DVSRQSLPQE TLRRGPLVAR ARDAQGKPTA AAEGFARSCG VSLDDLLTLE TEKGPVLAWR
     EVGTAQDSHA LLPEIASRLV TSLPLRKRMR WGAGSDSFLR PVRWLLLRQG GQVLDWKMFG
     LDAGGESFGH RVHHPQAVRI STPAGYAGSL LQAKVMVDFA ERRAHISGKM AALADEMAVT
     PILPEALLDE ITGLNEWPVV LAGSFAADYL RVPEEALITV MMQHQRYVPL RGRNERLVPH
     YLFAANLHSR DTQVVIDGNN RVLRARLADA AFFWDQDRQI SLQTRRAALA GVLFQDGLGS
     ILDKTVRLQE LAAALSPQFA VDAGDMNRAA ALCKSDLLSG LVGEFPELQG IMGGHYARHD
     GENNRVATAI AQHYLPSGRD DEIPADAHGQ CLAIADKLDT LCGFFAIGKV PTGDRDPFAL
     RRAALGVLRI VLDAGVPLNL DEAVTRTLAA YGGAFARNRT EIRSAILDFF QDRMRVYFRE
     EGFRADQIAA VLSRQPHEPL DARQRLEALA LFQAEHAAAD ALAALIKRIN NLLRKEVISG
     DWPIDPQYFM DPVENTLWDY WQALEQPLHA QLAERRYTAA LGLLAGLRPA VDQFFDGVMV
     LAEDPVLRQN RLALLARLQE AFLRIADFSQ LQGA