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Database: UniProt
Entry: A0A1F5AX17_9BACT
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ID   A0A1F5AX17_9BACT        Unreviewed;       700 AA.
AC   A0A1F5AX17;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE            EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00255};
DE   AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE            Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00255};
GN   Name=glyS {ECO:0000256|HAMAP-Rule:MF_00255};
GN   ORFNames=A2W03_03215 {ECO:0000313|EMBL:OGD22936.1};
OS   Candidatus Aminicenantes bacterium RBG_16_63_16.
OC   Bacteria; Candidatus Aminicenantes.
OX   NCBI_TaxID=1797273 {ECO:0000313|EMBL:OGD22936.1, ECO:0000313|Proteomes:UP000178699};
RN   [1] {ECO:0000313|EMBL:OGD22936.1, ECO:0000313|Proteomes:UP000178699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:0000256|ARBA:ARBA00000201,
CC         ECO:0000256|HAMAP-Rule:MF_00255};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00255}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00255}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGD22936.1}.
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DR   EMBL; MEYB01000005; OGD22936.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5AX17; -.
DR   Proteomes; UP000178699; Unassembled WGS sequence.
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   NCBIfam; TIGR00211; glyS; 1.
DR   PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00255};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00255}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00255};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00255};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00255}.
SQ   SEQUENCE   700 AA;  77010 MW;  B4D547B30EDB9BCF CRC64;
     MKEFLLEINT EEMPSSHVKA GLAQLKEKIG AGLAARRVAV GEIEAMGSSR RLVVRGKFAP
     RQEDMEETVI GPPKAAAFGP DGAPAAAARG FARSQGIDVG ALRVVETPRG QYVGVTKTVA
     GVPTDEILAG MLPGIITSLS FPKMMKWGES SLKFSRPIKN ILCVFGRRPL AFSVDGLEAA
     DRTSGHRLHA SRKFRIRRTA KETLFEAYVR QLGERFVILR AEERKRIILE QAGERLAGSG
     AFLYPDDELL DKLSHDVEWP HVIQGGFPAE YLDLPIEVLS MAMREGQKLF SVVKDGRQLP
     LFIGITDTPG DPKSLICRGN ERVLRARLED ARFFWQHDRK TPLAGRRAGL ADVVFQQRLG
     SYADKTERLE ALVGRLCEEL GQDALKPDAV AAAGLSKVDL ITDMVREFPA LQGKMGGLYA
     RAEGYPETVW RAIYEHYLPL SFEGPLPETL AGALLSLADK LDSIVGVMGL GIQVTGSSDP
     FGLRRNAHGI VRIILDRGLT LSFRGLIAET ASRFSADKKQ DLPLEAAIET CLGFFEQRLR
     HIFESQGYRY DLVNAALAGG LDNLHFLRLK LEALDALKKS DDFTALILMA KRVNNILRGV
     PPRTVDPRLF IEPEEKQLFA SLTRTVETSG PMLAAGDFLG AQSEILSLRS PLGLFFDKVL
     VMAEEPGLRQ NRLALLQAIR ALLSRLADYS LIVVEGERPA
//
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