ID A0A0R2FLY3_9LACO Unreviewed; 693 AA.
AC A0A0R2FLY3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=IV38_GL000405 {ECO:0000313|EMBL:KRN29520.1}, IV40_GL000263
GN {ECO:0000313|EMBL:KRN33950.1};
OS Lactobacillus selangorensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=81857 {ECO:0000313|EMBL:KRN29520.1, ECO:0000313|Proteomes:UP000051751};
RN [1] {ECO:0000313|Proteomes:UP000051645, ECO:0000313|Proteomes:UP000051751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-66 {ECO:0000313|EMBL:KRN29520.1,
RC ECO:0000313|Proteomes:UP000051751}, and DSM 13344
RC {ECO:0000313|EMBL:KRN33950.1, ECO:0000313|Proteomes:UP000051645};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRN29520.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JQAT01000001; KRN29520.1; -; Genomic_DNA.
DR EMBL; JQAZ01000001; KRN33950.1; -; Genomic_DNA.
DR RefSeq; WP_057768559.1; NZ_JQAZ01000001.1.
DR AlphaFoldDB; A0A0R2FLY3; -.
DR STRING; 81857.IV38_GL000405; -.
DR PATRIC; fig|81857.3.peg.410; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000051645; Unassembled WGS sequence.
DR Proteomes; UP000051751; 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}; Reference proteome {ECO:0000313|Proteomes:UP000051645}.
SQ SEQUENCE 693 AA; 78934 MW; 3DB72CA230CAB8C2 CRC64;
MSKTFLLEIG LEEMPAHVVT PSVEQLENRV EDFLDKNHLA YESVRPYSTP RRLAVMVEGL
ADKQDDIEVD AKGPAKKIAV DADGNWTKAA KGFARGQKSD PDQIVFKDLK GTEYAYIHKL
IPGKPAAEVL QGLDKVVEAM TFPTRMHWHT YHFEYIRPIH WIVALLDDQV IDFQVLNIKT
GRQTQGHRFL GEPVALKQAS DYQQALADQF VIADAEDRKN MIRQQINQMA AEQNWQVVLD
ADLLEEVNNL VEYPTAFYGT FEKRFLDIPE AVLITSMKDN QRYFYVRDQN GKLLPYFISV
RNGDKAHLEN VVHGNEKVLT ARLEDAAFFY QEDQKHTIDD YVERLKKVSF HDKIGSMYAK
MLRVHAIAHF LGEKYQLSNQ EMKDLDRASM IYKFDLVTSM VGEFSELQGV MGEVYAKLAG
EDENVAVAIR EHYMPTSSEG ELPQTSVGSV LALADKIDSI GAFFSVDMIP NGSNDPYALR
RQAYGIVRIV EDHGWHLPIG KVENEVARVL TDAGVTDGLD VTKNQKEVLD FMLDRMRQWL
GNAAVRHDII DAVVESSSED PLTMFAAAKT LEAHKDDDDF KDTIEAVTRV LRLDAKADFD
ENTDLTVDPS LFENDSEKQL NEAVIDLSEK WFDQTIEEDY QSLRELRPLI DEYFDQTMIM
DKNEQVRDNR LKQLAQVAKL ANVLGDLNQL VVK
//
