ID A0A0R1P4D5_9LACO Unreviewed; 689 AA.
AC A0A0R1P4D5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=FD27_GL000783 {ECO:0000313|EMBL:KRL27036.1};
OS Limosilactobacillus frumenti DSM 13145.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1423746 {ECO:0000313|EMBL:KRL27036.1, ECO:0000313|Proteomes:UP000051445};
RN [1] {ECO:0000313|EMBL:KRL27036.1, ECO:0000313|Proteomes:UP000051445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13145 {ECO:0000313|EMBL:KRL27036.1,
RC ECO:0000313|Proteomes:UP000051445};
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|ARBA:ARBA00004496,
CC 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:KRL27036.1}.
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DR EMBL; AZER01000016; KRL27036.1; -; Genomic_DNA.
DR RefSeq; WP_057750488.1; NZ_AZER01000016.1.
DR AlphaFoldDB; A0A0R1P4D5; -.
DR STRING; 1423746.FD27_GL000783; -.
DR PATRIC; fig|1423746.3.peg.791; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000051445; Unassembled WGS sequence.
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 NCBIfam; TIGR00211; glyS; 1.
DR PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF05746; DALR_1; 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:UP000051445}.
FT DOMAIN 586..676
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 689 AA; 78098 MW; FC5DC5CB5D3C00E4 CRC64;
MANSYLLEVG VEEMPAHVVT PSIKQLHQRV ADYLKKERIS FNDIHEFATP RRLALLIDGL
SDKQPDVDQS VKGPAKKIAQ DSDGNWTKAA IGFTRGQGAT VDDIQFKNVK GEEYVFVEKH
IAGKNVAEVL QGLPDVITSM TFPTLMKWGY YNLQFIRPIR WLVSLLNDQV VPFKILDITA
GRTTRGHRFL GHKFDLKQAT DYEKALHDDF VIADQAKRKQ VIEDQIDQIV KANDWVIDKD
ADLLEEVNNL VEWPTTFSGS FDPKYLVLPD EVLITSMKDN QRFFYLRDHD GKLLPHFIAV
RNGNTDYLDN VIKGNERVLV PRLEDAKFFY EEDQKISIDE YVDRLKRVSF HDKISSMYDK
MQRVAAIARV LGKHLHLSDQ EMADLDRAAH IYKFDLTTQM VGEFAELQGI MGDIYAKLFG
EDDAVATAIR EHYMPISADG DLPASKVGAV LAVADKLDSI MSFFAVDMIP SGSNDPYALR
RQAFGIVRII ADRDWHLPLL DIQPEIVQAF NDDQLNVSID ITKNADQVRA FFMDRIHQLL
SENKTGHDVI DAVTKAQTAD IEDVLESAET IKQHHSDDDF KENIEALTRV LRIAKKGQGA
AQVDASLFQN PSEKELADAV NKLNDHADHN SPADNFAALN ALSPIINRYF DENMIMDKDE
KIKNNRLALL NQIAHQVYQI GDLDQLVIK
//
