ID A0A0R2LTT8_9LACO Unreviewed; 692 AA.
AC A0A0R2LTT8;
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=IV66_GL000143 {ECO:0000313|EMBL:KRO02717.1};
OS Ligilactobacillus pobuzihii.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=449659 {ECO:0000313|EMBL:KRO02717.1, ECO:0000313|Proteomes:UP000051886};
RN [1] {ECO:0000313|EMBL:KRO02717.1, ECO:0000313|Proteomes:UP000051886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103219 {ECO:0000313|EMBL:KRO02717.1,
RC ECO:0000313|Proteomes:UP000051886};
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:KRO02717.1}.
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DR EMBL; JQCN01000001; KRO02717.1; -; Genomic_DNA.
DR RefSeq; WP_017868121.1; NZ_JQCN01000001.1.
DR AlphaFoldDB; A0A0R2LTT8; -.
DR STRING; 449659.IV66_GL000143; -.
DR PATRIC; fig|449659.4.peg.141; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000051886; 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:UP000051886}.
SQ SEQUENCE 692 AA; 78169 MW; 3C3B5301A90EA15E CRC64;
MKHTFLLEIG LEEIPAHVVT PSVKQLASRM EDFLNESRLS FDEIQTFSTP RRLAVKVLGL
ADKQPDIKEE AKGPAKKIAV DDQGNWSKAA QGFSRGQGVD PDQIYFKEFK GTEYAYVEKS
ILGKSATEVL KDVDQVIIAM RFPTMMRWST NEFEFVRPIR WIACLLDDEV IPVQILKIKA
DRISAGHRFL GQDVSLANAN GYPASLLDQM VVADACKRKK MIRSQIHEIA HKNEWQIVID
EDLLEEVNNL VEYPTVFAGS FDEQYLSLPD EVLITSMKDH QRFFYVLDSN GKMLPYFVSV
RNGNDQYLKN VVVGNEKVLT ARLEDARFFY EEDQKTPISA SVERLKNVMF HDKIGTIYAK
MQRVTEISTF LGKKVGLSAD ELQDLKRAAQ IYKFDIVTEM VGEFAELQGV MGEIYARLFG
ENENTAAAIK ESYMPLGSES ELPQTNVGAV LSIADKIDSI QSFFAASMLP SGSNDPYALR
RQALGIVRIA LAKKWKLSVI DLANAIDSAY QTEQNLYENT QPDQNQVEWQ EFIMGRVHQL
LVDQGYAYDI VNTVVATKDN TFQQIFAAAN VLTKHQSDLE FKQNIEALTR TVRLARKGQA
DVQPEVKVDL FENNSEKALH TAVVAVSKGY GDKDLEEKYV ALTSLRQPIS NYFDETMVMV
DDESVKNNRL TQLDAIARLT YSFGALDNLN VK
//
