ID A0A0R1UHZ7_9LACO Unreviewed; 687 AA.
AC A0A0R1UHZ7;
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=FC21_GL000252 {ECO:0000313|EMBL:KRL92532.1};
OS Limosilactobacillus equigenerosi DSM 18793 = JCM 14505.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1423742 {ECO:0000313|EMBL:KRL92532.1, ECO:0000313|Proteomes:UP000051084};
RN [1] {ECO:0000313|EMBL:KRL92532.1, ECO:0000313|Proteomes:UP000051084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18793 {ECO:0000313|EMBL:KRL92532.1,
RC ECO:0000313|Proteomes:UP000051084};
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:KRL92532.1}.
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DR EMBL; AZGC01000054; KRL92532.1; -; Genomic_DNA.
DR RefSeq; WP_056995800.1; NZ_AZGC01000054.1.
DR AlphaFoldDB; A0A0R1UHZ7; -.
DR STRING; 417373.GCA_001570685_00879; -.
DR PATRIC; fig|1423742.4.peg.266; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000051084; 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:UP000051084}.
SQ SEQUENCE 687 AA; 77513 MW; 4B81C7536A50436E CRC64;
MSHTYLLEVG LEEMPAHVVT PSMRQLQTRV EKYLTEQRIE FDQITAYSTP RRLALEITGL
SDKQPDIDES VKGPAKKIAL DDEGNWSKAA IGFTKGQGVS VDDIEFKEIK GTEYVFVNKH
VAGKSVAEVL SGLNDVITSM TFPTLMKWAE YKLDFIRPIH WLVSLLDDEI VPFKILDVEA
DRHTKGHRFL GHDLTIKTAT DYVQTLKDDF VIVDPAERKA LIKDQIEAIV AEHNWTLDWD
EELLEEVNNL VEWPTAFAGK FDEKYLVLPE EVLITSMKDN QRFFCVRDQA GKLQPAFIAV
RNGNTDYLDN VIAGNERVLV PRLEDAKFFY EEDQKVTVDE YAQRLTRVSF HDQISSMADK
MKRTRVIAEL LAKELNFTDQ EVADLQRAAD IYKFDLTTQM VGEFSELQGV MGEIYANLMG
ENKVVATAIR EHYMPISAEG ALPATKVGAL LAVADKLDSI FSFFAVDLIP SGSNDPYALR
RQAYGIVRIL NDQQWHLPIF SVQAQLPALF AAAGLTPKYE VAKNADQVQS FFMDRMKQFF
SLAKISHDVV DAVTAVPATD LLSVMSAAKV LAAHHQDAGL KDQMEALTRV IRLAKKQPID
NPTVDPTLFQ NEAEQALFDQ VSHFDQTAAL DAQFAALVNF KDVINDYFEA NMIMDPDEQI
KHNRLSQMNQ LANLTHVFGD LDQLIVK
//
