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Database: UniProt
Entry: V7HX07_9LACO
LinkDB: V7HX07_9LACO
Original site: V7HX07_9LACO 
ID   V7HX07_9LACO            Unreviewed;       693 AA.
AC   V7HX07;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
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=LEQ_1867c {ECO:0000313|EMBL:ETA74407.1};
OS   Ligilactobacillus equi DPC 6820.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1392007 {ECO:0000313|EMBL:ETA74407.1, ECO:0000313|Proteomes:UP000018559};
RN   [1] {ECO:0000313|EMBL:ETA74407.1, ECO:0000313|Proteomes:UP000018559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPC 6820 {ECO:0000313|EMBL:ETA74407.1,
RC   ECO:0000313|Proteomes:UP000018559};
RX   PubMed=24435863;
RA   O'Donnell M.M., Harris H.M., O'Toole P.W., Ross R.P.;
RT   "The Genome of the Predominant Equine Lactobacillus Species, Lactobacillus
RT   equi, Is Reflective of Its Lifestyle Adaptations to an Herbivorous Host.";
RL   Genome Announc. 2:e01155-e01113(2014).
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:ETA74407.1}.
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DR   EMBL; AWWH01000074; ETA74407.1; -; Genomic_DNA.
DR   RefSeq; WP_023859382.1; NZ_AWWH01000074.1.
DR   AlphaFoldDB; V7HX07; -.
DR   PATRIC; fig|1392007.3.peg.777; -.
DR   Proteomes; UP000018559; 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:UP000018559}.
FT   DOMAIN          586..683
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   693 AA;  76932 MW;  F846A8F91D7E0DA8 CRC64;
     MAHTFLLEIG LEEIPAHVVT PSVNQLVAKV ENYLKEERLA FDSVLPFSTP RRLAVKVTGL
     ADKQEDISTE AKGPAKKIAQ DAEGNWTKAA QGFARGQGLT TDDLFFKELK GVEYVYANKF
     EAGKSALEVL AGMKEVAMSL KFPTMMRWGT NDFEYVRPIR WLVALLDNEV VNFDILGTKT
     GRVSQGHRFL GKEVTLNSTD DYPEALLAES VIADATKRKN MIRGQINDLA QENGWKVDID
     EDLLEEVNNL VEWPTVFAGN FDEKYLAVPD VVLITSMKDN QRYFYVTDAA GKLLPHFIAI
     RNGKDAFLNN VIAGNEKVLT ARLEDAKFFF EEDQKQSLQH YVDRLDKVMF HDKIGTLAQK
     MQRVGLLAQF LGQKLGLSDQ ELADLARASQ IYKFDLVTGM VGEFSELQGV MGEIYANLMG
     ENAVVAQAIR EEYMPTSAEG VLPASTVGSV LSIADKLDSL QAFFSAGMVP SGSNDPYALR
     RQTLGIIRIA LANNWQLSVD DLMDAVAFAQ GKAHDLYANI DPATNAQALR DFVADRLHQI
     LANDHYRHDV LETVVANMAN TFVDVSQAAK TLTAHLDDAD FKETIEALTR VARLAAKADL
     SQTLTVDESL FENDSEKALF AAYQVQKEAM EAANDYDAKY QAIHALKDAI SAYFEATMVM
     VEDTAVKNNR LHQLVLVKQL TQNFGDLAQL NVK
//
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