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Database: UniProt
Entry: A0A0F4KR76_9LACO
LinkDB: A0A0F4KR76_9LACO
Original site: A0A0F4KR76_9LACO 
ID   A0A0F4KR76_9LACO        Unreviewed;       693 AA.
AC   A0A0F4KR76;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
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   ECO:0000313|EMBL:KJY48910.1};
GN   ORFNames=JG29_07300 {ECO:0000313|EMBL:KJY48910.1};
OS   Bombilactobacillus mellis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Bombilactobacillus.
OX   NCBI_TaxID=1218508 {ECO:0000313|EMBL:KJY48910.1, ECO:0000313|Proteomes:UP000033695};
RN   [1] {ECO:0000313|EMBL:KJY48910.1, ECO:0000313|Proteomes:UP000033695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hon2 {ECO:0000313|EMBL:KJY48910.1,
RC   ECO:0000313|Proteomes:UP000033695};
RA   Ellegaard K.M., Tamarit D., Javelind E., Olofsson T., Andersson S.G.,
RA   Vasquez A.;
RT   "Comparative genomics of the lactic acid bacteria isolated from the honey
RT   bee gut.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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:KJY48910.1}.
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DR   EMBL; JXBZ01000007; KJY48910.1; -; Genomic_DNA.
DR   RefSeq; WP_045922579.1; NZ_KQ033877.1.
DR   AlphaFoldDB; A0A0F4KR76; -.
DR   STRING; 1218508.JG29_07300; -.
DR   PATRIC; fig|1218508.4.peg.748; -.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000033695; 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; IPR016024; ARM-type_fold.
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; SSF48371; ARM repeat; 1.
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:UP000033695}.
SQ   SEQUENCE   693 AA;  78709 MW;  7A6960239E56BA43 CRC64;
     MGKTFLLEIG LEEMPAHVVS SASLQLKQRV SDYLTAQKLE FQDIQAYSTP RRLAVLVHEL
     ADQQPDENIA VKGPAKKIAL DKEGHWSKAA QGFVRGQKMT TDDIYFQDVK GTEYVYVQKH
     IAGQSAVQVL QGLIEPIKAM TFPTRMRWNK FDFAYIRPIH WLVAMLDQQV IDLKLLNITA
     NNQTRGHRFL GSTITLATAQ DYQKALADDY VIVDAQERKN LIRQQIAALA AENNWQVDVD
     EDLLEEVNNL VEYPTAFAGK FSEKYLEMPE EVLITSMKDN QRYFYVRKKD GSLAPNFIAV
     RNGNQEYLEN VIAGNEKVLV ARLDDAAFFF AEDQKHDLNY YVRQLQHVTF HDKIGSMSEK
     MARTKVIADL LAQKLQLSSS DTAAVLRAAE IYKFDLVTDM VGEFAELQGV MGEKYALLMG
     EKPAVAQAIR EHYLPNSAEG QLPQSLVGSV LAVADKLESI MSFFAVDLIP NGSNDPYGLR
     RQALGIIRIL EQRNWQLNLH QLQNEIVAAY QKQFSTLKFD YFKHQAEVDE FLIDRIRQLF
     SQDQVAHDLI DTVVALPSLD PTAMQQLVQV ISHHQTDPDF KGAIEALTRV LRITQKAPLT
     DSTDLAVDPQ LFQTDSEKQL YQAVQACQAD FKDSDFEQKY QALAHLEPVI TDYFTVNMVM
     DPNPEIRNNR LHQLQQLATL IKQLGDLNQL IVK
//
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