ID   A0A0U2NSY0_9ENTE        Unreviewed;       693 AA.
AC   A0A0U2NSY0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=ATZ35_13950 {ECO:0000313|EMBL:ALS38210.1};
OS   Enterococcus rotai.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=118060 {ECO:0000313|EMBL:ALS38210.1, ECO:0000313|Proteomes:UP000067523};
RN   [1] {ECO:0000313|EMBL:ALS38210.1, ECO:0000313|Proteomes:UP000067523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 26678 {ECO:0000313|EMBL:ALS38210.1,
RC   ECO:0000313|Proteomes:UP000067523};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) 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}.
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DR   EMBL; CP013655; ALS38210.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U2NSY0; -.
DR   STRING; 118060.ATZ35_13950; -.
DR   Proteomes; UP000067523; Chromosome.
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}.
SQ   SEQUENCE   693 AA;  78774 MW;  3B2CE238A5C70E13 CRC64;
     MAKDLLLEIG LEEMPAHIVS PSRIQLENKI VKFLDENKLT YETVQSFSTP RRLAVRVTQL
     PEQQEDTQEE VKGPAKKIAQ DSEGNWSKAA EGFVRGQGLT TEAITFKELN GVEYVYVTKQ
     NHGQKTLDVL AGLKEVITSL TFPVTMHWAD HEFEYIRPIH WIVALLDDEV IPFSVLDVTT
     GKKSRGHRFL GDDVTFDHSK EYEEKMKEQF VIVDPNERKT MITDQANQLA EKYHWTLDLD
     ENLLEEVNNL VEYPTAFVGA FDEKYLSVPE EVLVTSMKEH QRYFDVRNEQ GLLLPHFISV
     RNGDSVHIEN VIKGNEKVLI ARLEDAEFFY SEDKKLSIEE CIEKLKSVTF HEKIGTIYEK
     MQRVGVIGQI IGKEVGLSND ELTDLKRASE IYKFDLVTNM VGEFPELQGI MGEKYALLQG
     EKPTVAQAIR EHYLPTSSDG DLPESTIGAV LALADKLDSV FAFFAVGMIP SGSNDPYALR
     RQTYGVIRII EEKGWQFPLV QLQMDIDAAV NADSEKYGVQ LTSGQEEVID FVKARLRQLL
     MTKDVRHDVI DAVISSEQKD LAKLFSSATI LKKHLLDKDF RPSIEALTRV INLAKKGHDL
     LNQESEVDAA LFENDAEKAL HQAVDKIEEQ FAENTMSENY QALVALRPLI EQYFEETMVM
     VEDEQVKVNR LKELNRIAKM SLSLASLDLL IVK
//