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Database: UniProt
Entry: E9CMU1_9GAMM
LinkDB: E9CMU1_9GAMM
Original site: E9CMU1_9GAMM 
ID   E9CMU1_9GAMM            Unreviewed;       403 AA.
AC   E9CMU1;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000256|ARBA:ARBA00022032};
DE            EC=6.1.1.14 {ECO:0000256|ARBA:ARBA00012829};
DE   AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000256|ARBA:ARBA00031650};
DE   Flags: Fragment;
GN   Name=glyS {ECO:0000313|EMBL:EFW12168.1};
GN   ORFNames=SSYM_1841 {ECO:0000313|EMBL:EFW12168.1};
OS   Serratia symbiotica str. Tucson.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia; Serratia symbiotica.
OX   NCBI_TaxID=914128 {ECO:0000313|EMBL:EFW12168.1, ECO:0000313|Proteomes:UP000013568};
RN   [1] {ECO:0000313|Proteomes:UP000013568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson {ECO:0000313|Proteomes:UP000013568};
RX   PubMed=21266540;
RA   Burke G.R., Moran N.A.;
RT   "Massive genomic decay in Serratia symbiotica, a recently evolved symbiont
RT   of aphids.";
RL   Genome Biol. Evol. 3:195-208(2011).
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   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|ARBA:ARBA00011209}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226}.
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DR   EMBL; GL636117; EFW12168.1; -; Genomic_DNA.
DR   RefSeq; WP_006709142.1; NZ_GL636117.1.
DR   AlphaFoldDB; E9CMU1; -.
DR   HOGENOM; CLU_007220_3_0_6; -.
DR   Proteomes; UP000013568; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro.
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   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000313|EMBL:EFW12168.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013568}.
FT   NON_TER         403
FT                   /evidence="ECO:0000313|EMBL:EFW12168.1"
SQ   SEQUENCE   403 AA;  44444 MW;  7B4D347EB26D0118 CRC64;
     MTQQTFLVEI GTEELPPKAL RSLAGAFAAN FTTELENANL EHGSVSWFAT PRRLALKVAN
     LSAAQADRIV EKRGPAISQA FDATGKPNKA AEGWARGGGI TVDQAERLVT DKGEWLLYRA
     HVKGQPVQQL LASMVNTALS KLPIPKLMRW GDSEVQFVRP VHTVTLLLGA ELIPGSVLGV
     ESARTIRGHR FMGETEFTLD NADHYPQILL ERGKVIADYE ARKALIKRDS ERAAAKIGGK
     ADLSESLLEE VASLVEWPVV LTAKFEEEFL AVPAEALVYT MKGDQKYFPV YGSAGNLLPN
     FIFVANIESK DPQQIITGNE KVVRPRLADA EFFFNTDRKK RLEDHLPRLD TVLFQQQLGT
     LRDKTDRIQA LAGWIAGQIG ADVNHATRAG LLSKCDLMTN MVF
//
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