ID A0A1U9JLW2_9NEIS Unreviewed; 691 AA.
AC A0A1U9JLW2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=BXU06_08285 {ECO:0000313|EMBL:AQR65059.1};
OS Aquaspirillum sp. LM1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Aquaspirillaceae; Aquaspirillum.
OX NCBI_TaxID=1938604 {ECO:0000313|EMBL:AQR65059.1, ECO:0000313|Proteomes:UP000188659};
RN [1] {ECO:0000313|EMBL:AQR65059.1, ECO:0000313|Proteomes:UP000188659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM1 {ECO:0000313|EMBL:AQR65059.1,
RC ECO:0000313|Proteomes:UP000188659};
RA Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT "Genome sequences of bacteria isolated from the littoral zone of southern
RT Lake Michigan.";
RL Submitted (JAN-2017) 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|ARBA:ARBA00011209, 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP019509; AQR65059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9JLW2; -.
DR STRING; 1938604.BXU06_08285; -.
DR KEGG; aql:BXU06_08285; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000188659; Chromosome.
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:UP000188659}.
FT DOMAIN 582..678
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 691 AA; 73774 MW; 6EE30BA74A6787B6 CRC64;
MKHTLLVELF TEELPPKALP RLAASFAGAI VASLIEKKLV AADAQPTIFA SPRRLGVSIP
AVLAVAADEE AVEKIMPVAV ALGADGQPSP ALRKKLEARG IALDAVAQFE RRLDGKSETF
FYRYQAAGAK LADVLAGMVQ DALKKLPIPK VMRWGDSDVT FVRPVHKLVM LHGADVVAGE
VLGLTAGRET GGHRFLSAGA VTLTDADSYA STLHSVGKVV ASFDARRDAI RAGLASRAAA
LNATLASDDA LLDEVTALVE WPVVLEAGFA ETFLNVPQEC LILTMQQNQK YFPLLDAQGK
LMNRFLLVSN LENADPSHII HGNERVLRAR LSDAKFFFEQ DQKQKLESRV PRLGNVVYHN
QIGTQLERVE RLESLAGQIA ALIGANVDDA RRAARLAKAD LVSDMVGEFP ELQGIMGMYY
AHLDGENDTV AAAIEGHYHP RFAGDSLPVG DVAKAVALAD KLETVVGIYG IGLIPTGDKD
PFGLRRHALG ILRMALELPL DITELLALTA AAFPAGKLSA SVASDVFGFM LDRLKNLLLA
DARADEIDAV LALAPTRLDR LRATLAAVAA FRALPEAATL AAANKRVKNI LKKVEGEVSD
TLNPALLAEA AEQALAAAIV TVRSEVDSAY AAHDLTGALT RLAALKAPVD AFFDGVMVMA
DDLAVRQNRL ALLAQLAGLF NRVADISLLL E
//
