ID A0A0Q6TVE0_9CAUL Unreviewed; 802 AA.
AC A0A0Q6TVE0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=ASC62_11730 {ECO:0000313|EMBL:KQV56954.1};
OS Caulobacter sp. Root342.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1736519 {ECO:0000313|EMBL:KQV56954.1, ECO:0000313|Proteomes:UP000051656};
RN [1] {ECO:0000313|EMBL:KQV56954.1, ECO:0000313|Proteomes:UP000051656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root342 {ECO:0000313|EMBL:KQV56954.1,
RC ECO:0000313|Proteomes:UP000051656};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV56954.1, ECO:0000313|Proteomes:UP000051656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root342 {ECO:0000313|EMBL:KQV56954.1,
RC ECO:0000313|Proteomes:UP000051656};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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|ARBA:ARBA00011209, 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:KQV56954.1}.
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DR EMBL; LMDD01000007; KQV56954.1; -; Genomic_DNA.
DR RefSeq; WP_056050683.1; NZ_LMDD01000007.1.
DR AlphaFoldDB; A0A0Q6TVE0; -.
DR STRING; 1736519.ASC62_11730; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000051656; 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; 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 802 AA; 88125 MW; 904F4E128F08A230 CRC64;
MPQLLLELFS EEIPARMQAQ AAKDLERMAR EHLAAAGFLP EALKTFAGPR RLTLVAEGLP
LAQADRKEEL KGPRVGAPPQ AMEGFLRKAG LTQDQLVERD GVYMAFIEKK GRPTPEIVAE
MVEAIVRNFP WPKSMTWGTK KLRWVRPLKR ILCVLDREVV PFAIEGIESG DITEGHRFMG
DAQPFVAKDF DEYAAGLEAH YVVLDVEERK ERILEGCKTL CFARHLELVE DQGLLEEVAG
LAEWPTPVLG DMDPVFLSLP SEVIRTSMRT HQKYFAVRKA GEQGLAPHFI TIANIQAADG
GAVIAAGNAK VLSSRLSDAR FFWDEDVKVG FEPWLKKLDG VTFHAKLGTM AQRVERIVAL
AGEIAPLVGA DVEKTKEAAR LAKADLASQM VGEFPELQGI MGGYYARTFG LDGEIADAVR
DHYKPQGPSD AVPTAPVSVA VALADKLDTL VGFFAIDEKP TGSKDPYALR RAALGVIRII
LENQIHAELR PLAVKSLVAM HANLDSTRLH AIWGRIEYGG LVDSISDEDI QFLLQSYFVD
RWLNFDGVVD DLQKKSKAAH GVVSPDSEVG TAVLKLHKPV GERIIDLAYL VERVRDPSKE
LSELTHENDV KHVRAEIENI PNIVAEKFSK DLRDFDSFFA DRLKVTLRDQ GKRHDLVDAV
FALGDDDLVR IVARVEALDG FLKTDDGKTL MAGYKRASNI LKAEEKKGAL PTGEPQAPAA
GSDAEVQLFD ALRVLKAPLA DALAREDFTG AMAQLAGLRG PVDAYLDGVF VNDPEHRDNR
LKTLAAVRDA MGQVADFGLI AG
//