SYGB_COXBU
ID SYGB_COXBU Reviewed; 689 AA.
AC P45651;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 2.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Glycine--tRNA ligase beta subunit;
DE EC=6.1.1.14;
DE AltName: Full=Glycyl-tRNA synthetase beta subunit;
DE Short=GlyRS;
GN Name=glyS; OrderedLocusNames=CBU_1914;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 404-689.
RC STRAIN=Nine Mile phase I / Bratislava;
RX PubMed=8071197; DOI=10.1128/jb.176.17.5233-5243.1994;
RA Suhan M., Chen S.Y., Thompson H.A., Hoover T.A., Hill A., Williams J.C.;
RT "Cloning and characterization of an autonomous replication sequence from
RT Coxiella burnetii.";
RL J. Bacteriol. 176:5233-5243(1994).
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;
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA56913.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAO91405.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE016828; AAO91405.2; ALT_INIT; Genomic_DNA.
DR EMBL; U10529; AAA56913.1; ALT_FRAME; Genomic_DNA.
DR PIR; I40648; I40648.
DR RefSeq; NP_820891.2; NC_002971.3.
DR AlphaFoldDB; P45651; -.
DR SMR; P45651; -.
DR STRING; 227377.CBU_1914; -.
DR EnsemblBacteria; AAO91405; AAO91405; CBU_1914.
DR GeneID; 1209827; -.
DR KEGG; cbu:CBU_1914; -.
DR PATRIC; fig|227377.7.peg.1898; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 PANTHER; PTHR30075; PTHR30075; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01045; TRNASYNTHGB.
DR TIGRFAMs; TIGR00211; glyS; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..689
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_0000072898"
FT CONFLICT 404
FT /note="F -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="S -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 689 AA; 77974 MW; F67660BAD15208AA CRC64;
MTTQDFLLEI GCEELPPRRL NQLSQALSQT IKSELEKADL SFENIHRYAT PRRLAVLVNN
LALQQPQRKI ERQGPSVKAA FDKDQTPTLA CFGFAQSCGV STAQLKVKKT KKGEFIYCEI
EQPGQNTLDL LPNIIQSALK QLPTPKAMRW GDHKEFFVRP VHWIILMLGK DLVPATLLGK
MASCETRGHR FHHPKNILVT KPDDYQKLLL THGMVIADFE KRREKIRDLI QKAASEKGEA
IIDEGLLEEV TGMVEWPVIL VGNFKAEFLK LPPEVLITTM KVHQRTFPIK NKNGDLLPYF
IIVSNIESKN PKRVIVGNER VINARLADAS FFYDNDLRTS LENRLPKLGD VIFQRQLGTL
ADKARRIEKL AAFIAKQINI DEQLAARAGL LSKCDLVSEM VYEFPTLQGI MGYYYAFHDK
EPPLVAEAIK EHYLPRFSGD QLPRNLLSPC VAVADRIDTI IGIIGINKSP TGDKDPFALR
RAALGILRIL IEKELSLDLF ALLNEAKNNY AVELPNVNVV NQSFDFIIER LRAWYLEKEV
PASVFMAVLA SHPDDPLDFD RRIKAVQHFQ TLPEADALAA ANKRVSNILK KQAAELKSKT
IDHSLFDSDA EHLLADQLKE RAELVNNLYK KADYTKALSE LASLKEPIDI FFDKVMVMVD
DKEKRENRLA LLSSLQQLFS QIADISLLS