SYT1_BACSU
ID SYT1_BACSU Reviewed; 643 AA.
AC P18255; P06570;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Threonine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00184};
DE EC=6.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00184};
DE AltName: Full=Threonyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00184};
DE Short=ThrRS 1 {ECO:0000255|HAMAP-Rule:MF_00184};
GN Name=thrS; Synonyms=thrSV; OrderedLocusNames=BSU28950;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2115870; DOI=10.1128/jb.172.8.4593-4602.1990;
RA Putzer H., Brakhage A., Grunberg-Manago M.;
RT "Independent genes for two threonyl-tRNA synthetases in Bacillus
RT subtilis.";
RL J. Bacteriol. 172:4593-4602(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA Emmerson P.T., Harwood C.R.;
RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT chromosome containing genes responsible for stress responses, the
RT utilization of plant cell walls and primary metabolism.";
RL Microbiology 142:3067-3078(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-180.
RX PubMed=3027671; DOI=10.1093/nar/14.24.9989;
RA Ogasawara N., Moriya S., Mazza P.G., Yoshikawa H.;
RT "Nucleotide sequence and organization of dnaB gene and neighbouring genes
RT on the Bacillus subtilis chromosome.";
RL Nucleic Acids Res. 14:9989-9999(1986).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=1379177; DOI=10.1002/j.1460-2075.1992.tb05384.x;
RA Putzer H., Gendron N., Grunberg-Manago M.;
RT "Co-ordinate expression of the two threonyl-tRNA synthetase genes in
RT Bacillus subtilis: control by transcriptional antitermination involving a
RT conserved regulatory sequence.";
RL EMBO J. 11:3117-3127(1992).
CC -!- FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-
CC step reaction: L-threonine is first activated by ATP to form Thr-AMP
CC and then transferred to the acceptor end of tRNA(Thr). Also edits
CC incorrectly charged L-seryl-tRNA(Thr). {ECO:0000255|HAMAP-
CC Rule:MF_00184}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-
CC threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670,
CC Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00184};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00184};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00184};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00184}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184}.
CC -!- DEVELOPMENTAL STAGE: Expressed during vegetative growth.
CC {ECO:0000269|PubMed:1379177}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00184}.
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; M36594; AAA22864.1; -; Genomic_DNA.
DR EMBL; Z75208; CAA99608.1; -; Genomic_DNA.
DR EMBL; AF008220; AAC00362.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14855.1; -; Genomic_DNA.
DR EMBL; X04963; CAA28636.1; -; Genomic_DNA.
DR PIR; B37770; YSBST1.
DR RefSeq; NP_390773.1; NC_000964.3.
DR RefSeq; WP_003229473.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P18255; -.
DR SMR; P18255; -.
DR IntAct; P18255; 1.
DR MINT; P18255; -.
DR STRING; 224308.BSU28950; -.
DR jPOST; P18255; -.
DR PaxDb; P18255; -.
DR PRIDE; P18255; -.
DR EnsemblBacteria; CAB14855; CAB14855; BSU_28950.
DR GeneID; 937410; -.
DR KEGG; bsu:BSU28950; -.
DR PATRIC; fig|224308.179.peg.3143; -.
DR eggNOG; COG0441; Bacteria.
DR InParanoid; P18255; -.
DR OMA; FYYDFAY; -.
DR PhylomeDB; P18255; -.
DR BioCyc; BSUB:BSU28950-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_00184; Thr_tRNA_synth; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR033728; ThrRS_core.
DR InterPro; IPR012947; tRNA_SAD.
DR PANTHER; PTHR11451; PTHR11451; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF02824; TGS; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00418; thrS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51880; TGS; 1.
PE 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding; Zinc.
FT CHAIN 1..643
FT /note="Threonine--tRNA ligase 1"
FT /id="PRO_0000100938"
FT DOMAIN 3..64
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT REGION 245..542
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 519
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ SEQUENCE 643 AA; 73515 MW; 11DFF31CF5800ADE CRC64;
MSDMVKITFP DGAVKEFAKG TTTEDIAASI SPGLKKKSLA GKLNGKEIDL RTPINEDGTV
EIITEGSEEG LQIMRHSAAH LLAQAIKRIY KDVKFGVGPV IENGFYYDVE MDEAITPEDL
PKIEKEMKKI VNANLPIVRK EVSREEAKAR FAEIGDDLKL ELLDAIPEGE TVSIYEQGEF
FDLCRGVHVP STGKIKEFKL LSLAGAYWRG DSKNQMLQRV YGTAFFKKAD LEEHLRMLEE
AKERDHRKLG KELKLFANSQ KVGQGLPLWL PKGATIRRVI ERYIVDKEIS LGYEHVYTPV
LGSKELYETS GHWDHYQEGM FPPMEMDNET LVLRPMNCPH HMMIYKQDIH SYRELPIRIA
ELGTMHRYEM SGALSGLQRV RGMTLNDAHI FVRPDQIKDE FIRTVRLIQD VYEDFGLSDY
TFRLSYRDPE DTEKYFDDDE MWNKAQSMLK EAMDEIGHDY YEAEGEAAFY GPKLDVQVKT
AIGKEETLST VQLDFLLPER FDLTYIGEDG KQHRPVVIHR GVVSTMERFV AFLIEEHKGA
LPTWLAPVQF QVIPVSPAVH LDYAKKVQER LQCEGLRVEV DSRDEKIGYK IREAQMQKIP
YMLVVGDQEA ENGAVNVRKY GEQNSETISL DEFVKKAVAE AKK
