(data stored in ACNUC7421 zone)

SWISSPROT: SYC_BACSU

ID   SYC_BACSU               Reviewed;         466 AA.
AC   Q06752;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   11-DEC-2019, entry version 145.
DE   RecName: Full=Cysteine--tRNA ligase;
DE            EC=6.1.1.16;
DE   AltName: Full=Cysteinyl-tRNA synthetase;
DE            Short=CysRS;
GN   Name=cysS; Synonyms=spnA; OrderedLocusNames=BSU00940;
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=7510287;
RA   Gagnon Y., Breton R., Putzer H., Pelchat M., Grunberg-Manago M.,
RA   Lapointe J.;
RT   "Clustering and co-transcription of the Bacillus subtilis genes encoding
RT   the aminoacyl-tRNA synthetases specific for glutamate and for cysteine and
RT   the first enzyme for cysteine biosynthesis.";
RL   J. Biol. Chem. 269:7473-7482(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8194536; DOI=10.1002/j.1460-2075.1994.tb06532.x;
RA   Seror S.J., Casaregola S., Vannier F., Zouari N., Dahl M., Boye E.;
RT   "A mutant cysteinyl-tRNA synthetase affecting timing of chromosomal
RT   replication initiation in B. subtilis and conferring resistance to a
RT   protein kinase C inhibitor.";
RL   EMBO J. 13:2472-2480(1994).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=168;
RX   PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA   Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA   Mann M.;
RT   "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT   Bacillus subtilis.";
RL   Mol. Cell. Proteomics 6:697-707(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-
CC         cysteinyl-tRNA(Cys); Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661,
CC         Rhea:RHEA-COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78517,
CC         ChEBI:CHEBI:456215; EC=6.1.1.16;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
DR   EMBL; L14580; AAA21798.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05328.1; -; Genomic_DNA.
DR   EMBL; X73989; CAA52167.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11870.1; -; Genomic_DNA.
DR   PIR; C53402; C53402.
DR   RefSeq; NP_387975.1; NC_000964.3.
DR   RefSeq; WP_004399682.1; NZ_JNCM01000029.1.
DR   SMR; Q06752; -.
DR   IntAct; Q06752; 1.
DR   MINT; Q06752; -.
DR   STRING; 224308.BSU00940; -.
DR   iPTMnet; Q06752; -.
DR   jPOST; Q06752; -.
DR   PaxDb; Q06752; -.
DR   PRIDE; Q06752; -.
DR   EnsemblBacteria; CAB11870; CAB11870; BSU00940.
DR   GeneID; 936859; -.
DR   KEGG; bsu:BSU00940; -.
DR   PATRIC; fig|224308.179.peg.97; -.
DR   eggNOG; ENOG4105C8N; Bacteria.
DR   eggNOG; COG0215; LUCA.
DR   HOGENOM; HOG000245250; -.
DR   InParanoid; Q06752; -.
DR   KO; K01883; -.
DR   OMA; AKYWMHN; -.
DR   PhylomeDB; Q06752; -.
DR   BioCyc; BSUB:BSU00940-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd00672; CysRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR   InterPro; IPR015803; Cys-tRNA-ligase.
DR   InterPro; IPR015273; Cys-tRNA-synt_Ia_DALR.
DR   InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR10890; PTHR10890; 1.
DR   Pfam; PF09190; DALR_2; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   SMART; SM00840; DALR_2; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   TIGRFAMs; TIGR00435; cysS; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q06752.
DR   SWISS-2DPAGE; Q06752.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome; Zinc.
FT   CHAIN           1..466
FT                   /note="Cysteine--tRNA ligase"
FT                   /id="PRO_0000159352"
FT   MOTIF           31..41
FT                   /note="'HIGH' region"
FT   MOTIF           266..270
FT                   /note="'KMSKS' region"
FT   METAL           29
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           209
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           234
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           238
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         270
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
SQ   SEQUENCE   466 AA;  53908 MW;  742D225C2E377CC3 CRC64;
     MTITLYNTLT RQKETFVPLE EGKVKMYVCG PTVYNYIHIG NARPAIVYDT VRNYLEYKGY
     DVQYVSNFTD VDDKLIKAAN ELGEDVPTIS ERFIKAYFED VGALGCRKAD LHPRVMENMD
     AIIEFVDQLV KKGYAYESEG DVYFKTRAFE GYGKLSQQSI DELRSGARIR VGEKKEDALD
     FALWKAAKEG EISWDSPWGK GRPGWHIECS AMVKKYLGDQ IDIHAGGQDL TFPHHENEIA
     QSEALTGKTF AKYWLHNGYI NIDNEKMSKS LGNFVLVHDI IKQHDPQLLR FFMLSVHYRH
     PINYSEELLE NTKSAFSRLK TAYSNLQHRL NSSTNLTEDD DQWLEKVEEH RKAFEEEMDD
     DFNTANAISV LFDLAKHANY YLQKDHTADH VITAFIEMFD RIVSVLGFSL GEQELLDQEI
     EDLIEKRNEA RRNRDFALSD QIRDQLKSMN IILEDTAQGT RWKRGE
//

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