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 03-AUG-2022, entry version 153.
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; DOI=10.1016/s0021-9258(17)37310-6;
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}.
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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 AlphaFoldDB; Q06752; -.
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; BSU_00940.
DR GeneID; 936859; -.
DR KEGG; bsu:BSU00940; -.
DR PATRIC; fig|224308.179.peg.97; -.
DR eggNOG; COG0215; Bacteria.
DR InParanoid; Q06752; -.
DR OMA; AKYWMHN; -.
DR PhylomeDB; Q06752; -.
DR BioCyc; BSUB:BSU00940-MON; -.
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;
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 BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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
