CDLS_BACSU
ID CDLS_BACSU Reviewed; 248 AA.
AC O34351; Q795E6;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Cyclo(L-leucyl-L-leucyl) synthase;
DE EC=2.3.2.22;
DE AltName: Full=Cyclodileucine synthase;
DE AltName: Full=Cyclodipeptide synthase;
DE Short=CDPS;
GN Name=yvmC; OrderedLocusNames=BSU35070;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.;
RT "Nucleotide sequence of the 300-304 chromosomal segment of Bacillus
RT subtilis.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=19430487; DOI=10.1038/nchembio.175;
RA Gondry M., Sauguet L., Belin P., Thai R., Amouroux R., Tellier C.,
RA Tuphile K., Jacquet M., Braud S., Courcon M., Masson C., Dubois S.,
RA Lautru S., Lecoq A., Hashimoto S., Genet R., Pernodet J.L.;
RT "Cyclodipeptide synthases arec a family of tRNA-dependent peptide bond-
RT forming enzymes.";
RL Nat. Chem. Biol. 5:414-420(2009).
RN [4]
RP SUBUNIT.
RX PubMed=21325056; DOI=10.1073/pnas.1019480108;
RA Bonnefond L., Arai T., Sakaguchi Y., Suzuki T., Ishitani R., Nureki O.;
RT "Structural basis for nonribosomal peptide synthesis by an aminoacyl-tRNA
RT synthetase paralog.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:3912-3917(2011).
CC -!- FUNCTION: Involved in the biosynthesis of pulcherrimin, a red
CC extracellular pigment. It uses activated amino acids in the form of
CC aminoacyl-tRNAs (aa-tRNAs) as substrates to catalyze the ATP-
CC independent formation of cyclodipeptides which are intermediates in
CC diketopiperazine (DKP) biosynthetic pathways. Catalyzes the formation
CC of cyclo(L-Leu-L-Leu) (cLL) from L-leucyl-tRNA(Leu). Can also
CC incorporate various nonpolar residues, such as L-phenylalanine, L-
CC leucine and methionine, into cyclodipeptides.
CC {ECO:0000269|PubMed:19430487}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-leucyl-tRNA(Leu) = cyclo(L-leucyl-L-leucyl) + 2 H(+) + 2
CC tRNA(Leu); Xref=Rhea:RHEA:46452, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:15378, ChEBI:CHEBI:67269, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78494; EC=2.3.2.22;
CC Evidence={ECO:0000269|PubMed:19430487};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:21325056}.
CC -!- SIMILARITY: Belongs to the CDPS family. {ECO:0000305}.
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DR EMBL; AF017113; AAC67279.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15512.1; -; Genomic_DNA.
DR PIR; A70044; A70044.
DR RefSeq; NP_391387.1; NC_000964.3.
DR RefSeq; WP_003242712.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O34351; -.
DR SMR; O34351; -.
DR STRING; 224308.BSU35070; -.
DR PaxDb; O34351; -.
DR EnsemblBacteria; CAB15512; CAB15512; BSU_35070.
DR GeneID; 936633; -.
DR KEGG; bsu:BSU35070; -.
DR PATRIC; fig|224308.179.peg.3796; -.
DR eggNOG; ENOG50332PQ; Bacteria.
DR InParanoid; O34351; -.
DR OMA; LAYHRPW; -.
DR BioCyc; BSUB:BSU35070-MON; -.
DR BioCyc; MetaCyc:BSU35070-MON; -.
DR BRENDA; 2.3.2.22; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016755; F:aminoacyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046148; P:pigment biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.11710; -; 1.
DR InterPro; IPR030903; CDPS.
DR InterPro; IPR038622; CDPS_sf.
DR Pfam; PF16715; CDPS; 1.
DR TIGRFAMs; TIGR04539; tRNA_cyclodipep; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase.
FT CHAIN 1..248
FT /note="Cyclo(L-leucyl-L-leucyl) synthase"
FT /id="PRO_0000359945"
FT ACT_SITE 37
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180..184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 209..210
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 40
FT /note="Could have a critical role in the catalytic
FT mechanism"
FT /evidence="ECO:0000250"
FT SITE 88
FT /note="Could be involved in aa-tRNA binding"
FT /evidence="ECO:0000250"
FT SITE 98
FT /note="Could be involved in aa-tRNA binding"
FT /evidence="ECO:0000250"
FT SITE 180
FT /note="Could be involved in aa-tRNA binding(Leu) binding"
FT /evidence="ECO:0000250"
FT SITE 184
FT /note="Could have a critical role in the catalytic
FT mechanism"
FT /evidence="ECO:0000250"
SQ SEQUENCE 248 AA; 28507 MW; 17DFF79833A0B1B8 CRC64;
MTGMVTERRS VHFIAEALTE NCREIFERRR HVLVGISPFN SRFSEDYIYR LIGWAKAQFK
SVSVLLAGHE AANLLEALGT PRGKAERKVR KEVSRNRRFA ERALVAHGGD PKAIHTFSDF
IDNKAYQLLR QEVEHAFFEQ PHFRHACLDM SREAIIGRAR GVSLMMEEVS EDMLNLAVEY
VIAELPFFIG APDILEVEET LLAYHRPWKL GEKISNHEFS ICMRPNQGYL IVQEMAQMLS
EKRITSEG
