ID   CDLS_CORJK              Reviewed;         216 AA.
AC   Q4JVS0;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 65.
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   OrderedLocusNames=jk0923;
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=306537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411;
RX   PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA   Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA   Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant nosocomial
RT   pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT   human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
RN   [2]
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).
CC   -!- FUNCTION: It uses activated amino acids in the form of aminoacyl-tRNAs
CC       (aa-tRNAs) as substrates to catalyze the ATP-independent formation of
CC       cyclodipeptides which are intermediates in diketopiperazine (DKP)
CC       biosynthetic pathways. Catalyzes the formation of cyclo(L-Leu-L-Leu)
CC       (cLL) from L-leucyl-tRNA(Leu). Can incorporate various nonpolar
CC       residues, such as L-leucine and L-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   -!- SIMILARITY: Belongs to the CDPS family. {ECO:0000305}.
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DR   EMBL; CR931997; CAI37087.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4JVS0; -.
DR   SMR; Q4JVS0; -.
DR   STRING; 306537.jk0923; -.
DR   EnsemblBacteria; CAI37087; CAI37087; jk0923.
DR   KEGG; cjk:jk0923; -.
DR   eggNOG; ENOG50332PQ; Bacteria.
DR   HOGENOM; CLU_084186_1_0_11; -.
DR   OMA; LIWERRE; -.
DR   Proteomes; UP000000545; Chromosome.
DR   GO; GO:0016755; F:aminoacyltransferase activity; IEA:InterPro.
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..216
FT                   /note="Cyclo(L-leucyl-L-leucyl) synthase"
FT                   /id="PRO_0000423354"
FT   ACT_SITE        14
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         155..159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            17
FT                   /note="Could have a critical role in the catalytic
FT                   mechanism"
FT                   /evidence="ECO:0000250"
FT   SITE            65
FT                   /note="Could be involved in aa-tRNA binding"
FT                   /evidence="ECO:0000250"
FT   SITE            75
FT                   /note="Could be involved in aa-tRNA binding"
FT                   /evidence="ECO:0000250"
FT   SITE            155
FT                   /note="Could be involved in aa-tRNA binding"
FT                   /evidence="ECO:0000250"
FT   SITE            159
FT                   /note="Could have a critical role in the catalytic
FT                   mechanism"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   216 AA;  24549 MW;  987F0F9F4041BBAD CRC64;
     MGESKQEHLI VGVSPFNPRF TPEWLSSAFQ WGAERFNTVD VLHPGEISMS LLTSTGTPLG
     RAKRKVRQQC NRDMRNVEHA LEISGIKLGR GKPVLISDYL QTQSYQCRRR SVIAEFQNNQ
     IFQDACRAMS RAACQSRLRV TNVNIEPDIE TAVKYIFDEL PAYTHCSDLF EYETAALGYP
     TEWPIGKLIE SGLTSLERDP NSSFIVIDFE KELIDD