CDLS_STAHJ
ID CDLS_STAHJ Reviewed; 234 AA.
AC Q4L2X9;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=pSHaeC06;
OS Staphylococcus haemolyticus (strain JCSC1435).
OG Plasmid pSHaeC.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(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-phenylalanine, L-leucine and L-methionine, into
CC cyclodipeptides. {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}.
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; AP006719; BAE05998.1; -; Genomic_DNA.
DR RefSeq; WP_011276926.1; NC_007171.1.
DR PDB; 6EZ3; X-ray; 3.00 A; A/B/C/D/E/F=1-234.
DR PDBsum; 6EZ3; -.
DR AlphaFoldDB; Q4L2X9; -.
DR SMR; Q4L2X9; -.
DR EnsemblBacteria; BAE05998; BAE05998; pSHaeC06.
DR KEGG; sha:pSHaeC06; -.
DR HOGENOM; CLU_084186_1_0_9; -.
DR OMA; LAYHRPW; -.
DR OrthoDB; 1802439at2; -.
DR BRENDA; 2.3.2.22; 5877.
DR Proteomes; UP000000543; Plasmid pSHaeC.
DR GO; GO:0016755; F:aminoacyltransferase activity; 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 3D-structure; Plasmid; Transferase.
FT CHAIN 1..234
FT /note="Cyclo(L-leucyl-L-leucyl) synthase"
FT /id="PRO_0000423352"
FT ACT_SITE 28
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 171..175
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 200..201
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 79
FT /note="Could be involved in aa-tRNA binding"
FT /evidence="ECO:0000250"
FT SITE 89
FT /note="Could be involved in aa-tRNA binding"
FT /evidence="ECO:0000250"
FT SITE 171
FT /note="Could be involved in aa-tRNA binding"
FT /evidence="ECO:0000250"
FT SITE 175
FT /note="Could have a critical role in the catalytic
FT mechanism"
FT /evidence="ECO:0000250"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:6EZ3"
FT HELIX 11..19
FT /evidence="ECO:0007829|PDB:6EZ3"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:6EZ3"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:6EZ3"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:6EZ3"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:6EZ3"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:6EZ3"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:6EZ3"
FT HELIX 73..97
FT /evidence="ECO:0007829|PDB:6EZ3"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:6EZ3"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:6EZ3"
FT TURN 109..114
FT /evidence="ECO:0007829|PDB:6EZ3"
FT HELIX 116..131
FT /evidence="ECO:0007829|PDB:6EZ3"
FT HELIX 133..149
FT /evidence="ECO:0007829|PDB:6EZ3"
FT HELIX 162..175
FT /evidence="ECO:0007829|PDB:6EZ3"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:6EZ3"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:6EZ3"
FT STRAND 189..197
FT /evidence="ECO:0007829|PDB:6EZ3"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:6EZ3"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:6EZ3"
SQ SEQUENCE 234 AA; 27355 MW; B8BBBD0E0D64F850 CRC64;
MQNFKVDFLT KNCKQIYQRK KHVILGISPF TSKYNESYIR KIIQWANSNF DDFSILLAGE
ESKNLLECLG YSSSKANQKV RKEIKRQIRF CEDEIIKCNK TITNRIHRFS DFKNNIYYID
IYKTIVDQFN TDSNFKNSCL KMSLQALQSK GKNVNTSIEI TDETLEYAAQ YVLAELPFFL
NANPIINTQE TLMAYHAPWE LGTNIINDQF NLKMNEKQGY IILTEKGDNY VKSV
