ID   CYPA_STRSQ              Reviewed;          64 AA.
AC   E5KIB6;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Cypemycin {ECO:0000303|PubMed:7802859};
DE   Flags: Precursor;
GN   Name=cypA {ECO:0000312|EMBL:ADR72962.1};
OS   Streptomyces sp.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1931;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ADR72962.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 45-60, FUNCTION,
RP   MASS SPECTROMETRY, AND METHYLATION AT ALA-43.
RC   STRAIN=OH-4156 {ECO:0000269|PubMed:20805503};
RX   PubMed=20805503; DOI=10.1073/pnas.1008608107;
RA   Claesen J., Bibb M.;
RT   "Genome mining and genetic analysis of cypemycin biosynthesis reveal an
RT   unusual class of posttranslationally modified peptides.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:16297-16302(2010).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 43-64, FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=OH-4156 {ECO:0000269|PubMed:7802859};
RX   PubMed=7802859; DOI=10.7164/antibiotics.46.1666;
RA   Komiyama K., Otoguro K., Segawa T., Shiomi K., Yang H., Takahashi Y.,
RA   Hayashi M., Otani T., Omura S.;
RT   "A new antibiotic, cypemycin. Taxonomy, fermentation, isolation and
RT   biological characteristics.";
RL   J. Antibiot. 46:1666-1671(1993).
RN   [3] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 43-64, MASS SPECTROMETRY, DEHYDRATION AT THR-44;
RP   THR-47; THR-49 AND THR-59, METHYLATION AT ALA-43, THIOETHER BOND, AND
RP   STRUCTURE BY NMR.
RC   STRAIN=OH-4156 {ECO:0000269|Ref.3};
RX   DOI=10.1016/0040-4039(94)80033-2;
RA   Minami Y., Yoshida K., Azuma R., Urakawa A., Kawauchi T., Otani T.,
RA   Komiyama K., Omura S.;
RT   "Structure of cypemycin, a new peptide antibiotic.";
RL   Tetrahedron Lett. 35:8001-8004(1994).
CC   -!- FUNCTION: Antibiotic peptide structurally related to lantibiotics.
CC       Active against M.luteus (MIC=0.2 ug/ml). Has cytotoxic activity against
CC       mouse P388 leukemia cells (IC(50)=1.3 ug/ml).
CC       {ECO:0000269|PubMed:20805503, ECO:0000269|PubMed:7802859}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7802859}.
CC   -!- PTM: Maturation involves the enzymatic conversion of Cys-61 into 2,3-
CC       didehydroalanine followed by formation of a thioether bond with Cys-64.
CC       The C-terminal meso-lanthionine then undergoes decarboxylation.
CC       {ECO:0000269|Ref.3}.
CC   -!- PTM: Dimethylated at the N-terminus. Dimethylation is required for
CC       antibiotic activity. {ECO:0000269|PubMed:20805503, ECO:0000269|Ref.3}.
CC   -!- PTM: The configuration of reformed Cys-61 as the D form was attributed
CC       by similarity to related structures. {ECO:0000269|PubMed:20805503}.
CC   -!- MASS SPECTROMETRY: Mass=2094; Method=FAB;
CC       Evidence={ECO:0000269|PubMed:20805503, ECO:0000269|Ref.3};
CC   -!- MASS SPECTROMETRY: Mass=2096; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20805503, ECO:0000269|Ref.3};
CC   -!- SIMILARITY: Belongs to the linaridin family.
CC       {ECO:0000269|PubMed:20805503}.
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DR   EMBL; HQ148718; ADR72962.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5KIB6; -.
DR   iPTMnet; E5KIB6; -.
DR   GO; GO:0043245; C:extraorganismal space; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; D-amino acid; Direct protein sequencing;
KW   Methylation; Secreted; Thioether bond.
FT   PROPEP          1..42
FT                   /evidence="ECO:0000269|PubMed:7802859, ECO:0000269|Ref.3"
FT                   /id="PRO_0000408757"
FT   PEPTIDE         43..64
FT                   /note="Cypemycin"
FT                   /evidence="ECO:0000269|PubMed:7802859"
FT                   /id="PRO_0000408758"
FT   MOD_RES         43
FT                   /note="N,N-dimethylalanine"
FT                   /evidence="ECO:0000269|PubMed:20805503, ECO:0000269|Ref.3"
FT   MOD_RES         44
FT                   /note="(E)-2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000269|Ref.3"
FT   MOD_RES         47
FT                   /note="(E)-2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000269|Ref.3"
FT   MOD_RES         49
FT                   /note="(E)-2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000269|Ref.3"
FT   MOD_RES         55
FT                   /note="L-allo-isoleucine"
FT                   /evidence="ECO:0000269|Ref.3"
FT   MOD_RES         59
FT                   /note="(E)-2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000269|Ref.3"
FT   MOD_RES         60
FT                   /note="L-allo-isoleucine"
FT                   /evidence="ECO:0000269|Ref.3"
FT   CROSSLNK        61..64
FT                   /note="S-(2-aminovinyl)-D-cysteine (Cys-Cys)"
FT                   /evidence="ECO:0000269|Ref.3"
SQ   SEQUENCE   64 AA;  6533 MW;  C62C08E55FD070E4 CRC64;
     MRSEMTLTST NSAEALAAQD FANTVLSAAA PGFHADCETP AMATPATPTV AQFVIQGSTI
     CLVC