ID   LANSB_STRLI             Reviewed;          42 AA.
AC   Q7BQR2;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Lanthionine-containing peptide SapB;
DE   AltName: Full=Morphogen SapB;
DE   AltName: Full=Rapid aerial mycelium protein S;
DE   AltName: Full=Spore-associated protein B;
DE   Flags: Precursor;
GN   Name=ramS;
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=66 / 1326;
RX   PubMed=11075933;
RA   Keijser B.J., van Wezel G.P., Canters G.W., Kieser T., Vijgenboom E.;
RT   "The ram-dependence of Streptomyces lividans differentiation is bypassed by
RT   copper.";
RL   J. Mol. Microbiol. Biotechnol. 2:565-574(2000).
CC   -!- FUNCTION: Lanthionine-containing peptide devoid of antibiotic
CC       properties, involved in the formation of aerial mycelium. Suggested to
CC       self-assemble at air-water interfaces, thus providing a film of
CC       surfactant through which nascent aerial hyphae can emerge. The aerial
CC       hyphae differentiate further into spores (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Maturation involves the enzymatic conversion of Ser into
CC       dehydrated AA and the formation of thioether bonds with cysteine. This
CC       is followed by membrane translocation and cleavage of the modified
CC       precursor.
CC   -!- SIMILARITY: Belongs to the lanthionine-containing morphogen protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF139177; AAD33774.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7BQR2; -.
DR   InterPro; IPR045825; RamS.
DR   Pfam; PF19402; RamS; 1.
PE   3: Inferred from homology;
KW   Signal; Thioether bond.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   PEPTIDE         22..42
FT                   /note="Lanthionine-containing peptide SapB"
FT                   /id="PRO_0000342632"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         27
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         37
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        24..31
FT                   /note="Lanthionine (Ser-Cys)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        34..41
FT                   /note="Lanthionine (Ser-Cys)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   42 AA;  4496 MW;  F4EEB70DD9DC020A CRC64;
     MNLFDLQSME TPKEEAMGDV ETGSRASLLL CGDSSLSITT CN