ID   CYPM_STRSQ              Reviewed;         245 AA.
AC   E5KIC0;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=Cypemycin N-terminal methyltransferase;
DE            EC=2.1.1.301;
GN   Name=cypM {ECO:0000312|EMBL:ADR72966.1};
OS   Streptomyces sp.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1931;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
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]
RP   CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX   PubMed=22841713; DOI=10.1016/j.febslet.2012.07.050;
RA   Zhang Q., van der Donk W.A.;
RT   "Catalytic promiscuity of a bacterial alpha-N-methyltransferase.";
RL   FEBS Lett. 586:3391-3397(2012).
CC   -!- FUNCTION: Involved in the biosynthesis of the lanaridin cypemycin. The
CC       enzyme can methylate a variety of oligopeptides, cyclic peptides and
CC       the epsilon-amino group of lysine. {ECO:0000269|PubMed:20805503}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal L-alanyl-[cypemycin] + 2 S-adenosyl-L-methionine =
CC         3 H(+) + N-terminal N,N-dimethyl-L-alanyl-[cypemycin] + 2 S-adenosyl-
CC         L-homocysteine; Xref=Rhea:RHEA:14393, Rhea:RHEA-COMP:9849, Rhea:RHEA-
CC         COMP:9850, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:64718, ChEBI:CHEBI:77037; EC=2.1.1.301;
CC         Evidence={ECO:0000269|PubMed:20805503, ECO:0000269|PubMed:22841713};
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000255}.
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DR   EMBL; HQ148718; ADR72966.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5KIC0; -.
DR   SMR; E5KIC0; -.
DR   KEGG; ag:ADR72966; -.
DR   GO; GO:0008170; F:N-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0030651; P:peptide antibiotic biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..245
FT                   /note="Cypemycin N-terminal methyltransferase"
FT                   /id="PRO_0000408759"
SQ   SEQUENCE   245 AA;  26525 MW;  DC67B1173524A885 CRC64;
     MSDPSVYDET AIEAYDLVSS MLSPGAGLVA WVSSHRPLDG RTVLDLGCGT GVSSFALAEA
     GARVVAVDAS RPSLDMLEKK RLDRDVEAVE GDFRDLTFDS TFDVVTMSRN TFFLAQEQEE
     KIALLRGIAR HLKPGGAAFL DCTDPAEFQR AGGDARSVTY PLGRDRMVTV TQTADRAGQQ
     ILSIFLVQGA TTLTAFHEQA TWATLAEIRL MARIAGLEVT GVDGSYAGEP YTARSREMLV
     VLERQ