ID   VLMB_LECSP              Reviewed;         231 AA.
AC   A0A024F8Y4;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Verlamelin biosynthesis protein B {ECO:0000303|PubMed:24848421};
GN   Name=vlmB {ECO:0000303|PubMed:24848421};
OS   Lecanicillium sp.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Lecanicillium;
OC   unclassified Lecanicillium.
OX   NCBI_TaxID=1756136;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   PATHWAY.
RC   STRAIN=HF627;
RX   PubMed=24848421; DOI=10.1007/s00253-014-5803-7;
RA   Ishidoh K., Kinoshita H., Nihira T.;
RT   "Identification of a gene cluster responsible for the biosynthesis of
RT   cyclic lipopeptide verlamelin.";
RL   Appl. Microbiol. Biotechnol. 98:7501-7510(2014).
CC   -!- FUNCTION: Part of the gene cluster that mediates the biosynthesis of
CC       verlamelin, a lipopeptide that exhibits antifungal activity against
CC       plant pathogenic fungi (PubMed:24848421). Verlamelin is a cyclic
CC       hexadepsipeptide and is bridged by ester bonding between a 5-
CC       hydroxytetradecanoic acid moiety and a carboxyl group on the terminal
CC       Val of amide-bonded tetradecanoyl-hexapeptide D-allo-Thr-D-Ala-L-Pro-L-
CC       Gln-D-Tyr-L-Val (PubMed:24848421). VlmA and vlmB are altogether
CC       regarded as essential components in the biosynthesis of 5-
CC       hydroxytetradecanoic acid (PubMed:24848421). VlmA catalyzes the
CC       hydroxylation at position C5 of tetradecanoic acid produced in primary
CC       metabolism, while the precise function of vlmB still remains to be
CC       solved (PubMed:24848421). To be loaded onto the waiting NRPS, 5-
CC       hydroxytetradecanoic acid is activated in the form of acyladenylate by
CC       the AMP-dependent ligase vlmC (PubMed:24848421). VlmS seems to accept
CC       the fatty-acyl intermediate onto the initial module to further elongate
CC       amino acid residues by the downstream modules (PubMed:24848421). In
CC       addition, in the last module at its C-terminus, vlmS contains a surplus
CC       condensation (C) domain that may be involved in cyclization, the last
CC       step to form verlamelin (PubMed:24848421).
CC       {ECO:0000269|PubMed:24848421}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:24848421}.
CC   -!- DISRUPTION PHENOTYPE: Leads to highly reduced verlamelin production
CC       (PubMed:24848421). {ECO:0000269|PubMed:24848421}.
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; AB862314; BAO73254.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024F8Y4; -.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   SUPFAM; SSF54637; SSF54637; 1.
PE   4: Predicted;
KW   Virulence.
FT   CHAIN           1..231
FT                   /note="Verlamelin biosynthesis protein B"
FT                   /id="PRO_0000438570"
SQ   SEQUENCE   231 AA;  25440 MW;  F1D939216DB089B7 CRC64;
     MEVKKLEFIG PRVMPGGQKE MDYFCQVPEF QQRCQSGNAV VIPRRDQVAD GRGSTGKLFS
     QTLNTADTIP HCIVMFEDTY TAQSSTQPWL PISTCSVFYQ LGEGVCGFGN ICHGGIQTTL
     LDDVMGVLGV LNARLQDGII PSKVPGAYWP RNNPGMVDLT KSLFATQGIE VKFLRPLRTP
     QVIEVSAQLV DMDVSGGSFT VQCVIRDMKG KQYAVANANW VIHTPRPRSR L