ID   VLMC_LECSP              Reviewed;         580 AA.
AC   A0A024F9J0;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=AMP-dependent ligase vlmC {ECO:0000303|PubMed:24848421};
DE            EC=6.3.2.- {ECO:0000305|PubMed:24848421};
DE   AltName: Full=Verlamelin biosynthesis protein C {ECO:0000303|PubMed:24848421};
GN   Name=vlmC {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: AMP-dependent ligase; part of the gene cluster that mediates
CC       the biosynthesis of verlamelin, a lipopeptide that exhibits antifungal
CC       activity against plant pathogenic fungi (PubMed:24848421). Verlamelin
CC       is a cyclic hexadepsipeptide and is bridged by ester bonding between a
CC       5-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 complete loss of verlamelin production
CC       (PubMed:24848421). {ECO:0000269|PubMed:24848421}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AB862315; BAO73255.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024F9J0; -.
DR   SMR; A0A024F9J0; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Virulence.
FT   CHAIN           1..580
FT                   /note="AMP-dependent ligase vlmC"
FT                   /id="PRO_0000438580"
FT   BINDING         264..265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P40871"
FT   BINDING         338
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P40871"
FT   BINDING         464
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P40871"
FT   BINDING         562
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P40871"
FT   BINDING         562
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P40871"
SQ   SEQUENCE   580 AA;  63739 MW;  FA8F5F75E2BCF553 CRC64;
     MIFTQPSFVP ALPSPLPLGE TIGDFCMSER LAKVGNDAVE EQPIPFIDAA IDKSWTTDEI
     NTRVAQLTRA LATEWNIAPG EKWHKQVAVL ASNCVSIFMD TLILTWAIHR LGGGCLMLQP
     TSSVEEMAAH IDHVPPFAMF VTLDLVTLGQ ETIQKSSQSA DLPFYKFSKV YGPPAKNAPD
     TSNVKSLDAL LEKSKDQAPI EKLLLAEGEG SKRVAYYCTT SGTGGFQRIV AITHENIIAS
     ILQAGLFTGI TKEKSEIALV FTPFNHIYGL LTAHTLMWLG HSTVIHRGFN MLEVLMSIPK
     RRITTLYLVP PIINAMSRNA SLLDRFDLSS VSSVIAGGGP LNKEDYAKMQ TVRPNWKLLS
     GWGQTESCAV GSLAYPKDTV AGSSGVVLPG VRLRMRNDDG NLVQGLEEMG EIEMSSPSVL
     YEYIDNATEA LITPHTEEYW RPTGDVGLIR ECPSGIQHLF IVDRIRDMIK VKGHQVAPGE
     IEVHLMKHDA VGETAVVGIA DAVAGERPLA FVIREPSYSP ETSDAELRKI LQDHNDSALP
     EIYRLQNRII IVESIPKSAN GKILKRELRK QVVGWTPPKE