VERP_CLORO
ID VERP_CLORO Reviewed; 1983 AA.
AC A0A1U9YHZ2;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=Nonribosomal peptide synthetase verP {ECO:0000250|UniProtKB:Q4WMJ7};
DE Short=NRPS verP {ECO:0000250|UniProtKB:Q4WMJ7};
DE EC=6.3.2.- {ECO:0000250|UniProtKB:Q4WMJ7};
DE AltName: Full=Verticillin biosynthesis cluster protein P {ECO:0000303|PubMed:28376389};
GN Name=verP {ECO:0000303|PubMed:28376389};
OS Clonostachys rogersoniana.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Bionectriaceae; Clonostachys.
OX NCBI_TaxID=122658;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=XZC04-CC-302;
RX PubMed=28376389; DOI=10.1016/j.fgb.2017.03.007;
RA Wang Y., Hu P., Pan Y., Zhu Y., Liu X., Che Y., Liu G.;
RT "Identification and characterization of the verticillin biosynthetic gene
RT cluster in Clonostachys rogersoniana.";
RL Fungal Genet. Biol. 103:25-33(2017).
RN [2]
RP INDUCTION.
RX PubMed=29058652; DOI=10.1099/mic.0.000557;
RA Guo Z., Hao T., Wang Y., Pan Y., Ren F., Liu X., Che Y., Liu G.;
RT "VerZ, a Zn(II)2Cys6 DNA-binding protein, regulates the biosynthesis of
RT verticillin in Clonostachys rogersoniana.";
RL Microbiology 163:1654-1663(2017).
CC -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster
CC that mediates the biosynthesis of 11'-deoxyverticillin A, one of the
CC dimeric epipolythiodioxopiperazines (ETPs) from the verticillin family
CC that act as mycotoxins (PubMed:28376389). 11'-deoxyverticillin A is
CC required for normal conidiation (PubMed:28376389). The nonribosomal
CC peptide synthetase verP is speculated to be responsible for
CC condensation of amino acids to form the carbon skeleton of verticillin,
CC whereas the cluster-specific tailoring enzymes are involved in further
CC modifications leading to the production of 11'-deoxyverticillin A
CC (Probable). {ECO:0000269|PubMed:28376389, ECO:0000305|PubMed:28376389}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:28376389}.
CC -!- INDUCTION: Expression is regulated by the cluster-specific regulator
CC verZ. {ECO:0000269|PubMed:29058652}.
CC -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC (C) domains) which when grouped together are referred to as a single
CC module. Each module is responsible for the recognition (via the A
CC domain) and incorporation of a single amino acid into the growing
CC peptide product. Thus, an NRP synthetase is generally composed of one
CC or more modules and can terminate in a thioesterase domain (TE) that
CC releases the newly synthesized peptide from the enzyme. Occasionally,
CC epimerase (E) domains (responsible for L- to D-amino acid conversion)
CC are present within the NRP synthetase. VerP has the following
CC architecture: A-T-C-A-T-C. {ECO:0000250|UniProtKB:Q4WMJ7}.
CC -!- DISRUPTION PHENOTYPE: Completely abolishes the 11'-deoxyverticillin A
CC production and conidiation. {ECO:0000269|PubMed:28376389}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; KY359203; AQZ42163.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9YHZ2; -.
DR SMR; A0A1U9YHZ2; -.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.40.50.12780; -; 2.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 2: Evidence at transcript level;
KW Ligase; Phosphopantetheine; Phosphoprotein; Repeat.
FT CHAIN 1..1983
FT /note="Nonribosomal peptide synthetase verP"
FT /id="PRO_0000450169"
FT DOMAIN 526..602
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1584..1662
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 11..405
FT /note="Adenylation 1"
FT /evidence="ECO:0000255"
FT REGION 769..1047
FT /note="Condensation 1"
FT /evidence="ECO:0000255"
FT REGION 1089..1469
FT /note="Adenylation 2"
FT /evidence="ECO:0000255"
FT REGION 1652..1976
FT /note="Condensation 2"
FT /evidence="ECO:0000255"
FT MOD_RES 563
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1622
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1983 AA; 218369 MW; 28D564FA66F6D693 CRC64;
MTLPTSLCDL FAQAASRCPD NLAVDHTEGS LTYRQLDDVS NSLANMLMGL GVNQLSPVIL
LTSHGTFNII ATLAILKVGS CCVPIDRATW PQERINYVCQ TVANSVILNT TSEPFMPSEG
AGDVLNYTSM QSGPSFRPNP VFQAHKVAAD DTAYIIFTSG STGKPKGVLI SHKSLCLYST
TSPINLDIGP GDRLLHILSV AFDACACMLF SALGNCGTIV PAQAEDVLLQ APSCTVLAAT
PAMLKNLPSP TTENSIFSNL SRVILGGETA SPDLLGLWID AGVQVLIAYG VTETTSMGSI
YRVERDPRTD AINPYIIGGV LEQSPIWIVD SELRIIKNEN SEGEIIVGGD GVAQGYYNDE
QKTRSNFIHW NGSRIYRTGD FGCWVLDANG RRVIEFRGRK DRTVKNQGYL VNLDRDVEAA
LYRVGESFGL TSVRAVATGN GIVAVVTPSN VNTSALIEKA KDIMCSYCIP YRIGAVDDLP
LSPNGKVQHN ELAELIKIID EGQHNQENKA DSQLSEKIER GKFGDDRHLD TLLTVARDVL
SLPGQSFRIL QPHDSFFAVG GSSLLAFKLV SVLGQHGLNI PARELFKNQP FSDVAPLITS
RAHSSTWRLT EHDDKTQQTL AELQNQACQM LGLVQNSFEI GPLTSLQLDL ALPTLGDESR
NINQVKIAYN APHSGIMRRA WQGLWQSEPV FRTEVSLAVG CGALIVHNKP FRKYRVVSHS
CRDKYEEAVK GINMGVGLGC TLDVLTYHKT SDGLPYLPVS SNHNSSSSET DELTVVLTIH
HSLMDGESLK LLLDKVDRIA LGFSQPLSGS SINANLALIK TQNSRDSEVR SFFSDYLRHL
SPENIAPGQV SATENLEGSS SRETAFFETS VSSVEVSDFA KLNCSSAACI YYIAWAMAVA
AFDNSPDVLI GAVVSNRPAL QHHEHAIGAY MSTLPLVFNF RDDEETVVDR IQKTMEDLAT
VGEYAWARSD QCGIGRRMRT LLSMQFPLPN ESSKPPALWT ESAENSDFPL CLLVESSGDF
RMLYDATQFN WEAAQRLGQH FKHALYSLHH ETRVTDCMTV NRLQENLAKQ SEIFRLKPSE
RIVKQVLEQV MGQFPSLIAV EDCLGGKLTY SELDKLTNVI AHHINSTVPN AEVIALYSDG
TIQWILGLLG TVKAGCTYVN LDPRSSVSRR ETICKQCGAE ALLLPNASQA SEAPLMDNLK
VLAVDEMLSG NSKKHNGKQP DRASLDSSLV IVFTSGTTGN PKGILISNRS FLSMETSYGT
TMFAAPGRRI AQFMSPVFDV CNMEIFSALL HGATLVLRDP SDPYANLHRV NTAAVTPSAM
AVIDLDDFPN LQLIYACGEP VTKSLVKRYT KRALLYNAYG PAECSILTSI ERLIPGDQVT
VGRPLSTVRV YILDEDQHPM APGDRGEVCV AGVQVLRDYI NAPEQAARNI LTDPWYPGER
MYRSGDSGSI GRDGRLSLHG RIDRLVKLRG FRVELAGVEH AVVSGPTEEG VSQCAAIAVN
GLLIVYVSFE RSQQHDSLSN KERIAQLLSR LREQLLPSSV PQEIVHIDNF PRTINGKIDT
RALETQYSSY KNTSIEKAVG DCPITRPKIE DKLAHEWRQV LQLIPETQLQ ESDDFFKLGG
HSVSIMLLAT RLTAAFGKKI TVRELLPSPT FKDQINMVRA LLEIETFHKE EPQMLPPLLT
EELTSIEKQV WFQHQVATTV TAFNIIRVIQ IEGAVEIDKL CQSLNNILSI DPIFRSNIVE
GPKGPARILR NSAPTVQEVD EFDIERALHH RFNLAHDYLI QVYLARHGCK GDNNDHATLV
ILTSHVIADL GTLQNFLQLT STAYSGSTLV PLDRPKHLDS KSWTRIPTFS ERKFWSEYLK
GLIRRLGLTH HQLALAVGAL FLQWFSAEDD LVLGAPNSGR PTSQEQESLG QFLDRLPIRI
TPNDLGNDDT MTKLTEILNR VRHSSLKALS NAISFSNIIQ DLGYPSGGLE HPLFECDCFY
TVS
