NPS6_ALTBR
ID NPS6_ALTBR Reviewed; 1460 AA.
AC Q09MP4;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Nonribosomal peptide synthetase 6 {ECO:0000303|PubMed:17056706};
DE Short=NPRS 6 {ECO:0000303|PubMed:17056706};
DE EC=6.3.2.- {ECO:0000305|PubMed:17056706};
DE AltName: Full=Extracellular siderophore synthetase {ECO:0000303|PubMed:17056706};
DE Flags: Fragment;
GN Name=NPS6 {ECO:0000303|PubMed:17056706};
OS Alternaria brassicicola (Dark leaf spot agent).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Brassicicola.
OX NCBI_TaxID=29001;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DOMAIN, DISRUPTION PHENOTYPE,
RP INDUCTION, AND PATHWAY.
RC STRAIN=Tf383;
RX PubMed=17056706; DOI=10.1105/tpc.106.045633;
RA Oide S., Moeder W., Krasnoff S., Gibson D., Haas H., Yoshioka K.,
RA Turgeon B.G.;
RT "NPS6, encoding a nonribosomal peptide synthetase involved in siderophore-
RT mediated iron metabolism, is a conserved virulence determinant of plant
RT pathogenic ascomycetes.";
RL Plant Cell 18:2836-2853(2006).
CC -!- FUNCTION: NRPS involved in extracellular coprogen-type siderophores
CC biosynthesis (PubMed:17056706). The role of extracellular siderophores
CC in fungal virulence to plants is to supply iron to the fungus during
CC plant infection, but not to act as phytotoxins, depriving their hosts
CC of iron (PubMed:17056706). {ECO:0000269|PubMed:17056706}.
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:17056706}.
CC -!- INDUCTION: Expression is up-regulated under iron depletion
CC (PubMed:17056706). {ECO:0000269|PubMed:17056706}.
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 (By similarity). Each module is responsible for the recognition
CC (via the A domain) and incorporation of a single amino acid into the
CC growing peptide product (By similarity). Thus, an NRP synthetase is
CC generally composed of one or more modules and can terminate in a
CC thioesterase domain (TE) that releases the newly synthesized peptide
CC from the enzyme (By similarity). Occasionally, methyltransferase
CC domains (responsible for amino acid methylation) are present within the
CC NRP synthetase (By similarity). NPS6 contains a degenerate A domain
CC (dA) in the second module and has the following architecture: A-T-C-dA-
CC T-T-C (PubMed:17056706). {ECO:0000250|UniProtKB:A0A144KPJ6,
CC ECO:0000305|PubMed:17056706}.
CC -!- DISRUPTION PHENOTYPE: Leads to increased sensitivity to oxidative
CC stress and raduces the virulence toward Arabidopsis thaliana plants
CC (PubMed:17056706). {ECO:0000269|PubMed:17056706}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; DQ860091; ABI51983.1; -; Genomic_DNA.
DR AlphaFoldDB; Q09MP4; -.
DR SMR; Q09MP4; -.
DR PHI-base; PHI:1009; -.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 3.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.559.10; -; 2.
DR Gene3D; 3.40.50.12780; -; 1.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 3.
DR SMART; SM00823; PKS_PP; 3.
DR SUPFAM; SSF47336; SSF47336; 3.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 3.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE 2: Evidence at transcript level;
KW Ligase; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein.
FT CHAIN 1..1460
FT /note="Nonribosomal peptide synthetase 6"
FT /evidence="ECO:0000255"
FT /id="PRO_5004167804"
FT DOMAIN 600..675
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1168..1241
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1236..1312
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 63..468
FT /note="Adenylation"
FT /evidence="ECO:0000255"
FT REGION 712..1135
FT /note="Condensation"
FT /evidence="ECO:0000255"
FT REGION 1303..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 636
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1202
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1273
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT NON_TER 1460
FT /evidence="ECO:0000305"
SQ SEQUENCE 1460 AA; 160190 MW; F3781473AD4A3788 CRC64;
MSHHQAVSQL HLFVSILDAL FSDPDCLLSS FMNVTEDELD ELWSWNSPLQ PELRFCMHEK
VSEQAALHPE KIAIDAWDGT LTYRQVEDYS TDLAQTLQLL DGSHNQIIPV LFEKSRWTSV
AVLAIMKAGA CFALLDPAQP EGRLRAVVQQ VSARLFVSSK AQATLAARVA PAATIIPVSA
SKFDKVYSPC AAQQPKTTLP PVSPDQPLYI QFTSGSTGLP KGCILTHSQY TSGAIPRADA
VGYRSHSRVL DFASYAFDVC IDSMLCTLAH GATLCTPSDE RRMNDMSGAM RDMRVTFAGM
TPSVARTLDV DILDHLDSIA LGGEGVSTSD AMSWGQRTRV VNAYGPSEAT VGATINDNVA
SKPYITMGKR KGCAIWLTDP EDSNKLVPPG AVGELLIEGP IVATDISITR RKPRKFSLKI
PNSWLKGSKS FPGRHGRIYK TGDLVRFDPD GNGEPIFVGR QDQQVKLRGQ RIKLAEIEFN
MQKHLPADTQ LAVEVIKPSG GGEQTLVAFL VEQKKNGMRH LDGNVFGSFT TKFQSALKDM
TKQLAVDLPG YMVPSAYIPL WKMPLLVSCK TDRKRLREIG TSVTRQDLRR FNSVISEKKE
PTTEMEIKLR SLWGKLLGGE DDFSANDNFF SMGGDSLRAM RLVAAAREAG LVLNVPDIML
NPTLSAMATK IKPLSEEATN DVPAFSLIEK DWDMNSAKAE TAKLCGVDVN EVQDVYPCTP
LQEGLMALSA KFQDAYVAQR IATLPSETAQ RLKEAFDTAA EGSPILRTRI VNVSGRGLFQ
VVLKNGRLLR EHGADPAEYL RRDREEAMDL GTALFRYGLV QEAGSDETHF VITMHHAVYD
GWSMPLIFDR INRAFNGLQT ERSVSFKHFI KHLTSLDPAE AQDYWRERLA GVNPYQFPPL
PQKGYTTQAD SLLEHYVSVP TTAHNKLTLA TIIRGAWALV SSLYMGHPDV VFGETLTGRS
APVNGIEEIE GPMITTVPIR VRLSLDRPIS DYLQAVHAQT VKQIPHEHLG LQNIRRLSKD
ARVACDLRTG LVLHPREDDV GEVDMEAVPA NTFLPADDAE AAREALKFNT YALMLVCTLD
ENGFLIMASF DSKCISKDAM ERVLVVMNRI VTAFLGNPES KLGDVAVLDP SEAQDAEAMR
PRDVMSDSGI GTSPIDSPKL DAAMKALSPN EEKLHSILGR ILGMPETEIK SSDSFFELGG
DSIGAMRLVS DARAQGLTLT VAQVFQSQSL AELAASIGNE KEDKLLDILS RILGMPKSEI
NGSDSFFELG GDSIGAMRLV SDARAQGLNL TVAQVFQSQS LSELASSAEE TDSPQTETNS
NAPYAALGKE ASLYSPDRIG AYLQDQSWEI VDVYPTRPLQ QLAVEGTVDL PRYSLRYELI
KFATPINRQK LEQACQELVA RNEVLRTVFV KDESKVLGVV LSSPRVPYSE IAVPDGEDIN
AFSQANIQKD IEAPKPHGSS
