NPS6_COCH4
ID NPS6_COCH4 Reviewed; 1761 AA.
AC Q5D6D3; N4X0N9;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Nonribosomal peptide synthetase 6 {ECO:0000303|PubMed:15755917};
DE Short=NPRS 6 {ECO:0000303|PubMed:15755917};
DE EC=6.3.2.- {ECO:0000305|PubMed:15755917};
DE AltName: Full=Extracellular siderophore synthetase {ECO:0000303|PubMed:17056706};
GN Name=NPS6 {ECO:0000303|PubMed:15755917}; ORFNames=COCC4DRAFT_154881;
OS Cochliobolus heterostrophus (strain C4 / ATCC 48331 / race T) (Southern
OS corn leaf blight fungus) (Bipolaris maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665024;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, DISRUPTION
RP PHENOTYPE, AND DOMAIN.
RC STRAIN=C4 / ATCC 48331 / race T;
RX PubMed=15755917; DOI=10.1128/ec.4.3.545-555.2005;
RA Lee B.N., Kroken S., Chou D.Y., Robbertse B., Yoder O.C., Turgeon B.G.;
RT "Functional analysis of all nonribosomal peptide synthetases in
RT Cochliobolus heterostrophus reveals a factor, NPS6, involved in virulence
RT and resistance to oxidative stress.";
RL Eukaryot. Cell 4:545-555(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C4 / ATCC 48331 / race T;
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C4 / ATCC 48331 / race T;
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND PATHWAY.
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).
RN [5]
RP FUNCTION.
RX PubMed=17601875; DOI=10.1128/ec.00111-07;
RA Oide S., Krasnoff S.B., Gibson D.M., Turgeon B.G.;
RT "Intracellular siderophores are essential for ascomycete sexual development
RT in heterothallic Cochliobolus heterostrophus and homothallic Gibberella
RT zeae.";
RL Eukaryot. Cell 6:1339-1353(2007).
RN [6]
RP INDUCTION, FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=23980626; DOI=10.1094/mpmi-02-13-0055-r;
RA Zhang N., MohdZainudin N.A., Scher K., Condon B.J., Horwitz B.A.,
RA Turgeon B.G.;
RT "Iron, oxidative stress, and virulence: roles of iron-sensitive
RT transcription factor Sre1 and the redox sensor ChAp1 in the maize pathogen
RT Cochliobolus heterostrophus.";
RL Mol. Plant Microbe Interact. 26:1473-1485(2013).
CC -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster
CC that mediates the biosynthesis of hydroxamate-containing siderophores
CC that play a critical role in virulence (PubMed:15755917,
CC PubMed:17056706, PubMed:23980626). Cochliobolus heterostrophus produces
CC extracellular coprogen-type siderophores including coprogen,
CC neocoprogen I and neocoprogen II, as well as the intracellular
CC siderophore ferricrocin (PubMed:17056706). The role of extracellular
CC siderophores is to supply iron to the fungus during plant infection,
CC and the intracellular ferricrocin is required for intracellular iron
CC distribution and storage with a crucial role in ascus and ascospore
CC development (PubMed:17056706, PubMed:17601875). SIDA2 catalyzes the
CC conversion of L-ornithine to N(5)-hydroxyornithine, the first step in
CC the biosynthesis of all hydroxamate-containing siderophores
CC (PubMed:23980626). The assembly of extracellular coprogen-type
CC siderophores is then performed by the nonribosomal peptide synthetase
CC (NRPS) NPS6 whereas the intracellular siderophore ferricrocin is
CC assembled by NPS2 (PubMed:17056706, PubMed:17601875).
CC {ECO:0000269|PubMed:15755917, ECO:0000269|PubMed:17056706,
CC ECO:0000269|PubMed:17601875, ECO:0000269|PubMed:23980626}.
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:17056706,
CC ECO:0000269|PubMed:23980626}.
CC -!- INDUCTION: Expression is up-regulated under iron depletion
CC (PubMed:15755917, PubMed:17056706). Expression is repressed by the
CC transcription repressor SRE1 under iron replete conditions
CC (PubMed:23980626). {ECO:0000269|PubMed:15755917,
CC ECO:0000269|PubMed:17056706, ECO:0000269|PubMed:23980626}.
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:15755917). {ECO:0000250|UniProtKB:A0A144KPJ6,
CC ECO:0000305|PubMed:15755917}.
CC -!- DISRUPTION PHENOTYPE: Leads to increased sensitivity to oxidative
CC stress and to iron depletion (PubMed:15755917, PubMed:17056706).
CC Reduces the virulence toward maize plantst (PubMed:15755917,
CC PubMed:23980626). Causes a defect in colonization in planta, but not in
CC prepenetration growth or in penetration (PubMed:17056706).
CC {ECO:0000269|PubMed:15755917, ECO:0000269|PubMed:17056706,
CC ECO:0000269|PubMed:23980626}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; AY884191; AAX09988.1; -; Genomic_DNA.
DR EMBL; KB733499; ENH98811.1; -; Genomic_DNA.
DR RefSeq; XP_014072724.1; XM_014217249.1.
DR AlphaFoldDB; Q5D6D3; -.
DR SMR; Q5D6D3; -.
DR EnsemblFungi; ENH98811; ENH98811; COCC4DRAFT_154881.
DR GeneID; 25839302; -.
DR HOGENOM; CLU_000022_60_2_1; -.
DR OrthoDB; 4243at2759; -.
DR PHI-base; PHI:416; -.
DR PHI-base; PHI:4232; -.
DR Proteomes; UP000012338; Unassembled WGS sequence.
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; 2.
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..1761
FT /note="Nonribosomal peptide synthetase 6"
FT /id="PRO_0000444386"
FT DOMAIN 600..675
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:15755917"
FT DOMAIN 1169..1242
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:15755917"
FT DOMAIN 1237..1313
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:15755917"
FT REGION 63..468
FT /note="Adenylation"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:15755917"
FT REGION 712..1135
FT /note="Condensation 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:15755917"
FT REGION 1354..1677
FT /note="Condensation 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:15755917"
FT MOD_RES 636
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1203
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1274
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1761 AA; 194461 MW; EE52B58EA057D881 CRC64;
MARHQAVSQL HFFALILESL FKGADHPLSH FHNVSEDELD ELWSWNTPLQ PELRFCMHEK
VSERAALHPE KIAIDAWDGT LTYGQIEDYS DKLAKLLRLL DDSSNRIIPV LFEKSRWTSV
AVLAIMKSGA CFALLDPAQP EGRLRAVVQQ VNAKIFLSSK AQSTLAARVA PAATIIPISK
SKFNKIFSPY TAEQPNTTLP PVSPDQPLYI QFTSGSTGVP KGCILTHSQY TSGAIPRAAA
VGYYPHSRVL DFASYAFDVC IDSMLCTLAH GATLCTPSDE RRMNDMSGAM RDMQVTFAGM
TPSVARTLEV DILNNLESIA LGGEGVSISD AMSWGQRTRV VNAYGPSEAT VGATINDNVA
AKPYITMGKR KGCALWLSDP ENHNKLVPVG AVGELLIEGP IVGNGYLNNP SKTKEVFIED
PEFLLKGSKS YPGRHGRIYK TGDLVRFDPD GDGEPIFVGR QDQQVKLRGQ RIELAEIEFN
MQKHLPPDTQ LAAEVIKPSG GGEQTLVAFL VEQKKNGMRH LDGNVFGSFT NKFQDALRDM
TKQLFVDLPS YMIPSAYIPL WKMPLLVSCK TDRKRLREIG ASVTRQDLRR FNSAVSEKKE
ATTEMELKLQ SLWAKLLGGD ADFSANDNFF SMGGDSLRAM RLVAAARDEG VVLSVPDIML
NPTLSSMAEK AKPVSAEETS DVPPFSMIAK DWDVDAARQE SARLCGVDVA NVEDVYPCTP
LQEGLIALSA KFQDAYVAQR VATLPAETAV RLKEAFDTAV QGSPILRTRI INVSGRGLFQ
VVLKDGQLVR EYSTEVSEYL RLDRNEPMDL GTALFRYGLV EEPGSDKMNF VITMHHAVYD
GWSMPLVFDR VNRAFNGLHT ERPSSFKHFI KHLISLDPAD AQQYWKERLE GTIPHQFPPL
PQKGYTTQAD SLLEHYVTVP TSAHSKLTLA TIIRGAWALV SSLYMGHPDI VFGETLTGRS
APVPGIEQIE GPMITTVPIR VRLSLDRPIA EYLQKIHAQT VKQIPHEHLG LQNIRRLSKD
ARVACDLRTG LVLHPKEDED WGTVDIRNPA NTFLPANDAE GAREALKFNT YALMLVCTLE
ENGFLVMASF DSNCISKEAM ERVLAVLDRI VHAFLGNPES KLGDVAVLDP VEAQDAEAMR
PRDVMSDSAL GMSPVDGPES MDASLKELSP NEEKLRSILG RILGMKETDI RPSDSFFDLG
GDSIGAMRLV SDARAQGLNL TVAQVFQSSS LSDLAASASN EREDKLAEIL SRILGMAKTD
IKSSDSFFEL GGDSIGAMRL VSDARAQGLN ITVAQVFQSK SLAELASSAE EETPSQPRVD
TDAPFIALGK DANLHSPDRV GLYLENQGWE ITNIYPTRPL QQLAVEGTVD LPRYSLRYEL
IKFATPIDRQ RLEQACQELV ARNEVLRTVF VKDDGLTLGV VLSSLVVPYT ETAVPDGEDA
DAFIQAGIKQ DIEAPKPYGS SFVAFNLFTH TNGASTLVFR ISHAQYDEIC LPILFEQLSA
LYAGTTVPET VPFSKHINHV VLDNIPKAIP YWKNLLSGSE MTVLKPSIPL THRGPADIYK
EFDISRRPAN ITIGSLPTAA WALVLSRRLS RTDVVFGEVV SGRNVGAPNA DRIFGPTWQY
IPFRVAFSKS WSYLDLLRYV QDQHMTSAAY ESMGFSEIVK NCTHWDPESV QWFDTVVHQA
PAWVEEMPFG NGVEAKFQTL YPHAEPLREW KCQAFVKDGG RKLGIEIVTF EEWIGEAEGV
LEEVGKALEC LMEGRAGESI F
