ID   NRPS2_ZYMTI             Reviewed;        4476 AA.
AC   F9X9V1;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   23-FEB-2022, entry version 58.
DE   RecName: Full=Nonribosomal peptide synthetase 2 {ECO:0000303|PubMed:28818040};
DE            EC=6.3.2.- {ECO:0000305|PubMed:28818040};
DE   AltName: Full=Ferrichrome A-like siderophore biosynthesis protein NRPS2 {ECO:0000303|PubMed:28818040};
GN   Name=NRPS2 {ECO:0000303|PubMed:28818040}; ORFNames=MYCGRDRAFT_92222;
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS   fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=336722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323;
RX   PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA   Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA   Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA   Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA   Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA   Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA   van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA   Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA   Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA   Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA   Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA   de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA   Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT   reveals dispensome structure, chromosome plasticity, and stealth
RT   pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(2011).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=28818040; DOI=10.1186/s12864-017-3969-y;
RA   Cairns T., Meyer V.;
RT   "In silico prediction and characterization of secondary metabolite
RT   biosynthetic gene clusters in the wheat pathogen Zymoseptoria tritici.";
RL   BMC Genomics 18:631-631(2017).
CC   -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster 14
CC       that mediates the biosynthesis of a ferrichrome A-like siderophore
CC       which may contribute to organismal virulence (Probable). The first step
CC       of siderophore biosynthesis is performed by the HMG-CoA synthase (HMGS)
CC       MYCGRDRAFT_54740 which catalyzes the generation of HMG-CoA and CoA
CC       using acetoacetyl-CoA and acetyl-CoA as substrates (By similarity). The
CC       enoyl-CoA isomerase/hydratase MYCGRDRAFT_76805 then catalyzes the
CC       conversion of HMG-CoA to methylglutaconyl-CoA (By similarity). The
CC       acyltransferase MYCGRDRAFT_85486 then fuses methylglutaconyl-CoA with
CC       hydroxyornithine to yield methylglutaconyl hydroxyornithine (By
CC       similarity). Methylglutaconyl hydroxyornithine is then available for
CC       use by the nonribosomal peptide synthetase NRPS2 to generate the
CC       ferrichrome A-like siderophore (By similarity).
CC       {ECO:0000250|UniProtKB:Q4P3F1, ECO:0000250|UniProtKB:Q4PEM9,
CC       ECO:0000250|UniProtKB:Q4PEN0, ECO:0000250|UniProtKB:Q4PEN1,
CC       ECO:0000305|PubMed:28818040}.
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000305|PubMed:28818040}.
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. NRPS2 has the following
CC       architecture: A-T-C-T-C-A-T-C-T-C-T-C (Probable). The lack of
CC       corresponding A domains in the 3 modules suggests that A domains have
CC       to be used iteratively to incorporate the six amino acids in the
CC       siderophore (By similarity). {ECO:0000250|UniProtKB:Q4PEM9,
CC       ECO:0000305|PubMed:28818040}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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; CM001199; EGP88586.1; -; Genomic_DNA.
DR   RefSeq; XP_003853610.1; XM_003853562.1.
DR   SMR; F9X9V1; -.
DR   STRING; 1047171.Mycgr3P40534; -.
DR   GeneID; 13400882; -.
DR   KEGG; ztr:MYCGRDRAFT_92222; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   InParanoid; F9X9V1; -.
DR   Proteomes; UP000008062; Chromosome 4.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   Gene3D; 1.10.1200.10; -; 4.
DR   Gene3D; 3.30.300.30; -; 3.
DR   Gene3D; 3.30.559.10; -; 5.
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; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF00668; Condensation; 5.
DR   Pfam; PF00550; PP-binding; 5.
DR   SMART; SM00823; PKS_PP; 4.
DR   SUPFAM; SSF47336; SSF47336; 5.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS50075; CARRIER; 5.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 5.
PE   3: Inferred from homology;
KW   Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW   Virulence.
FT   CHAIN           1..4476
FT                   /note="Nonribosomal peptide synthetase 2"
FT                   /id="PRO_0000451093"
FT   DOMAIN          714..790
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1524..1598
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          2724..2800
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          3307..3381
FT                   /note="Carrier 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          3889..3967
FT                   /note="Carrier 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          156..587
FT                   /note="Adenylation 1"
FT   REGION          826..1261
FT                   /note="Condensation 1"
FT   REGION          1645..2106
FT                   /note="Condensation 2"
FT   REGION          2151..2585
FT                   /note="Adenylation 2"
FT   REGION          2867..3232
FT                   /note="Condensation 3"
FT   REGION          3418..3854
FT                   /note="Condensation 4"
FT   REGION          3858..3888
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          4030..4300
FT                   /note="Condensation 5"
FT   COMPBIAS        3858..3878
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         749
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1558
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         2761
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3341
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3928
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   4476 AA;  492986 MW;  78AA1F699D1F86EA CRC64;
     MLLHELLPLN VLTSATCRPN VCSRKNYGCN VTGHLVTRAE YLSPSAGWNA GAESEAVVED
     VERVEDVPSG FLLDLRFVAR IVPTNTGYQI VLDVDGHLIP EAALDTLLEL LCSQISGNDH
     NAAQKSILNY PHHSRPVPFP QEPDIERHPA LLHGCFERRV EQFPDRMAID YLNLDQTRVQ
     YTYREVNAIA ERIAARIASG DQQNEGPVAI VMGPSPEMYI AYIAVLKAGR PFCPIPVDAP
     VERQMVILED LECRIVITRN HDIGLEIFGG NDQTKALSDD VQIVNASDFL DPKLLTEEPE
     IQHSIRTCLS SADEDDLAYI LYTSGTTGKP KGVQISHLSA ACLVAADSAI VPIASSPNAR
     PTRWFQFCAP TFDPSIMEIF VTLSGGGTLC CAERQLTLND IYSVLAQMDV DVMLATPSLA
     TLLDPLQLKG LWAMGEALNV KVTETFAALN PAASSDWSPD DGPRGLYNGY GPTEAAMNCS
     ALLHVLANNR GGIIGSPLPS VSLIVVDEQD PLRPLPYGCA GELLISGPQV SSRGYLNRPE
     ETAKAFLPVT PWGRAYRTGD RARVVWDSAG NPSVEFLGRI SSDQVKLSGR RVELGEIDAA
     VLAVPEVREA LTVIYKPPGS EGKGSEKPLT AVSLVDGAEW DAVKEKIEAT VQKNLLPFMR
     PYRLFMMEQI PRSLAGKLDR RALTTVLHEK INAEQTMQSS EEVADDEPQD PLPPHLAEVE
     GKLLDILSDI LQYRPSPTAS LVSDAGLDSL RGMQLLSRVR AQYLVEDLSL QDLLSGQSVR
     RLLLSKDDRL ASAADDKTKA ILRDFSHRHL NSASRSAGLP AEDIEKVVPA TAGQSGAIAS
     LMRSSQGTRK TYINHSCYHL EPGRVDIDRL IAAIEDVLIA REAYRTTFVP IDDAIAPFAH
     CILTPEAAAK HGLCRVVRRC GSHSEEHWLQ EAENAISIVA NTLYRIQIVD DHLLIISLFH
     GIFDGASLEL LMVDIERQYH GLPKEHRSDI SFAAEHDLKL QSKKTDDFWL QETANFHAET
     IPVLIGSKSQ PWTEQEAETL VVKHTTSLKY KDLETRSREI GASPLAIWQT AWAMLLSSYS
     ERQASDVMLG SVVSNRFDTE SAVCHGPTFT VLPCRVQVPN DPDSITSVGQ AVSQVARAGT
     RALGHAYPSL GLITTPEGKL PYDSLLAFQH FQVEESSKSE RESLWNRISW PAMRHDFGAM
     LEVWPCDQAI PRSQWNTECP MIVKLTFKTD LFAEVTAERI LSQLSSIVMA ILERPQQTAR
     ECLGSIPRAL LSVQNVDAKR VKFDLGNVPS TNPSDNHSTA SNTDNTLACT SRFVVTSEPP
     HRLVPFHGVG ELALNGPRIG EAREHASSTA GRSVWSEDLQ QHIILTGDIV RMVDHGIEML
     GRSDNFVKVN GIGIHLSRIN AAFSDAHEDP EDIETLLMTR PGMENSALVS FASVRNESAD
     APLIAEDKRA WSVRESILIA ARQKLDDYMV PSFVVMLNSI PRTASNDVDR KALEDVFTKL
     DLDRFATSNE FQLSKAQPEF KVRTPTDDRV IGILSEITGV DAASITDNMS LARLGIHSMA
     AIRLAWRLKK EAQISVAVVD LLTCSSVGQL LQIVSSGAAR GARDEEQRKT AEYLDRIEWQ
     LFDKFAEQLN PQAGSSDFTL HCLRPATTMQ EALVIETLRD NRSYWSHRMF RLPPGVDFDR
     LRAAWEAVAR DNEILRTSFM VAAEIAPDAT SWLREADLPT AILQAIVKST EIRWTVAEWS
     SASQSLATVA NDIAQHARNE CSPIASSKLT PPWSVTILQD SSTDEKTMIL HMHHALHDAA
     SMESIFEDLV KQYQDGSQKS ERAQFGEAMR YGIFATREQT ERAQSKVQEL YGPLVEQFGA
     ITTTKCPDLT GSRQPQQRKI LRTTASIRPC DDLKLWSALQ ASVAKYDLKS PAQIISTAFG
     SVLAEYLESK YVVIGETLDQ RIQDTKLQSV IGPLIVTVPI AVRIDLSTAD FFSSLSRETN
     AAMQDLYHMQ PAALRKTLGI SSDQPLYPAL VVFHPRMGDD ETKDDAKNTT SSKFFDEMED
     VVGLSVEHSL ALNIFEGEPG NGYTFELSGD SSVISVPQLE LLLSQVKSQL SAMLSHPNVP
     IIELNNTLPR SVLSVNDATY KAMNEIKKLS RKSQWSGIAP PTVNPVAWIE YHARHHPRWT
     AVEQIADMDD PYAVRRWTYS FLLFKVSRIL EALSKRGIQR GSIVAVHLGR TLESFATIIA
     LFRGGYIYLP LDEELPSERT ATLATDAGAA AFITTQELLT ELKSDLGDSS LVGIDVMLLE
     TLLTNPNPQA DATVSLPKYR SHKHSTDDGY ILFTSGSTGK PKGVRVTNFN LCNFIESLGK
     RILDHSPQTG RLGGIGKYLN IASRSFDPHL THMFMAWRFG LAATIGPRMM MLGNLEQIIN
     ENSITHFGTV PSVLQQAQLT PARVPSVVLV TVGGEKVSNS VLDTWAGDSN GPSAGPLVLN
     AYGPTECTIG CSSNVVDYDS NARNIGWAHD SATAIVFAQE VFGHIGKQVI AKRGQIGELC
     IAGNMVSLGY LSRPEAQAEA FATTTLLRSE DNGKPLRFYR TGDLVRMMAD GSMEFLGRSD
     QQAKVNGQRL ELGEVEHFLQ KTAEAMKLKL EFAAAVIDHP ELPRPRLFTF IAAARDTDDP
     SSKNILELTT IAGSRSLSDE LSEACAKSLP AFMVPELVWV NHIPHLKASG KVDTKTLNLL
     IKSMSLSQLH GDEQEAESND TLQQSLTKDE ETVLLAIEYT LGSKTKHPSA SRSIYELGID
     SISAIQLSAH LKQSGFRLST ADVLSHATIR HLAQKGRTSS PADDHTLLHN AAQRIKQFQK
     DYESEVKSSF GDSGVQVEQI LPTMPLQGAL LARSIAQLQE DEDESFEKIK YVTQFRYSLS
     DSTDLERFVS AVKKVLQKEQ MLRTCFRQIS TGQMAQIVLS RCLGGPFVTF VNSPWATWCQ
     SSSPDMIARQ LVEDIGNLPP VRVHVFDGSS PEILLSIHHA LFDGDAISQL RDRIQEQYQG
     AVKNKSRQDA IQQLLVTFEA VDPDAAIAFW HRNLQDVAPC LVGDHSNASE RQTKNLARSM
     RRLSLPLEKL RSAVQNCSVS LNALFQTVFA VLLSELLPER SDVVFGNVVS LRPLLASTIP
     DIDQVIAPCL NTLPQRIQLS EAGQNQGSLR SLAQSVREIF SETMQHAFVP LDQILKWAQS
     NEALFDAVIS VNMHNHQVGA TGDKTSSQPA FLTLEETMSA TNVPFAADVN IHSFGSYLGY
     VEVELSSSTQ NVQVSELVGR FEEICNIFVE RPETQVFGLL PLLPKTVVAP VSARNDGVHE
     PDDTPWSCTE MIIRDVVCEL LAVPPEKMRK RTSFYRLGLD SILVLRMVKL LHDRIGVKLS
     PLAVLRARCV AGVADAVEKR GSIARYPHKE LQSGRSDDTG DLLRLAKNLG VYPAASRCYL
     ATPMQQGMLS AGLAHFVEAH NQSKPYVYRH TFEIKDRSKF RLEAFHHAWK QSVEQVEILR
     TTFHFTEDDS QPWLGIVRPF ADVFREAQVV QSMEDAVRTA ASIDASTCLA CCTLVVPKDL
     TERITAVFTM HHAIYDGVSL SRLWKIFTKS YHAFINGSDA SLAPLVPFSR AAEQIAAEQA
     PAVAYWSRQL EEYSYAPVMK NHDKGETIQS TRYRAVVSLP SGQHEEVKSR CRDIGSTVNA
     ALMVAWSKVL AKAVLKQSDV VFGQVLDGRL LALDVEGQGL NADSVVGPLL NTVPIRMLLS
     SDCSNQQMLQ RAQHLSEDAQ QHQVASLRVV QNTWRSTTSC AVSSELFQSL LVFNSEGGGK
     AEDSDNCIWR PSRLTSGDGQ DGFTEYPLVC NVSASRTGLD LRVSTAPSHF DALSADRLAS
     NLKTELLEQL TSLDAPSVPA TLPLQKQPSA NAQLSREESR STATDESKEE NVDLCTVVLD
     AFEAVRGRAK MTDTVDAHTN LFRAGLDSIL AIRLSSKLSR TAIPLTVPQI MQSKTVASMV
     ARLRTVQMRK QELQNTGCRS GPNVDARLVS DAEQQEAIRR LGWTESDVES VLPCLAGQEH
     HIESWTFAGH RFFEAPWIFK LKSDLLVSQV RRAWDELRRH HAILRSSFVA VTKSCVGGPK
     AMQVTQKAHC VNTRADGTFS LVESNEASTL DALLVQHLQQ TNDQTSSLLS PPARLTLLRT
     ADGHSAMVMR LHHAMYDAWS IRGILRDFDV LLADGELSGS TDLVEALHAI LAERKPNDEQ
     VFWSQTLKEA QKTILPGDAD ETETPGPLGP QHLVRMPSVV SAAAIRNLER LSQSKASASL
     SPALLLAFAQ TLAEYTGTTS PTFGFYHASR SLGPTDLTNM AVPTMTLTPL SVVVGHRAQY
     RSTAVAGVES IQNHLSKLGQ FGQASVHDIM RSIGHAQPFF NAYINLLYRD TSDLGGDKSA
     PSSRSLATLE RLTPSSNTYF TETRASEQCA PPVRELDTSY IAPERLFVDV VVDRENGGIS
     LGLRCDRSLY GVEQVRTFAR RFVRNLSRLE EVLSGV