ID   SIDC_ARTBC              Reviewed;        5087 AA.
AC   D4AU56;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Nonribosomal peptide synthase sidC {ECO:0000303|PubMed:26960149};
DE            Short=NPRS sidC {ECO:0000303|PubMed:26960149};
DE            EC=6.3.2.- {ECO:0000305|PubMed:26960149};
DE   AltName: Full=Siderophore peptide synthetase C {ECO:0000303|PubMed:26960149};
GN   Name=sidC {ECO:0000303|PubMed:26960149}; ORFNames=ARB_07686;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=26960149; DOI=10.1371/journal.pone.0150701;
RA   Kroeber A., Scherlach K., Hortschansky P., Shelest E., Staib P.,
RA   Kniemeyer O., Brakhage A.A.;
RT   "HapX mediates iron homeostasis in the pathogenic dermatophyte Arthroderma
RT   benhamiae but is dispensable for virulence.";
RL   PLoS ONE 11:E0150701-E0150701(2016).
CC   -!- FUNCTION: Nonribosomal peptide synthase; part of the siderophore
CC       biosynthetic pathway (PubMed:26960149). Arthroderma benhamiae produces
CC       2 types of extracellular siderophores, ferrichrome C and ferricrocin
CC       (PubMed:26960149). The biosynthesis of these siderophores depends on
CC       the hydroxylation of ornithine to N(5)-hydroxyornithine, catalyzed by
CC       the monooxygenase sidA (PubMed:26960149). The structure of ferricrocin
CC       differs from ferrichrome C only by a serine for alanine substitution
CC       and the assembly of both siderophores is suggested to be performed by
CC       the nonribosomal peptide synthase (NRPS) sidC (PubMed:26960149).
CC       {ECO:0000269|PubMed:26960149}.
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000305|PubMed:26960149}.
CC   -!- INDUCTION: Expression is under the control of the iron acquisition
CC       regulator hapX (PubMed:26960149). {ECO:0000269|PubMed:26960149}.
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). SidC has the following architecture: A-
CC       T-C-A-T-C-T-C-A-T-C-T-C-T-C. {ECO:0000250|UniProtKB:A0A144KPJ6,
CC       ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR   EMBL; ABSU01000010; EFE33326.1; -; Genomic_DNA.
DR   RefSeq; XP_003013966.1; XM_003013920.1.
DR   SMR; D4AU56; -.
DR   STRING; 663331.D4AU56; -.
DR   EnsemblFungi; EFE33326; EFE33326; ARB_07686.
DR   GeneID; 9521384; -.
DR   KEGG; abe:ARB_07686; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   HOGENOM; CLU_000092_2_0_1; -.
DR   OMA; QACSQAF; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
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; -; 6.
DR   Gene3D; 3.30.300.30; -; 3.
DR   Gene3D; 3.30.559.10; -; 6.
DR   Gene3D; 3.40.50.12780; -; 3.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR025110; AMP-bd_C.
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; 3.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 6.
DR   Pfam; PF00550; PP-binding; 6.
DR   SMART; SM00823; PKS_PP; 5.
DR   SUPFAM; SSF47336; SSF47336; 6.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 2.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 6.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 5.
PE   2: Evidence at transcript level;
KW   Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..5087
FT                   /note="Nonribosomal peptide synthase sidC"
FT                   /id="PRO_0000444379"
FT   DOMAIN          671..744
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1740..1817
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          2302..2378
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          3387..3464
FT                   /note="Carrier 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          3943..4019
FT                   /note="Carrier 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          4496..4569
FT                   /note="Carrier 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          165..563
FT                   /note="Adenylation 1"
FT                   /evidence="ECO:0000255"
FT   REGION          782..1112
FT                   /note="Condensation 1"
FT                   /evidence="ECO:0000255"
FT   REGION          1217..1611
FT                   /note="Adenylation 2"
FT                   /evidence="ECO:0000255"
FT   REGION          1855..2272
FT                   /note="Condensation 2"
FT                   /evidence="ECO:0000255"
FT   REGION          2419..2831
FT                   /note="Condensation 3"
FT                   /evidence="ECO:0000255"
FT   REGION          2860..3258
FT                   /note="Adenylation 3"
FT                   /evidence="ECO:0000255"
FT   REGION          3506..3910
FT                   /note="Condensation 4"
FT                   /evidence="ECO:0000255"
FT   REGION          4051..4416
FT                   /note="Condensation 5"
FT                   /evidence="ECO:0000255"
FT   REGION          4610..4913
FT                   /note="Condensation 6"
FT                   /evidence="ECO:0000255"
FT   REGION          5013..5048
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        5019..5048
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         705
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1777
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         2339
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3424
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3980
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         4530
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   5087 AA;  564032 MW;  8B065B8C2B4C9ABD CRC64;
     MDSFLCDRYT QFPSLNYGAE DVPSQASATW ELDNVTDLNR LILAWASILS RLSEEESPVI
     QIDGAAARIH LESGRIESVQ IEKSGNSGSR TAILTSDTPI TSERCQLEIR YTPHQLHGSI
     TSRGCTSVRY LDQLARNLES LLREPLPLSI VNPTPLILPG PRLFHEMVRH TGNEPAISFL
     NESGEVEDLS YEMLHSLSEQ LASHLVHILA SLPPPGQHGK IIPVLLPQSL DLYVAWLAIL
     KAGAAVCPLN LDTPSERLNF IVGDVDARVV VTNEGLTSAF QNIETSITIV KMEEIKTFAP
     GCLSSVDVCN EDLAYVMYTS GSTGLPKGVG ISHQAAVQAL LAHDEIIPGF RRFLQFAAPT
     FDVSVFEIFF PLFRGVTLVG CNRRLMLNDL PGIINQLNID AAELTPTVCG ELLQSRDAVP
     CLKLLLTIGE MLTRHVVDEF GSSKDRPGLL HGMYGPTEAT IHCTAVSSVR AGSLVGNIGT
     PFKTVSAFII SMDHIVGQEP VILPVGHVGE LVVGGPQLAR YYLNRPTENR NAFIDSKTYG
     RLYRTGDKAR LHPNGELQCM GRISTGQVKL RGQRIELGEI ENVLLKNQYV RNVAACVIQG
     ALVAFLSADV AHCTSRDLQL TCRRSLPKFM IPGNFVILNK LPRLPSGKID RKGLEAEYIL
     SKGVDQTDLA EPAGDIEQKI SVSLNLLLES SLTPTASLAS AGLDSLRAIH LASSLRKEGV
     FLNALDILEA DSIRKMAALV LKSQPEVTVI PTESEPLKMW NTIIQQGHEM LKLTENLQQP
     TDIIPCSPIQ TGMLLETKLN PKAYFNSVEL QFDRGISLED VKSAFLSTAL QNEVLRSGFI
     EIDFPGFPYA QVVWESLHPD QIIESKIFDH NLELQNQWDI LHPLRVQLCV IDGQPKALVH
     IHHSLYDGWS WDQIMRDLVS ALENKQLTQR PQYRLFTLFH INNHSSEIRE QALNYWRSHL
     QGSTPCLWPN FQDRSDLPKV TQVVERQFNV DIDQLDSFVR DFRISRQTIF QAAIGYLLSA
     YNGTSDIILG NVSAGRTLPI DGIESIVGPC ISTLPLRLNL QKARTVRDLL AILHGLNRKS
     LVHGFVPLRD VKQVSGINTA DQLFDTLFVW QDNFTTVCGP IAQVTSRDFL EFTLTTELGI
     QDGKIWAKAT FEESILPESH VVIFLKQIES IAMTFLESAD RLLEDIPFHL PESLLSMENN
     FPPPLKSVPG LSDSVEELAK TDSERIAVEF LDSLDPETGD RAIKTLTYSE LDAQSNKLAG
     QLRNLGVVEG NLVAICLEKS LELYISILAV IKAGAGYVPI TPQTPIMRMK HIIQQASCRI
     CIADSEIQAE LSDVPNTTAM LAKPQILVEN ALYEFPKAPG SCPAYAVFTS GTTGTPKGVL
     ISRFNLESNI AVLSALYPDF PESRLLQACS HAFDVSVFEI FFAWSRGMTL CSAKNDVLFR
     DIELAIRKMR ITHLSMTPTV AALVRANNVP LVKFLVTAGE ALTPKVRMDW AGKGLWQGYG
     PSETTNICTV KPNICMSHFI SNIGRPLPNT SVFVLAEGER FSLVPRGAVG ELCFGGDQVG
     IGYLNMEDLT RQKFLIHEAY GRIYKSGDYG RLLPDGSIAF VGRRDDLVKI RGQRIELGEI
     TSVLMTHENV KDCATIVCDS NNGDSGDSKQ LISFWVPDNI NIDGLGQHEN SHIFQQLFDY
     IGDHLPSYMI PSFLIPISHI PMTTIGRKID KEALKYMYLS ANPTLLDVYS RGKEEEHTQE
     NLTDNEAKVA GLVAQVTGVS TKEIGRHTSF YRLGFDSVIA IALSRELKLA GFGQIDISVI
     MKNDSIARLT RKISQSIEAQ MPSLESIPTF DHLFSRELIR KIKDEASSHG VNVTKILPCT
     SLQEGMLSGI STGNDASYYN HLVFEINRNI ELLKTAWMKM VARHDILRTW FRQTDDARFP
     FVQVVLERLD IAWQSIECPI ADAPSTLEKS KLAVAVKEGP HSLYSFTVLQ CVDSPKVFLL
     LSIHHALYDG EAMEVLLQEV QECLLEHQLP PVVPFDLYLH EMIKVNSDST DQFWSNYLKD
     FTPTLFTSPS SLVKGSPKMS RSTSHIPSSS FTEVCNACKS SSVTTLSLLQ AAWSRLICLL
     SGSPDICFGD VVNCRSIPID GAQRIVGPCF NTLPVRTSLN GNMTNIDLMR NLQSNRAATL
     PYQLSSMRRI QSRFSQRGQR IFDSLLLLQG RPLQLNESLW RMVSENGVMD FPIIFEIIPH
     PESDSLQFIF HFDEGLVPTT DIDTITACYH AILNHTLRFP EARVMDFSLV ESDGQVSGGL
     SVFRKLGEAN GDHKSNGYGK SEEWSAESLE IRNLLSAMSK IDKKRINMDT TIFELGLDSI
     NAIQIAGHFR KVGYEISAAD ILEGPSIREI ASVLQGSKSS PCVGLALHNF DFDSFQSLHL
     PSICDKLGLL ESSVEAIRPC TTPQAGMLAS FINSEGLLYF NSFTLKSPTP LNLIALRFVW
     ESVMERNEML RTGFCEVKDD IFPFAMVTYR PGIIELPWNE CLSPSKRMSD ARHEQHLNGK
     SILNQLHRPP WFLTVKPCSD STLMQLSAHH ALYDAHSMNL ILSEVINVYN GSTLPPAIPV
     SSVLGFIVEK FQSPESESYW SEVGPSFSAT KFPDMNPLHA KVNDTRFLSR DCSFTMEKLQ
     KGCRELGVTL QAVGQAAWSR ILSSYVGESN VTYGLVLSGR DISEQAQDTA FPCLTTVPAH
     QNVEATNREL LQQIMKSNAM AVKYQFTSLT KIQRLSKADS PLFDTLFVFQ KLASTDKQQP
     LWDVVEESSQ TEYSVSLELI PSSDTLKLAL TYQNHILPDG QASLLLDELD WLLTHILQYP
     DSTSSSLDTA SRSIVSVLPR KDSKIDCPTQ LLHEFVEVGA TRHPSRVALE FAERINGKLI
     TQSWTYKDLD EQGNRYANLL HHLGVKQGTL VGVSFQKCPE AYFSILGVLK VGCAFLAIDP
     SAPIARKQFI LDDSKADILM CGMEQQDELK SLTGIRLVPV NEEGLLDGVN STPPTLSFPL
     HGDATCYCLY TSGSTGTPKG CEITHDNAVQ AMLSFQRLFG GHWDESSRWF QFASFHFDVS
     VLEQYWTWSV GICLTSCPRD TLFEDFAGTL RDLSITHIDL TPSLAQLIQP EDVPSLCRGV
     FITGGEKLKQ EILEQWGPHE VIYNGYGPTE VTIGCTMLPR VTSSDKPTNI GPQFDNVSGY
     VFKQGTNTPV LRGGIGELCV SGPLVGKGYL NRPQLTAEKF QYIETYGERV YRTGDLVRMM
     HDESFCFLGR IDDQVKLRGQ RLEINEINHV IKNSTEEVGD VVTMVLKHPT ATKEQIVSFT
     TVVTSASTAA CPEVDFSPEA GRVLEAIRSE CRSHLPGYMI PTHIIPLTRF PLSSNNKIDN
     GQLRGIFASM LLSEMQALSS HEQESPTEDT DTIRKIIPIL SRFTKVEEKT ISSSSNIFEL
     GLDSILVISF SRALREAGCP AAHPSVVMKC STLSLLAKAV ESPDNNVEGE RRQYEDAKQK
     IAAFAHMHMS HLANELEVAP QDIEAITPCT SLQDGMLYQC LRNESHPYLT SFTFQLAPHT
     DIPMLKEAWK RAQVSFQLLR TKFPLTDDGY ALVVLKEAAL PWFEFAISKD DELESTAESY
     FKEWNLGFNN FMGRVWEIGI ISSPKRRWMC LNIFHGLYDG ISLPIILDAV KHVYNGGQMP
     RSMPFTEVLP LGPLRTVPAA KSFWAKHLEN LSQTTIPRRS LPEPGSRTST IRIEGFHCIE
     ETRRSLNVTE KAMFHACWVY TFERYFNYIP TMGIVVSGRS FDSEDADVAV GPLFNTIPCN
     IPKFSFSTFS ELIQACHDYS VSALPFQHTP LRSIMKWIGR SSQRPLFDVL FVFQKQENIT
     SQSGESLWEP VASFTEADYP LALEVQSQGS GSFQVTAACQ GDILTSDGIS DLLEQFRLSL
     RSLVEEPFSN LSFSGNSTSL EASSKQIANK VIGGPSPNVT TSFQWSQAAS LLRQEIAKLA
     NLDVSEINED SSVLEVGLDS IDAIKLSSRL KRDHIDLSVG NIMRNRTIRT MMAEVTVNGS
     ATKADLTYLK SLESQLRRSL EEDGKDLGDI EHIYPATPLQ EGMINEMLSS DGLHYFNHDI
     LQISEDVDVT MLKNAWETIA KRHPILRTSF ATVSDPNLPF SYAQLIHKSS IKIDWDIVDI
     AENSIESILQ EERARALSLV MSKPLFNLRL IRDGAKLLLI LSLPHAMYDG WSLTLLHQDV
     ASAYSGQFSA RPSYQHVLED IISSSRDEGL QFWKGVLSDA EPSIFPPQPG AGDQGALVHR
     DETASDIPLS HVLNFCKAHG VTAQALGLTC WTIVLASYLG QLDVLFGTVM LGRDTEEASK
     VAFPTMNTVA VRGILHGSVS EMLEYVQRNL GNMLAHQHYP LRKIKSMMGV GNKDLFDTLF
     IYQKSPSSQE GQDKPLYKSI NSSSSVEYSI CVELEAIDDS AVWRVACKDT ILGKKDTSQL
     VLQLLQVFKT IIQSPEIPTA GFVEVRERPT LDSVTQNGGS LPDGPGGIAI EPVVWSLLEE
     RIRDTLSLVA AVPKEEITRN TTIFHFGIDS ISAIKVSSLL RRQSVLISVR DILRAETVGK
     MAEIVNSARE KKPTTATSRE KLLSLQTLKN SNIDLQLRKY GMKREDVEVF LPATAGQVYM
     LETWKNSHGK LFFPDFFYRV TGRITQSQLD NAWKVMTAKL PILRTTILSI GDTGMPYVLA
     ELKQVSNPII WRSDLRVKSN RRHVAARQGS GLVYLYASQT ETETLLMLHI HHALYDAVAL
     QHLINILESL FQDVSTPVNT PVDIAEFIQY GKAMSSEAQQ EAFWKGYLGN DITPVAKKGS
     GPVMDVQAGA GKYQPGLLDN TDWLNKICQA EGLSVQAVFL AAYSKVHVRE FHVRGADLTV
     GVYLANRSHD LVGLPELVAP TLNIVPLRIQ DPGSRSVFEL ARIIQSDLHE IGSAENCTVS
     LAQIAEWTGI RLDTTVNFIK LPEVAAQVST ATSGAPQLVQ VTEEEVLEWL SKESCNSNGS
     EQVDAAAKGS SSKLWLEEML GIESGVGLEN AGDVYKVSPP GSQLSQDSPE KQEANNKPSP
     QPSVDIEAAV RNNTLDVGVF GPSSDKALGV LDGVRRELLA LQTSSAR