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INPB_EMENI
ID   INPB_EMENI              Reviewed;        2326 AA.
AC   Q5B7I4; C8V545;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Nonribosomal peptide synthase inpB {ECO:0000303|PubMed:20952652};
DE   AltName: Full=Fellutamide B biosynthesis cluster protein B {ECO:0000303|PubMed:27294372};
DE   AltName: Full=Inp cluster protein B {ECO:0000303|PubMed:20952652};
DE   AltName: Full=Interacting NRPS system protein inpA {ECO:0000303|PubMed:18804170};
GN   Name=inpB {ECO:0000303|PubMed:20952652}; ORFNames=ANIA_03496;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [3]
RP   IDENTIFICATION, FUNCTION, AND DOMAIN.
RX   PubMed=18804170; DOI=10.1016/j.fgb.2008.08.008;
RA   von Doehren H.;
RT   "A survey of nonribosomal peptide synthetase (NRPS) genes in Aspergillus
RT   nidulans.";
RL   Fungal Genet. Biol. 46:S45-S52(2009).
RN   [4]
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20952652; DOI=10.1128/aem.00683-10;
RA   Bergmann S., Funk A.N., Scherlach K., Schroeckh V., Shelest E., Horn U.,
RA   Hertweck C., Brakhage A.A.;
RT   "Activation of a silent fungal polyketide biosynthesis pathway through
RT   regulatory cross talk with a cryptic nonribosomal peptide synthetase gene
RT   cluster.";
RL   Appl. Environ. Microbiol. 76:8143-8149(2010).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=27294372; DOI=10.1021/acschembio.6b00213;
RA   Yeh H.H., Ahuja M., Chiang Y.M., Oakley C.E., Moore S., Yoon O.,
RA   Hajovsky H., Bok J.W., Keller N.P., Wang C.C., Oakley B.R.;
RT   "Resistance gene-guided genome mining: serial promoter exchanges in
RT   Aspergillus nidulans reveal the biosynthetic pathway for fellutamide B, a
RT   proteasome inhibitor.";
RL   ACS Chem. Biol. 11:2275-2284(2016).
CC   -!- FUNCTION: Nonribosomal peptide synthase; part of the inp gene cluster
CC       that mediates the biosynthesis of fellutamide B, a mycotoxin that acts
CC       as a proteasome inhibitor (PubMed:18804170, PubMed:20952652,
CC       PubMed:27294372). In the first step of fellutabmide B biosynthesis inpC
CC       activates 3-hydroxydodecanoic acid to generate 3-hydroxydodecanoyl-AMP
CC       that is then loaded onto the T0 domain of inpB (PubMed:27294372). The
CC       3-hydroxydodecanoyl-S-phosphopantetheinyl-T0 is sequentially extended
CC       with L-Asn and L-Gln by the two CAT modules of inpB (PubMed:27294372).
CC       The linear lipodipeptide from inpB is then transferred onto inpA for
CC       the addition of the third amino acid, L-Leu (PubMed:27294372).
CC       Reductive releasing of the lipotripeptide by the TE domain of inpA
CC       produces (2S)-fellutamide B (PubMed:27294372). InpF might be involved
CC       in the release and transfer of the lipodipeptide from inpB to inpA
CC       (PubMed:27294372). The inp cluster-encoded proteasome subunit inpE
CC       confers resistance to internally produced fellutamides
CC       (PubMed:27294372). The MFS efflux transporter inpD may contribute to
CC       fellutamide resistance as well (PubMed:27294372).
CC       {ECO:0000269|PubMed:27294372, ECO:0000305|PubMed:18804170,
CC       ECO:0000305|PubMed:20952652}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:27294372}.
CC   -!- INDUCTION: Expression is positively regulated by the secondary
CC       metabolism cross-pathway regulator scpR (PubMed:20952652).
CC       {ECO:0000269|PubMed:20952652}.
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). InpB has the following architecture:
CC       T0-C-A-T-C-A-T (PubMed:18804170). {ECO:0000250|UniProtKB:A0A144KPJ6,
CC       ECO:0000305|PubMed:18804170}.
CC   -!- DISRUPTION PHENOTYPE: Eliminates the production of fellutamides
CC       (PubMed:27294372). Does not impair the production of asperfuranone
CC       (PubMed:20952652). {ECO:0000269|PubMed:20952652,
CC       ECO:0000269|PubMed:27294372}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR   EMBL; BN001302; CBF76036.1; -; Genomic_DNA.
DR   RefSeq; XP_661100.1; XM_656008.1.
DR   AlphaFoldDB; Q5B7I4; -.
DR   SMR; Q5B7I4; -.
DR   STRING; 162425.CADANIAP00005261; -.
DR   EnsemblFungi; CBF76036; CBF76036; ANIA_03496.
DR   EnsemblFungi; EAA59057; EAA59057; AN3496.2.
DR   GeneID; 2872918; -.
DR   KEGG; ani:AN3496.2; -.
DR   VEuPathDB; FungiDB:AN3496; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   HOGENOM; CLU_000022_60_4_1; -.
DR   InParanoid; Q5B7I4; -.
DR   OMA; LFDFWSH; -.
DR   OrthoDB; 4243at2759; -.
DR   Proteomes; UP000000560; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IBA:GO_Central.
DR   GO; GO:0043041; P:amino acid activation for nonribosomal peptide biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019748; P:secondary metabolic process; IEP:AspGD.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR   Gene3D; 1.10.1200.10; -; 3.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.30.559.10; -; 2.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
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; 2.
DR   Pfam; PF00550; PP-binding; 3.
DR   SMART; SM00823; PKS_PP; 3.
DR   SUPFAM; SSF47336; SSF47336; 3.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 2.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS50075; CARRIER; 3.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   2: Evidence at transcript level;
KW   Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome.
FT   CHAIN           1..2326
FT                   /note="Nonribosomal peptide synthase inpB"
FT                   /id="PRO_0000444109"
FT   DOMAIN          8..84
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:18804170"
FT   DOMAIN          1145..1221
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:18804170"
FT   DOMAIN          2216..2294
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000305|PubMed:18804170"
FT   REGION          87..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..568
FT                   /note="Condensation 1"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:18804170"
FT   REGION          593..997
FT                   /note="Adenylation 1"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:18804170"
FT   REGION          1226..1247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1266..1680
FT                   /note="Condensation 2"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:18804170"
FT   REGION          1702..2097
FT                   /note="Adenylation 2"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:18804170"
FT   COMPBIAS        105..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         45
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1182
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         2253
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2326 AA;  253076 MW;  03AED830E5FDD3AA CRC64;
     MPGAIESSPS EWLQLELRRI CANVLQLDTK DVDPQRSFLS LGGDSLLAIK ILAQCRAQGI
     TINIADIMAA TTLESLYSMA QGPAELASSS TSDNASDKDS SLDDSETGAL TPTTDAGSSL
     ADTLSPEMKA KLSALSVSQD TAIQAVVPCS AIQDRMLVSQ LQNPHLYSCC FVLRLTHSHP
     GLPVDAKRLG TAWGEVVKRH SSLRTVLVES TQRPGHYNQV ILAGIIPAVE HYEGADHLGS
     VKFNVNNPIV FQPHSIPHRL QLVQVSPSEV YLKFDISHLL IDGQSAEVLL KDLSDAYRDG
     GLAAAPLSYA DYVSSYLLEP AQLNTSRKES GMEMSPLTVP MDRPNEGLFD FQTVSANVPL
     DSRLVQSVCA RYSVTLATVC QLAWGLVLRC YAGTDSVCFS YVNSGRSMSI PGVQEVIGPI
     VQTSMCSIQL GPADELPKIL QRIHRDALQA MSQLSPLEAN STSKSARQLS NTTMSFQRAL
     DDAAAQRAGL LVKIEGKANP TDYDISLGIA AGADGLSVDL DFWGSRLDEE SARTMLGAFE
     AAIRGIIDSP DSTVSNISLL SPGEVSQLAQ WNASIPKPER VCVHDKIMEI SKLQPGAAAV
     NSWDGNLTYH DLTVQASTLA HHLRDQLGVG PERFVGICMD KSKWAIVSML AVLMAGGIVV
     PLGVSHPRAR IRELLNDTAA VALLVDGKHG DRLAGLEVEN AAMLTVDQQL LDSLPTIPKP
     PVSGVTPDNA AWVIYTSGST GVPKGVVLLH QNISTSVIAH GAVFGVNCVT RTAQFASYTF
     DVSLSDIVMT LFHGGCVCIF SEESRMNSLT EALQGLAVNY VNLTPTVLGL LNPADLPVIR
     TVVAGGEAMD PGIIEKWSPH ARVFNSVGPS ECTIIAVAAG PVTDPAQAAN VGYPTGTRLW
     VALPTDPNQL CPVGVPGELL IEGPMLSRGY LNDPEKTAGA FITNPAFVKH LEAATPAWKV
     LFQKSERRFY RSGDLVRQKR DGSLVHMGRR DTQVKIRGQR VEIGEIEYWI MQRLKEVRRV
     AVLVIERGQG KEQKSLVAAV EFKEDYEDVR HSDDDISPVT KIGESTVLPQ LLPLTEPLSK
     ALHQLRNDLL EHLPPYMSPT MYAPVSQLPL NLSGKIDRRA VTQFINELDD VQLQQYLAVS
     GSHQEPSTET EFKLQKLWAK TLGVDVSQIS ADSHFFHIGG DSVAAMRVVA AARDVELVLR
     VADLFEYPRL PDLARAVESR VVDEADEEDP APFSVWRESR GSEPSEEPVE LDKIAAMCNL
     SKEQIEDVLP CTALQEGLIA LTAQQPTAYI DRRVFALSQE VDLSQYRAAW QIVIHRTSAL
     RTRIVSGPQT GSLQVVVVPR HIDWNKSSSL DEYLETDRQT GMMMGQPLNR FAFVDQPDGQ
     RFFVWTTHHS TYDGWSRALV LQQVADAYAS RDLPPIASFS RFIQYIHSQP QDAAASYWKA
     QLGGDTSADF PALPIANYRP RPQQRHQHTV NLASSSTKVM LPDLLRGAWA LVVHQYVGKT
     DPVFAIALSG RNAPVRNVPN IAGPTLTTVP VRIFIDPEQL VNEFLQSVRQ QAVDMIPYEH
     TGLQRIKKMV PELAAAVDLK HLFVVQPASD GESKFKIPGV TEHLVAVDEF DSYGLNVECM
     LSGQSIEVDV RFDEKMLSSS QVIRLMSQFE AVVHQLHLHG EGSLKIKDID LLSPEDVNQL
     RQWNALPLAQ PLDVCLHDLI AEVARSRPGA AAIEAWDGTL THAQLQSYAS TLAGYLIELG
     VGPEISVPVC MDKSVWAVVC FLAVLQAGGV VVPLGTGHPI PHIASIIEDT GAKLVLVDAQ
     QFERLLELTP SRGLTLVPID TQLLNSLPTA APQTSVTPAN AAWIVFTSGS TGKAKGVVLT
     HSNLSTAIKT HGARFGLGTH TRTIQFAAHT FDAVLQDYFT TLASGGTVCV PSEADRMNDL
     AGVMRGMNVN FANLTSTVAR LLTPDQVPSL KVLILAGEQI QDSVVETWYK HAEVLNVYGP
     TECSINSTCN GPISDLSNAQ SIGFGMGSRT WIADPTDPNR LCPVGTPGEL LIEGPGLARG
     YLGDPAKTEA AIIQNPSFAS RFALSDCRVY RTGDLAKQTE DGQILYLGRI DTQIKIRGQR
     VELGEIEHWI GRHLPHVKHT AVVAISRGEK QMRLAAVIER ENGHKPDPVI FTQLKKTLSS
     LLPSYMVPSL YIPVTEIPLT VSGKLDRRAI KQTVESMPTE ELEQYFAGES SGTRVPPSTE
     MEKALQRIWA NSLGIEVDAI GADDNFFQLG GDSVVAMHIS ASSRQDQSVK GLAVGDIFMH
     PRLADLAVLL EKRPREGEGG WDEEMRDDES PFALLQEVLD LDLKDI
 
 
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