INPE_EMENI
ID INPE_EMENI Reviewed; 215 AA.
AC Q5B7I7; C8V548;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Proteasome subunit beta inpE {ECO:0000303|PubMed:27294372};
DE EC=3.4.25.1 {ECO:0000305|PubMed:27294372};
DE AltName: Full=Fellutamide B biosynthesis cluster protein E {ECO:0000303|PubMed:27294372};
DE AltName: Full=Inp cluster protein E {ECO:0000303|PubMed:20952652};
GN Name=inpE; ORFNames=ANIA_03493;
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.
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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: Proteasome subunit beta type-6; part of the inp gene cluster
CC that mediates the biosynthesis of fellutamide B, a mycotoxin that acts
CC as a proteasome inhibitor (PubMed:20952652, PubMed:27294372). In the
CC first step of fellutabmide B biosynthesis inpC activates 3-
CC hydroxydodecanoic acid to generate 3-hydroxydodecanoyl-AMP that is then
CC loaded onto the T0 domain of inpB (PubMed:27294372). The 3-
CC 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:20952652}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1; Evidence={ECO:0000305|PubMed:27294372};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC Nucleus {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Strongly inhibits growth in fellutamide B-
CC producing conditions (PubMed:27294372). {ECO:0000269|PubMed:27294372}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; BN001302; CBF76042.1; -; Genomic_DNA.
DR RefSeq; XP_661097.1; XM_656005.1.
DR AlphaFoldDB; Q5B7I7; -.
DR SMR; Q5B7I7; -.
DR STRING; 162425.CADANIAP00005264; -.
DR MEROPS; T01.986; -.
DR EnsemblFungi; CBF76042; CBF76042; ANIA_03493.
DR EnsemblFungi; EAA59054; EAA59054; AN3493.2.
DR GeneID; 2872915; -.
DR KEGG; ani:AN3493.2; -.
DR VEuPathDB; FungiDB:AN3493; -.
DR eggNOG; KOG0179; Eukaryota.
DR HOGENOM; CLU_035750_1_0_1; -.
DR InParanoid; Q5B7I7; -.
DR OMA; IDQDGQG; -.
DR OrthoDB; 1092660at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IBA:GO_Central.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0019748; P:secondary metabolic process; IEP:AspGD.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR035202; Proteasome_beta1.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF59; PTHR11599:SF59; 1.
DR Pfam; PF00227; Proteasome; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Nucleus; Protease; Proteasome; Reference proteome;
KW Threonine protease.
FT CHAIN 1..215
FT /note="Proteasome subunit beta inpE"
FT /id="PRO_0000444112"
SQ SEQUENCE 215 AA; 23725 MW; EC90075E6E933C6F CRC64;
MAKETRFYPY TSNGGATLGV SGPDFAILAG DTRSTAGYNI NTRYEPKVFT IQDARDRSIV
ISVIGFAADG RALKERLDAI VAMYKYQHGK NIGLRACAQR VSTMLYEKRF FPYQLQTMVA
GIDADGQGAI YYYDPAGCIE KRSHCAAGEA SSLMLPFLDS QAPRLQPLSL QTAQQLVRDA
YTGATERHIE VGDHLQMLVV TREGVSEQLV DLKKD
