CCTQ_TALIS
ID CCTQ_TALIS Reviewed; 252 AA.
AC A0A0U1LSP7;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Probable MFS transporter cctQ {ECO:0000303|PubMed:26954535};
DE AltName: Full=Cyclochlorotine biosynthesis protein Q {ECO:0000303|PubMed:26954535};
GN Name=cctQ {ECO:0000303|PubMed:26954535}; ORFNames=PISL3812_02622;
OS Talaromyces islandicus (Penicillium islandicum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Islandici.
OX NCBI_TaxID=28573;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26535 / WF-38-12;
RX PubMed=26197417; DOI=10.1016/j.jbiotec.2015.07.004;
RA Schafhauser T., Wibberg D., Rueckert C., Winkler A., Flor L., van Pee K.H.,
RA Fewer D.P., Sivonen K., Jahn L., Ludwig-Mueller J., Caradec T., Jacques P.,
RA Huijbers M.M., van Berkel W.J., Weber T., Wohlleben W., Kalinowski J.;
RT "Draft genome sequence of Talaromyces islandicus ('Penicillium islandicum')
RT WF-38-12, a neglected mold with significant biotechnological potential.";
RL J. Biotechnol. 211:101-102(2015).
RN [2]
RP FUNCTION.
RX PubMed=26954535; DOI=10.1111/1462-2920.13294;
RA Schafhauser T., Kirchner N., Kulik A., Huijbers M.M., Flor L., Caradec T.,
RA Fewer D.P., Gross H., Jacques P., Jahn L., Jokela J., Leclere V.,
RA Ludwig-Mueller J., Sivonen K., van Berkel W.J., Weber T., Wohlleben W.,
RA van Pee K.H.;
RT "The cyclochlorotine mycotoxin is produced by the nonribosomal peptide
RT synthetase CctN in Talaromyces islandicus ('Penicillium islandicum').";
RL Environ. Microbiol. 18:3728-3741(2016).
CC -!- FUNCTION: Probable MFS transporter; part of the gene cluster that
CC mediates the biosynthesis of the mycotoxin cyclochlorotine, a
CC hepatotoxic and carcinogenic cyclic chlorinated pentapeptide
CC (PubMed:26954535). With the ABC transporter cctS, is most likely
CC responsible for cyclochlorotine secretion and thereby may contribute to
CC intrinsic resistance (PubMed:26954535). {ECO:0000269|PubMed:26954535}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:26954535}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {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; CVMT01000002; CRG85575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U1LSP7; -.
DR EnsemblFungi; CRG85575; CRG85575; PISL3812_02622.
DR OrthoDB; 1230185at2759; -.
DR Proteomes; UP000054383; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR036259; MFS_trans_sf.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Virulence.
FT CHAIN 1..252
FT /note="Probable MFS transporter cctQ"
FT /id="PRO_0000438671"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 252 AA; 28151 MW; 57B7CB870CCBA88D CRC64;
MGQKETFYRN WNGGGDFLRT VFGLGGLDHT NDSPAEQRYV NSLETSSMMA ENDIGSLMPL
VYTTVAFFVA VVLPHGSPMS NSHSSKKAFA LLNWPRVLTS RNIWSISHGI FAASMFGSFW
VQSAVGTIPL FGIVGFSWAV TCRIPYYLLH DELYRSSTQR NRQGDDLTDS QGLIHGIHNF
SICLAQIVVL LMINTVWILA SDDDGDSFLV WFLLLGGACA LLAMYFTTRL REPENIKYEE
IAMEEGDYGF SE