ID   CCTS_TALIS              Reviewed;        1553 AA.
AC   A0A0U1LQE1;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=ABC transporter cctS {ECO:0000303|PubMed:26954535};
DE   AltName: Full=Cyclochlorotine biosynthesis protein S {ECO:0000303|PubMed:26954535};
GN   Name=cctS {ECO:0000303|PubMed:26954535}; ORFNames=PISL3812_02624;
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: ABC transporter; part of the gene cluster that mediates the
CC       biosynthesis of the mycotoxin cyclochlorotine, a hepatotoxic and
CC       carcinogenic cyclic chlorinated pentapeptide (PubMed:26954535). With
CC       the MFS transporter cctQ, is most likely responsible for
CC       cyclochlorotine secretion and thereby may contribute to intrinsic
CC       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 ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; CVMT01000002; CRG85577.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U1LQE1; -.
DR   SMR; A0A0U1LQE1; -.
DR   EnsemblFungi; CRG85577; CRG85577; PISL3812_02624.
DR   OMA; ATHHTHL; -.
DR   OrthoDB; 138195at2759; -.
DR   Proteomes; UP000054383; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1560.10; -; 2.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF90123; SSF90123; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW   Virulence.
FT   CHAIN           1..1553
FT                   /note="ABC transporter cctS"
FT                   /id="PRO_0000438672"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        413..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        438..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        527..547
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        550..570
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        948..970
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        1017..1037
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        1086..1108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        1113..1135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        1204..1224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        1229..1249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          293..582
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          635..874
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          951..1255
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1294..1533
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         670..677
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1328..1335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        524
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        617
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        725
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        992
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1085
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1553 AA;  173835 MW;  40A14F38104B47DF CRC64;
     MNFRCSSPLW YDDHLSDCVV NHYLSTLIPL TACLASAIAC LISYFHARQN AKHIDTGFHP
     VASSEDEAVD QIAHVSQQYI TAIPPVIEKL EVALILAEIS IAIFLLIFSG ENTDLTSVFA
     SAVSSIYLLL ILFVRLTRSL QSYVDLQPHS SVLYTLQWTC LTAIVHAAIL GNSERNFTIA
     TLVRFALFTF LCLFHWTAPR IPVEPYDEDH VLFLDPSEDE TASLLSRMTF SWLDKLVWKA
     YRATLQVSDL YQLNHNHRSG VVAPRFKNTA TNSLLWRLFG FFKSDLLWQG AWATLNSFAV
     FVPPVLMRSL LEYLEVPDLA SQSTAWLYVT GLLVAGIVAG VAGCQCDWKG REMAARTRAV
     LINEIYTKVL RKGVALHLQT NSEQPEAADN FASDGNIFNL LTVDTEHVSE MSGYLYLVWI
     TFPVQTAIGT YLLYRLLGIS GIVGVALMLG LLPLNILISR RLVAVQARVL TASDARIQAS
     SEILNNVRTI KYSAWEAVFK KRVLSKRRIE LVEMRSRFIW WSINMTTFFS LPLIVTILTL
     FFYTVVWDNS MGTAVAFPAL VIFSILRIPF NRIADAITFL LRAHVSLGRI EKFLQEQETG
     KYEQLSRTDS VEVGFNNATL TWPNGGFGNK AVTENKRSDI QLTELPSMRP FKLKGLNIRF
     QPGALNVICG PSGSGKSSLL LALLGEMALV NGQVFLPHKH NWHELSTDSL TETTAYCPQE
     AWILNRTIRA NIVFDLPFDG RRYEAVLEAV ALRPDIASFD QGDQTLAGEG GSRLSGGQKQ
     RVSLARALYS RSKYVLLDDC LSAVDSKTAN HIFFHAVKGD LMQGRTCMFA TNSIQLTIPH
     CDYIVLLDDG RVRGQGTAEE LVSEGRIDAD IMQNKAEFGS EKPGAYDTIE LDHAIKSPSS
     RSSLDTVSLL EVDPQQEDPE AGYEESKAEG AVAWSVIRTY LVTLGPPWYW VLVLFMFGIQ
     QFISLATNIW IKEWAVRYDM LDNFAFDPIQ RNATTRDETL DEPEEPQKVQ ARYYMAIYVA
     ICLAYAFFTF ARDLIVFYGS LKASSEIYER LLNSVLFAKL LFFDRIPLGQ ITNRFSRDVE
     VLDQNISTFS INTLQIAASL VMIIVFISSV VPAFLIAAVF ICVAYWFVMT IFINGARDLR
     RIESVERSPV YQQFSEALSG CVSIRAYARA SIFTAQNQVL VDRLNSPYLL QWASQQWLGF
     RVNFLGSLIL FFTGAFVVWD LESVDPSSAA LVLTYAAMFS ESIMWFVQLY AIVQQNLNSV
     ERVVEYTEIE QEANQPLKRA VYDLPEDWPS RGGVRFDAYT TRYAPELPPV LNDITFNVPP
     GKRVAVVGRT GAGKSTLTLA LIRGLEAELG RIEIDGIDIS EVTLDRLRQA VTVVPQDPGV
     FRGTLRDNLD PLHLYSNEEM IETLRAVRLL DAVRTYIPGN SATPLDCLDH PANALSRGQR
     QLLCIARTLL RRSRVLVFDE ATASIDHTTD AAIQESLRAS VTVGTTVITV AHRLLTIADY
     DKVVVLDAGC VAEQGSVQEL LDRDDDGIFR RLCVQSGDLE KIERVAAEKS GRK