PATM_PENEN
ID PATM_PENEN Reviewed; 1394 AA.
AC B6RAL1; A0A0A2JK17;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=ABC transporter patM {ECO:0000303|Ref.1};
DE AltName: Full=Patulin biosynthesis cluster protein M {ECO:0000303|Ref.1};
GN Name=patM {ECO:0000303|Ref.1}; ORFNames=PEX2_082820;
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, AND INDUCTION.
RC STRAIN=NCPT44;
RA Puel O., Tadrist S., Dauteloup C., Lebrihi A.;
RT "Cloning and molecular characterization of Penicillium expansum ABC
RT transporter gene involved in patulin biosynthesis.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8;
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NRRL 35695;
RX PubMed=25120234; DOI=10.1016/j.ijfoodmicro.2014.07.028;
RA Tannous J., El Khoury R., Snini S.P., Lippi Y., El Khoury A., Atoui A.,
RA Lteif R., Oswald I.P., Puel O.;
RT "Sequencing, physical organization and kinetic expression of the patulin
RT biosynthetic gene cluster from Penicillium expansum.";
RL Int. J. Food Microbiol. 189C:51-60(2014).
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=15082620; DOI=10.1093/ije/dyh028;
RG Patulin Clinical Trials Committee, Medical Research Council;
RT "Clinical trial of patulin in the common cold. 1944.";
RL Int. J. Epidemiol. 33:243-246(2004).
RN [5]
RP BIOTECHNOLOGY.
RX PubMed=22222931; DOI=10.1016/j.fct.2011.12.022;
RA de Melo F.T., de Oliveira I.M., Greggio S., Dacosta J.C., Guecheva T.N.,
RA Saffi J., Henriques J.A., Rosa R.M.;
RT "DNA damage in organs of mice treated acutely with patulin, a known
RT mycotoxin.";
RL Food Chem. Toxicol. 50:3548-3555(2012).
RN [6]
RP BIOTECHNOLOGY.
RX PubMed=26619846; DOI=10.1007/s13277-015-4474-z;
RA Boussabbeh M., Ben Salem I., Rjiba-Touati K., Bouyahya C., Neffati F.,
RA Najjar M.F., Bacha H., Abid-Essefi S.;
RT "The potential effect of patulin on mice bearing melanoma cells: an anti-
RT tumour or carcinogenic effect?";
RL Tumor Biol. 37:6285-6295(2016).
RN [7]
RP INDUCTION.
RX PubMed=27528575; DOI=10.1111/mpp.12469;
RA Kumar D., Barad S., Chen Y., Luo X., Tannous J., Dubey A., Glam Matana N.,
RA Tian S., Li B., Keller N., Prusky D.;
RT "LaeA regulation of secondary metabolism modulates virulence in Penicillium
RT expansum and is mediated by sucrose.";
RL Mol. Plant Pathol. 18:1150-1163(2017).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=30100914; DOI=10.3389/fpls.2018.01094;
RA Kumar D., Tannous J., Sionov E., Keller N., Prusky D.;
RT "Apple intrinsic factors modulating the global regulator, LaeA, the patulin
RT gene cluster and patulin accumulation during fruit colonization by
RT Penicillium expansum.";
RL Front. Plant Sci. 9:1094-1094(2018).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=25625822; DOI=10.1094/mpmi-12-14-0398-fi;
RA Li B., Zong Y., Du Z., Chen Y., Zhang Z., Qin G., Zhao W., Tian S.;
RT "Genomic characterization reveals insights into patulin biosynthesis and
RT pathogenicity in Penicillium species.";
RL Mol. Plant Microbe Interact. 28:635-647(2015).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=30680886; DOI=10.1111/1462-2920.14542;
RA Li B., Chen Y., Zong Y., Shang Y., Zhang Z., Xu X., Wang X., Long M.,
RA Tian S.;
RT "Dissection of patulin biosynthesis, spatial control and regulation
RT mechanism in Penicillium expansum.";
RL Environ. Microbiol. 21:1124-1139(2019).
CC -!- FUNCTION: ABC transporter; part of the gene cluster that mediates the
CC biosynthesis of patulin, an acetate-derived tetraketide mycotoxin
CC produced by several fungal species that shows antimicrobial properties
CC against several bacteria (Probable) (PubMed:30680886). May be involved
CC in the secretion of E-ascladiol to be converted to patulin by the
CC secreted patulin synthase patE (Probable).
CC {ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:25625822,
CC ECO:0000305|PubMed:27528575, ECO:0000305|PubMed:30680886,
CC ECO:0000305|Ref.1}.
CC -!- PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis.
CC {ECO:0000269|PubMed:30680886}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:30680886};
CC Multi-pass membrane protein {ECO:0000269|PubMed:30680886}. Cell
CC membrane {ECO:0000269|PubMed:30680886}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:30680886}.
CC -!- INDUCTION: Expression is correlated with the production of patulin
CC (PubMed:25120234). Expression is positively regulated by the secondary
CC metabolism regulator laeA (PubMed:27528575, PubMed:30100914).
CC Expression is strongly decreased with increased sucrose concentrations.
CC This decrease is lost in the presence of malic acid (PubMed:30100914).
CC Expression is increased with pH changes from 2.5 to 3.5 in the presence
CC of a limiting concentration of sucrose, 50 mM (PubMed:30100914).
CC Natural phenols present in apple fruits such as chlorogenic acid or the
CC flavonoid epicatechin modulate patulin biosynthesis. They increase
CC expression in the absence of sucrose, have little impact in the
CC presence of 15 mM sucrose, and decrease expression in 175 mM sucrose
CC (PubMed:30100914). Expression is positively regulated by the patulin
CC cluster-specific transcription factor patL (PubMed:25625822). Finally,
CC expression is also positively regulated by the velvet family proteins
CC transcription regulators veA, velB, velC, but not vosA
CC (PubMed:30680886). {ECO:0000269|PubMed:25120234,
CC ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:27528575,
CC ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886}.
CC -!- DISRUPTION PHENOTYPE: Strongly reduces the production of patulin and
CC leads to the production of a distinct dark-red pigment.
CC {ECO:0000269|PubMed:30680886}.
CC -!- BIOTECHNOLOGY: Patulin was originally used as an antibiotic and
CC specifically trialed to be used against the common cold, but it is no
CC longer used for that purpose since it has been shown to induce
CC immunological, neurological and gastrointestinal effects
CC (PubMed:15082620). Genotoxic effects of patulin with dose-dependent
CC increase in DNA strand breaks in brain, liver and kidneys have been
CC detected in mice (PubMed:22222931). However, more recently, it has been
CC proposed that patulin might also have anti-tumor properties
CC (PubMed:26619846). {ECO:0000269|PubMed:15082620,
CC ECO:0000269|PubMed:22222931, ECO:0000269|PubMed:26619846}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=KGO52635.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EF051699; ABN48540.1; -; Genomic_DNA.
DR EMBL; KF899892; AIG62140.1; -; Genomic_DNA.
DR EMBL; JQFZ01000262; KGO52635.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_016595365.1; XM_016745552.1.
DR AlphaFoldDB; B6RAL1; -.
DR SMR; B6RAL1; -.
DR STRING; 27334.B6RAL1; -.
DR EnsemblFungi; KGO43539; KGO43539; PEXP_094400.
DR EnsemblFungi; KGO52635; KGO52635; PEX2_082820.
DR GeneID; 27680972; -.
DR HOGENOM; CLU_000604_35_0_1; -.
DR OrthoDB; 324553at2759; -.
DR UniPathway; UPA00918; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IDA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0140723; P:patulin biosynthetic process; IMP:GO_Central.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010929; PDR_CDR_ABC.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF06422; PDR_CDR; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Vacuole.
FT CHAIN 1..1394
FT /note="ABC transporter patM"
FT /id="PRO_0000445927"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 546..566
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 579..599
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 688..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1131..1151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1177..1197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1219..1239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1245..1265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1280..1300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1368..1388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 98..341
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 767..1013
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 808..815
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT VARIANT 178
FT /note="C -> CEMSPL"
FT /evidence="ECO:0000269|PubMed:25338147"
FT VARIANT 282
FT /note="M -> V (in strain: MD-8)"
FT /evidence="ECO:0000269|PubMed:25338147"
FT VARIANT 313
FT /note="I -> V (in strain: MD-8)"
FT /evidence="ECO:0000269|PubMed:25338147"
FT VARIANT 640
FT /note="P -> L (in strain: MD-8)"
FT /evidence="ECO:0000269|PubMed:25338147"
FT VARIANT 747
FT /note="S -> P (in strain: MD-8)"
FT /evidence="ECO:0000269|PubMed:25338147"
FT VARIANT 897
FT /note="S -> N (in strain: MD-8)"
FT /evidence="ECO:0000269|PubMed:25338147"
FT VARIANT 1122
FT /note="H -> Y (in strain: MD-8)"
FT /evidence="ECO:0000269|PubMed:25338147"
SQ SEQUENCE 1394 AA; 155346 MW; 8F4C997950E1E392 CRC64;
MVDNYHSSLD VAKTPIQSDA DAQKSEAETE GPSSKSSQIA AGESIADSVR NFLELRQGGI
PDDTGVVFDK ISAVGSGTGS QDAPTVTSAA QSAFGLLSPL QNRQRKQYSR PILSGFSGTI
NPGEMLLVLG KPGSGCTTFL KTLSGLWDEY KEIQGELTLG GHPLLDVMKQ RPQDILFCAE
SDDHFPTLTV AETLRFATRA RCGPQVSARE IDTMVTQLAK LVGLGNVLNT KVGDAKIRGV
SGGERRRVSL AEALATCARL ICLDNPTHGL DSSTAVEFME MMREWTTQSR CVAAMSVYQA
SDAIVSYFDK VLIINSGRQI YYGPVRDAKA YFEDLGFECL STTTVADFLN VMSADPDVRR
AQENRENQVP RTAEEFERAF SASPIYQEMQ KSVQVAKERF QTNPSPLVKT SAFALPIWHQ
IWYCAGRQFR IVTSDYSLWA VELATIVVQS LVLGTLFRNQ QRTTSSLFIF ASALFYSVLV
PALQSMAEFG NGFAQRPLIL KQKRYQISRP IAYALGLVTT DVVWKVAAIC YNIPLYFLTG
FQRTAGNFFT WFLIIYLEHL ALSMFFRSVA IFSPNMHRAV LPVGIFFNMY VLYTGLYVPA
PQMQVWLGWL RYLNPLYYAF ESVMVNEFRD LSYQCSASDP VPSGLGYNDM AHQVCAVVGS
EPGDRLLSGA SYIHAQYGFK TSHLWRNVGI NAALFVFFAL CSGIGMEMLK TPAGQLATVF
YKSSPGVTHR RDKIDSETGQ DQGNESSEMS AGQSNDALRL QEHQGPDKSH NLAWTNLCLD
IKTKEGDQRL LNNLSGSVKS GQLKALMGVS GAGKTTLLNA LAGRSTIGNL TGTLALNGQV
LPTFFRSRMG YVQQQDIHLP TQTVREALQM TARLRRPESI SVADKNAYVE KVIEWLSMEH
IADALVGVPG AGLNLEQRKK VSIGVEMASK PEILFLDEPT SGLDGQSAML IARLLRRLAD
SGQAILCTIH QPAAELIDQF DKLYLLSRGG NLVYDGSLGT RCHEAIQYFQ PRSRPCGPEE
NPAEYFLAVI GAGSRNDAHM DWASLWNDSE QGKEREKAEE SLVPAAEQAP QLEQQSLYSV
PFHVQLWVVV QRTWLYYWRE PDYVNSKLWM SVGNSLLNSL THLQSPNTER GAYNRVFSAF
MSLIVGPPLG LQVQPRFVTL RDIFVHRERE SLTYHWLAFV LSAFIVELPF TFLSSLVYWL
LWYFPVGYFN APSRAGYSFL MYELFGVFAT SLAQLCASLM PNIEAAFAAN GFFFMFCNTF
AGTLSPKPVT PSGWRWFYNI SPLFYLGEGV TVDVLQDLPI RCEESEVSIF YAVNGTTCGQ
YAQDFLKTAT GYLLNPASTT ECQYCRYRDG QSYFQQYGYE FAHRHRNIGV FICFIAFNFT
MVLVMTYLTK TRRH
