AFLT_ASPPU
ID AFLT_ASPPU Reviewed; 514 AA.
AC Q6UEH3; A0A0F0I2C7;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Efflux pump aflT {ECO:0000305};
DE AltName: Full=Aflatoxin biosynthesis protein T {ECO:0000303|PubMed:15006741};
GN Name=aflT {ECO:0000303|PubMed:15006741}; ORFNames=P875_00052986-2;
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND NOMENCLATURE.
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=15006741; DOI=10.1128/aem.70.3.1253-1262.2004;
RA Yu J., Chang P.K., Ehrlich K.C., Cary J.W., Bhatnagar D., Cleveland T.E.,
RA Payne G.A., Linz J.E., Woloshuk C.P., Bennett J.W.;
RT "Clustered pathway genes in aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 70:1253-1262(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=15094053; DOI=10.1016/s0014-5793(04)00327-8;
RA Yu J., Bhatnagar D., Cleveland T.E.;
RT "Completed sequence of aflatoxin pathway gene cluster in Aspergillus
RT parasiticus.";
RL FEBS Lett. 564:126-130(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=15341913; DOI=10.1016/j.fgb.2004.06.007;
RA Chang P.K., Yu J., Yu J.H.;
RT "aflT, a MFS transporter-encoding gene located in the aflatoxin gene
RT cluster, does not have a significant role in aflatoxin secretion.";
RL Fungal Genet. Biol. 41:911-920(2004).
CC -!- FUNCTION: Efflux pump; part of the gene cluster that mediates the
CC biosynthesis of aflatoxins (PubMed:15006741, PubMed:15094053).
CC {ECO:0000305|PubMed:15006741, ECO:0000305|PubMed:15094053}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is not regulated by the aflatoxin pathway aflR
CC activator or aflS coactivator but by the fadA-dependent signaling
CC pathway (PubMed:15341913). {ECO:0000269|PubMed:15341913}.
CC -!- DISRUPTION PHENOTYPE: Does not affect aflatoxin secretion
CC (PubMed:15341913). {ECO:0000269|PubMed:15341913}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=KJK60792.1; Type=Erroneous gene model prediction; Note=The predicted gene P875_00052986 has been split into 2 genes: P875_00052986-1 (aflU) and P875_00052986-2 (aflT).; Evidence={ECO:0000305};
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DR EMBL; AY371490; AAS66020.1; -; Genomic_DNA.
DR EMBL; JZEE01000728; KJK60792.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q6UEH3; -.
DR SMR; Q6UEH3; -.
DR STRING; 1403190.Q6UEH3; -.
DR TCDB; 2.A.1.3.83; the major facilitator superfamily (mfs).
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..514
FT /note="Efflux pump aflT"
FT /id="PRO_0000438340"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 514 AA; 55021 MW; E653DDCF19E615B7 CRC64;
MLIDEAAEAS SHISGMKLYL IVLSLLLAVF CVALDNTILS VAIPRITDEF HRLNDIGWYA
SAYLLTTCAF QLLYGKLYAL FSTKWVFLVA LCIFEVGSLI CGVAPSSVVL IVGRAIAGVG
SSGIFTGALV TIAHIVPLAK RPVYMGLLGG MYGIASVAGP LLGGAFTNEV TWRWCFYINL
PVGGVTAVVI LFLLRIPKSA DLRTHGAWEM LKGLDPLGTI VFTPSIICVL LALQWGGVDY
AWSNGRIIAL FVLFGVLLIT FIIIQVLMKD KATVPIKVAS QRSVACASVF VFFIGASMFV
MIYYVPIWFQ AIRNQSPVQA GIDSIALILA NTAGAIISGA VTNKTGHYAP WFIVSSVIMS
IGAGCLTLFT VDIAQSKWIG FLFLYGIGVG FGFQQGAVAV QAVLPMAQVP IGTALIWFVQ
MLGGALFTSV AQNIFSTHLA ENLANLQLPG LDPEAIVGAG ATGFRQLVQP EYMDQVLVAY
NAALLDVFQV ALICSCLSIL GAVGIEWRSV KQNR
