ACLA_ASPOR
ID ACLA_ASPOR Reviewed; 551 AA.
AC Q2UPC1;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=MFS efflux transporter aclA {ECO:0000303|PubMed:25302411};
DE AltName: Full=Aspirochlorine biosynthesis protein A {ECO:0000303|PubMed:25302411};
GN Name=aclA {ECO:0000303|PubMed:25302411}; ORFNames=AO090001000031;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP FUNCTION.
RX PubMed=25302411; DOI=10.1002/anie.201407624;
RA Chankhamjon P., Boettger-Schmidt D., Scherlach K., Urbansky B., Lackner G.,
RA Kalb D., Dahse H.M., Hoffmeister D., Hertweck C.;
RT "Biosynthesis of the halogenated mycotoxin aspirochlorine in koji mold
RT involves a cryptic amino acid conversion.";
RL Angew. Chem. Int. Ed. 53:13409-13413(2014).
CC -!- FUNCTION: MFS efflux transporter; part of the gene cluster that
CC mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an
CC unusual halogenated spiro compound with distinctive antifungal
CC properties due to selective inhibition of protein biosynthesis, and
CC which is also active against bacteria, viruses, and murine tumor cells
CC (PubMed:25302411). {ECO:0000305|PubMed:25302411}.
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; AP007154; BAE56594.1; -; Genomic_DNA.
DR RefSeq; XP_001818596.1; XM_001818544.1.
DR AlphaFoldDB; Q2UPC1; -.
DR SMR; Q2UPC1; -.
DR EnsemblFungi; BAE56594; BAE56594; AO090001000031.
DR GeneID; 5990567; -.
DR KEGG; aor:AO090001000031; -.
DR VEuPathDB; FungiDB:AO090001000031; -.
DR HOGENOM; CLU_000960_22_0_1; -.
DR OMA; NYVWIAN; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..551
FT /note="MFS efflux transporter aclA"
FT /id="PRO_0000441207"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 551 AA; 59081 MW; B151F46600DC6FE0 CRC64;
MDQPSPSAED SQPERQSTGT RGTRFWAVFV SLCFASFVAS LDITAITTAL PTVTRELDGG
ENYVWIANSY TLASAVVQPL IGQISNIVGR RNPMIILMCL FALGSGICGG ATSTGMMIAG
RTVQGLGAGG ILLLLEVIVC DLVPLRERAQ YVGIALSTCA LGISLGPLVG GALVQHATWR
WVFYINLPCA GVALVALVLC LNVQHKREVS WGRALARVDW VGNTIFIAAI CAIMYALVIG
GSVHPWSSYQ VLVPLVLGAF GWVLFHIFEA SPYCLEPTMP PRLFRNRTSM TAYVLAFLAA
MLMQWVVYFL TLFFQTVKGQ STTMSGVDVI PFTGFMIPSA IVGGAIMSKT GVYRPLHWAG
FALLSICMGV FSTWDAGTPR AEWVILQCLV GLGHGLLLTS VLPAIQAALP ESDNAAATSA
YAFLRSFGFV WGVEIPAVVF NGQVDRFISR VHDATVRNKL AHGGAYSLAG TSFLSQLGDE
ADAVRSTYTD SLRTVWQVGM AFALLGFALV VVEKHIELRT TLETDFGLEG SENRAATSVE
GVETGPVSKA Q
