ACLQ_ASPOR
ID ACLQ_ASPOR Reviewed; 804 AA.
AC Q2UPC0;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=ABC transporter aclQ {ECO:0000303|PubMed:25302411};
DE AltName: Full=Aspirochlorine biosynthesis protein Q {ECO:0000303|PubMed:25302411};
GN Name=aclQ {ECO:0000303|PubMed:25302411}; ORFNames=AO090001000032;
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, AND PATHWAY.
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: ABC transporter; part of the gene cluster that mediates the
CC biosynthesis of aspirochlorine (or antibiotic A30641), an unusual
CC halogenated spiro compound with distinctive antifungal properties due
CC to selective inhibition of protein biosynthesis, and which is also
CC active against bacteria, viruses, and murine tumor cells
CC (PubMed:25302411). {ECO:0000269|PubMed:25302411}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Heavy Metal importer (TC 3.A.1.210) subfamily. {ECO:0000305}.
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DR EMBL; AP007154; BAE56595.1; -; Genomic_DNA.
DR RefSeq; XP_001818597.1; XM_001818545.1.
DR AlphaFoldDB; Q2UPC0; -.
DR SMR; Q2UPC0; -.
DR STRING; 510516.Q2UPC0; -.
DR EnsemblFungi; BAE56595; BAE56595; AO090001000032.
DR GeneID; 5990568; -.
DR KEGG; aor:AO090001000032; -.
DR VEuPathDB; FungiDB:AO090001000032; -.
DR HOGENOM; CLU_000604_6_5_1; -.
DR OMA; VTIYMAK; -.
DR Proteomes; UP000006564; Chromosome 2.
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; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
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 InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..804
FT /note="ABC transporter aclQ"
FT /id="PRO_0000441201"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 236..518
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 552..786
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 585..592
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 804 AA; 90306 MW; CDF5B7E5558E92F2 CRC64;
MQLAVLTLAL CWAYPVTIYI SYLLSRLGIA LYRKHKDSTT GAWYEKHRKA AFTAIFWLQL
VQCFDLAISI TITGYAMNIS PQVEAWWVDK EFLASNIAVF MFLAAGLLPD PDVPFSPSLS
HSHAWIAGII MEALQLAMFC NQQSPVSVLS RVEYLQLGLV MVRLVLFVAM VALYFQPMYA
WSRIQLDETE PLLGEVDSKP VRDAQHGGWL DYVVGFSTLF PFLWPSDSRR LQLRAIFCFV
LLVIQRVVNI LVPHQLGIVV AHLGSGTIPY QKIAIYIALR ALQGQQGVIG SIRALLWIPV
SQSTYRRLTS SAFEHVLSLS LEFHLGKRIG EVMSALSKGS ALNTFLDGLV FQLFPMVADL
WIAALYFLIQ FDAFYSLIVI TVTWLYLFVT IYMAKYRGRA RREMVNRERE MEAAKTDALM
SYETVHHNSA VPHEINRFNR LVQAFQKAEY FVFFSLNLLN ATQNLLFTAG VAIVCLLCAY
QISADMQQVA MFVTLLTYLA QLQAPLNFFG SFYTQVQNNL VDAERMLALF KEKPLVQDRD
GAIDLNTCAG RVEFTHVNFA YDERRPALQD VSFTVEPGTS TAIVGESGSG KSTILKLLFR
FYDVAAGSVR FDGVDARDMT IASLRSHLGV VPQDTILFND TLLYNLLYAR PQATMEEVYA
ACRAASIHDR IMSFPDGYET KVGERGLRLS GGEKQRIAIA RTFLRSPQIL LLDEATASLD
SQTERQIQGA LDNIAKGRTT ITIAHRLSTI TKANQIIVLH QGRIVEKGTH EELLAANGMY
SQMWAKQTKA KEKKDSNATL VEVA
