IMQJ_ASPFN
ID IMQJ_ASPFN Reviewed; 510 AA.
AC B8NI27;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Peptide transporter imqJ {ECO:0000303|PubMed:29182847};
DE AltName: Full=Imizoquin biosynthesis cluster protein J {ECO:0000303|PubMed:29182847};
GN Name=imqJ {ECO:0000303|PubMed:29182847}; ORFNames=AFLA_064320;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2]
RP INDUCTION, AND FUNCTION.
RX PubMed=29182847; DOI=10.1021/acschembio.7b00731;
RA Khalid S., Baccile J.A., Spraker J.E., Tannous J., Imran M.,
RA Schroeder F.C., Keller N.P.;
RT "NRPS-derived isoquinolines and lipopetides mediate antagonism between
RT plant pathogenic fungi and bacteria.";
RL ACS Chem. Biol. 13:171-179(2018).
CC -!- FUNCTION: Peptide transporter; part of the gene cluster that mediates
CC the biosynthesis of imizoquins A to D, tripeptide-derived alkaloids
CC that serve a protective role against oxidative stress that are
CC essential for normal germination (PubMed:29182847).
CC {ECO:0000269|PubMed:29182847}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is down-regulated by ralstonins, lipopeptides
CC produced by the plant pathogenic bacteria Ralstonia solanacearum
CC (PubMed:29182847). Expression is positively regulated by the imizoquins
CC cluster-specific transcription regulator imqK (PubMed:29182847).
CC {ECO:0000269|PubMed:29182847}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
CC {ECO:0000305}.
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DR EMBL; EQ963479; EED49611.1; -; Genomic_DNA.
DR RefSeq; XP_002379992.1; XM_002379951.1.
DR AlphaFoldDB; B8NI27; -.
DR SMR; B8NI27; -.
DR EnsemblFungi; EED49611; EED49611; AFLA_064320.
DR VEuPathDB; FungiDB:AFLA_064320; -.
DR eggNOG; KOG0143; Eukaryota.
DR eggNOG; KOG1237; Eukaryota.
DR HOGENOM; CLU_534158_0_0_1; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006857; P:oligopeptide transport; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 1.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR000109; POT_fam.
DR InterPro; IPR018456; PTR2_symporter_CS.
DR PANTHER; PTHR11654; PTHR11654; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF00854; PTR2; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS01023; PTR2_2; 1.
PE 2: Evidence at transcript level;
KW Dioxygenase; Glycoprotein; Iron; Membrane; Metal-binding; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..510
FT /note="Peptide transporter imqJ"
FT /id="PRO_0000444549"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 348..468
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 377
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 379
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 439
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 459
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 510 AA; 56962 MW; 46A6B66570B16421 CRC64;
MVNQAFMLWC YITPVLGAVV AEQYIGRVKT IIFSSSVYLC GLVTLFLSSL PTAYAMGISL
PGLLVSLFLI GIGTGGIKTN VSSLIAEQYT GPKESRRILK SGEEVIVDRD LTIQRIFTTF
FLYINIGSFS PLLITIIEKE YGFSAAFSLS AITFSIGFII VLVSRHLYIS RDPDSSIIFN
ACKAFWIAIK HKGNLDYARP SYQTEQAATR RLSWDDSFID DLRRAIASCK IFILYPIYWA
AYSQFLTNFI SQAATMETHG VPNDIMTNID PITVLILLPV LDRIVFPFLR RQGVPVRHVD
RITIGMPDFQ PFVQESYQIC QRTCFQIISA IELGLGLQAG RLTQCCQPAA SEIRLLYYPP
TTKNLFDEGL KKRAWPHTDL GIITLLFQDM VGGLEVEDRA AGKPRSFIPV KRVSPNEMIV
NTSDSLQRWT NNVIRAGLHQ VTAPDAAKLS NGVDMLPARC SSVFFFKAGR DTSVGPLPEF
VTEDRPAAFE DMTALQYQQL KTRILHGVEG
