PAAT_PENRW
ID PAAT_PENRW Reviewed; 548 AA.
AC B6HIC2;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=MFS-rype transporter paaT {ECO:0000303|PubMed:23053082};
GN Name=paaT {ECO:0000303|PubMed:23053082}; ORFNames=Pc21g01300;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=23053082; DOI=10.1007/s00253-012-4425-1;
RA Fernandez-Aguado M., Ullan R.V., Teijeira F., Rodriguez-Castro R.,
RA Martin J.F.;
RT "The transport of phenylacetic acid across the peroxisomal membrane is
RT mediated by the PaaT protein in Penicillium chrysogenum.";
RL Appl. Microbiol. Biotechnol. 97:3073-3084(2013).
CC -!- FUNCTION: MFS-type transporter involved in penicillin production, most
CC likely through the translocation of side-chain precursors (phenylacetic
CC acid and phenoxyacetic acid) from the cytosol to the peroxisomal lumen
CC across the peroxisomal membrane. {ECO:0000269|PubMed:23053082}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000269|PubMed:23053082}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Probably recruited to the peroxisomal membrane by
CC pex19. {ECO:0000305|PubMed:23053082}.
CC -!- DOMAIN: The peroxisomal targeting signal allows recruitment to the
CC peroxisomal membrane by pex19. {ECO:0000305|PubMed:23053082}.
CC -!- DISRUPTION PHENOTYPE: Leads to a clear reduction in benzylpenicillin
CC production. {ECO:0000269|PubMed:23053082}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family.
CC Polyamines/proton antiporter (TC 2.A.1.2.16) subfamily. {ECO:0000305}.
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DR EMBL; AM920436; CAP95027.1; -; Genomic_DNA.
DR RefSeq; XP_002567200.1; XM_002567154.1.
DR STRING; 1108849.XP_002567200.1; -.
DR TCDB; 2.A.1.2.78; the major facilitator superfamily (mfs).
DR EnsemblFungi; CAP95027; CAP95027; PCH_Pc21g01300.
DR GeneID; 8305644; -.
DR KEGG; pcs:Pc21g01300; -.
DR VEuPathDB; FungiDB:PCH_Pc21g01300; -.
DR eggNOG; KOG0255; Eukaryota.
DR HOGENOM; CLU_008455_11_5_1; -.
DR OMA; YKWYCTM; -.
DR OrthoDB; 608951at2759; -.
DR BioCyc; PCHR:PC21G01300-MON; -.
DR Proteomes; UP000000724; Contig Pc00c21.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal 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 3: Inferred from homology;
KW Glycoprotein; Membrane; Peroxisome; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..548
FT /note="MFS-rype transporter paaT"
FT /id="PRO_0000455152"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 505..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 258..269
FT /note="Peroxisomal targeting signal"
FT /evidence="ECO:0000305|PubMed:23053082"
FT COMPBIAS 8..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 548 AA; 60841 MW; 0BE9D3AEAC578BC9 CRC64;
MEAPRSDQAH TDATTPMEAI RTTSLGTNNY GPVPDDYLDL PVREVNDGAD LREYITETRT
GEIIKPIKSN VTGKTEDWKM VTFTIDDPEN PKNWSKAFKW YCTMVVAFTC FVVAFCSSVI
TADVEGPIEE FGIGREASLV VITVFVIGFG LGPMVFAPMS EIVGRRPVYA LTLALAVIFV
IPCAVSKNIG TLIVCRLIDG IAFSAPMTLV GGTLADLWKS EERGVPMAAF SAAPFIGPAI
GPLVGGYLAD NCGWRWLYWI QLILAFVAWV MITFTVPETF APILLKKRAQ KLRKAEDDPK
YTTETELDAR PMGEKLRIFL FRPFQLLFLE PIVLFISLYM SVIYGLLYMF FVAYPIVYMG
GKGWSASNTG LMFIPLAIGV IFSACCAPFV NNHYLKVSVA YGGKPPAEKR LIPMMWACWC
IPSGLFVFAW TSYPDLHWMG PAMGGFLIGV GVILLYNSAN NYLVDTYQHQ AASALAAKTF
IRSIWGACTV LFTEQMYERL GDQWASTLLA FIGLACCAIP YVFYFKGESI RRFSKFAFSD
DEEKAIKA
