ATR1_USTMA
ID ATR1_USTMA Reviewed; 1382 AA.
AC A0A0D1BUH6;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=ABC-type transporter atr1 {ECO:0000303|PubMed:17850255};
DE AltName: Full=Ustilagic acid biosynthesis cluster protein atr1 {ECO:0000303|PubMed:17850255};
GN Name=atr1 {ECO:0000303|PubMed:17850255}; ORFNames=UMAG_06461;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=17850255; DOI=10.1111/j.1365-2958.2007.05941.x;
RA Teichmann B., Linne U., Hewald S., Marahiel M.A., Boelker M.;
RT "A biosynthetic gene cluster for a secreted cellobiose lipid with
RT antifungal activity from Ustilago maydis.";
RL Mol. Microbiol. 66:525-533(2007).
RN [4]
RP INDUCTION.
RX PubMed=20173069; DOI=10.1128/aem.02211-09;
RA Teichmann B., Liu L., Schink K.O., Boelker M.;
RT "Activation of the ustilagic acid biosynthesis gene cluster in Ustilago
RT maydis by the C2H2 zinc finger transcription factor Rua1.";
RL Appl. Environ. Microbiol. 76:2633-2640(2010).
CC -!- FUNCTION: ABC-type transporter; part of the gene cluster that mediates
CC the biosynthesis of the glycolipid biosurfactant ustilagic acid (UA)
CC (PubMed:17850255). UA is a secreted cellobiose glycolipid that is toxic
CC for many microorganisms and confers biocontrol activity to U.maydis
CC (PubMed:17850255). Export of UA is presumably catalyzed by the ABC
CC transporter atr1 (Probable). Atr1 appears to be quite unspecific, as
CC many of the UA derivatives produced by cluster mutant strains are
CC readily exported (Probable). {ECO:0000269|PubMed:17850255,
CC ECO:0000305|PubMed:17850255}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17850255};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is strongly induced under conditions of nitrogen
CC starvation (PubMed:17850255). Expression is positively regulated by the
CC cluster-specific transcription factor rua1 that recognizes and binds to
CC the specific 5'-T/G-G/T-C-G-C-A-T-A/T-C/T-C/T-G/A-3' upstream
CC activating sequence found in all promoters of the UA biosynthesis genes
CC (PubMed:20173069). {ECO:0000269|PubMed:17850255,
CC ECO:0000269|PubMed:20173069}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
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DR EMBL; CM003162; KIS65757.1; -; Genomic_DNA.
DR RefSeq; XP_011392729.1; XM_011394427.1.
DR AlphaFoldDB; A0A0D1BUH6; -.
DR SMR; A0A0D1BUH6; -.
DR STRING; 237631.A0A0D1BUH6; -.
DR EnsemblFungi; KIS65757; KIS65757; UMAG_06461.
DR GeneID; 23566043; -.
DR KEGG; uma:UMAG_06461; -.
DR VEuPathDB; FungiDB:UMAG_06461; -.
DR eggNOG; KOG0055; Eukaryota.
DR OMA; FIIACSY; -.
DR OrthoDB; 248727at2759; -.
DR Proteomes; UP000000561; Chromosome 23.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
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; 2.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1382
FT /note="ABC-type transporter atr1"
FT /id="PRO_0000452756"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 800..820
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 848..868
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 911..931
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 951..973
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1034..1054
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1067..1087
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 101..400
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 445..688
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 797..1094
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1136..1377
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 480..487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1171..1178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 827
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 903
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1020
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1382 AA; 148733 MW; 913CCC6D2514003D CRC64;
MRFRSDSRAD HQHPKKQGSM DPDTIQALKY QDRSSSSSSN NKPKEKVGSA STSPSPTLFA
SNDSVKVEIG VGSSDKEKPD VKVSFFTIFR YASKRQLLIN LFGTGMAIAA GAAQPLMNIF
IGKIATVFLH FTSAIRSGDL DAIRAAHSDV YSTINSDALI LLYLGIGMFF ASMLYMAVFS
YTSERIASNI KYAYLSSLFS KPIDFFEQCG QGTVAAKIGS DVHLIQIGIG EKLPMAIMYF
STFVTAAAVA FAFSWRLSLV LLPIAPLILL AGGVMGALTK GCKLVELDCI AKAASRAEEA
FNAIKILKAF SKERTIGQEY DTLTTDTKAA GAKAGRIQGV GVGALLFIIY AGYALAFFYG
AQLIARGELL PGRIVSVVFA NFAGAFAIAN LFSMIENFTM ATAAASSVIG TIQQDLASSE
LSESRRNEEK SQTSRQLATG YNAELKLDHV HFAYPSKPER PVLKDLSLTI PSCVTTAIVG
LSGSGKSTIF ALLQRFYAPT RGSIRLDDVD ISALDVDWLR GQIGVVEQQP TLFAMSIQAN
IELGLPNRHT RSAEELESLV VQAAKKANAH NFITALTHGY QTEVGSQGFL LSGGQKQRIA
IARALIRDPK ILLLDEATSA LDSKSEAVVQ AALDEAAKDR TTIIISHRLS TVRNADNIVV
LGPDGIIEQG SHHELSIKPN GTFASMLRHQ DDKTKPVMVT SEPEIVDSSH SLCLTEIPTM
EIAHSLEVSR TISALADSVK PKDPSKNFEP PGESYASPAA DGVKQDAPKT DSVGLRTLLH
ILIKDPETGR LAQLYMLGSL CAAIIGAVYP VYAILFGTAI EDYAPCNSSD GRPCPNPARG
TMLHNNRISS GSFFIVAVGC AFISFYHVRS LYIAGSRVTH RLRVLVFQSL LCLDASFFDD
PVNTSNDLAS SLSVLSQGIY GGVGPTLGSI VQSLATVIVG YAVAIGYGWR LALVVIASTP
LTITAGLLRL RVLARKESKT KQAHQHTTQQ ACESIGAIRT VSAFNLQPQT LQVYQKNLEN
ASRSLRPTMC YSSVLFGLSQ CVQLLVTALA FWYGGRELAQ GHTSSKGFFT ILISVVYGSV
QAGNIFNYSA DFSSAHSAAC KSLSILKQAK EVVAEAQAND RDVQWNTEDS LPSGQIALKE
VTFRYPQRPT CTVLDRLSLT IEPGTFCAIV GGSGSGKSTV LQLIERFYTP ESGRVLLDGY
SITEGDPARF RKYMSYVPQE PTLFQGTIGW NIALGATDEN PEDVPLAKIQ QAAELAQLGD
LLASLPEGLN TQLSARGVQM SGGQKQRIAI ARAMIRDPRV LLLDEATSAL DPASERAVQG
ALDNVSQGRT TIAVAHRLST IAKADKVIVM QAGKVVEEGS PRELFQRDGL FALMARLQGV
SF
