FER6_USTMA
ID FER6_USTMA Reviewed; 1337 AA.
AC A0A0D1CZ63; A1A655; Q4PEN2;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Multidrug resistance protein fer6 {ECO:0000303|PubMed:17138696};
DE AltName: Full=ATP-binding cassette sub-family C member fer6 {ECO:0000305};
DE AltName: Full=Fe-regulated protein 6 {ECO:0000303|PubMed:17138696};
DE Flags: Precursor;
GN Name=fer6 {ECO:0000303|PubMed:17138696}; ORFNames=UMAG_01431;
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 INDUCTION, AND FUNCTION.
RC STRAIN=521 / FGSC 9021;
RX PubMed=17138696; DOI=10.1105/tpc.106.043588;
RA Eichhorn H., Lessing F., Winterberg B., Schirawski J., Kamper J.,
RA Muller P., Kahmann R.;
RT "A ferroxidation/permeation iron uptake system is required for virulence in
RT Ustilago maydis.";
RL Plant Cell 18:3332-3345(2006).
RN [4]
RP FUNCTION.
RC STRAIN=521 / FGSC 9021;
RA Winterberg B., Uhlmann S., Linne U., Lessing F., Marahiel M.A.,
RA Eichhorn H., Kahmann R., Schirawski J.;
RT "Elucidation of the complete ferrichrome A biosynthetic pathway in Ustilago
RT maydis.";
RL Mol. Microbiol. 75:1260-1271(2010).
CC -!- FUNCTION: Multidrug resistance protein; part of the gene cluster that
CC mediates the biosynthesis of siderophore ferrichrome A which is
CC contributing to organismal virulence (PubMed:17138696, Ref.4).
CC {ECO:0000269|PubMed:17138696, ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression regulated by iron through the urbs1 transcription
CC factor (PubMed:17138696). {ECO:0000269|PubMed:17138696}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=DAA04936.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CM003141; KIS71538.1; -; Genomic_DNA.
DR EMBL; BK004083; DAA04936.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_011387300.1; XM_011388998.1.
DR AlphaFoldDB; A0A0D1CZ63; -.
DR SMR; A0A0D1CZ63; -.
DR STRING; 5270.UM01431P0; -.
DR EnsemblFungi; KIS71538; KIS71538; UMAG_01431.
DR GeneID; 23562455; -.
DR KEGG; uma:UMAG_01431; -.
DR VEuPathDB; FungiDB:UMAG_01431; -.
DR eggNOG; KOG0054; Eukaryota.
DR OrthoDB; 138195at2759; -.
DR Proteomes; UP000000561; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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; -; 2.
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 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; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Transport; Virulence.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1337
FT /note="Multidrug resistance protein fer6"
FT /id="PRO_0000441962"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 220..242
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 247..269
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 769..789
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 817..837
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 890..909
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 915..933
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 999..1019
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1028..1048
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 95..386
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 417..667
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 781..1056
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1097..1325
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 432..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 478..485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1131..1138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 731
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1057
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1337 AA; 147780 MW; 21B703023735001B CRC64;
MTPEASANWF SLCWFAWIDP ILTAGYTRPM EKDDLYLLQP HRCSEHLGSQ LLAALEKRRK
QRQDYVEANP NKTDKPAKIP PLMWAMNDIV FRYFWIGGLL KLLADVGTIT SPLLVRALIN
FGRDSYNLRG DRDQAPNLGS GVGLAIGLFL VQALCVFLNV HAFNRGFGTG IILRGALIQA
IFQRGMNLST RARTVGGLGV SKLVTLISAD ATRIDYAGQF FHMAWTSAVQ IIICVALLIW
SLSYSALPGI AVLVLMSPIQ TAITKRLFAL RKKSMVWTDK RNKAVNEVVG GIRVVKQFAW
EEPYSVRIAE LRRKEMSFHR VRLYLRSLNL ALAFATPTIA TVLSFVTYAL VGNELDAAIL
FSSLSFFTLL RTPLQFLPIA WNAIVDAKNA ADRIEKVFDA EIQRDQIIRD CSATNGIQLE
DASFTWETAQ AADTAKPVNE KKGQDSPSNE KETPVDRAST LDSLNLTVPR GTLCAIVGGV
GSGKSSLISA LAGEMRQIAG KVTLSGSTAV CAQTAWIQST TIRNNIVFGN AFDPERYRYV
LEVCCLLPDL DTLADGDQTI VGEKGVSLSG GQKQRLNIAR ALYHNSEIVL LDDCLSALDA
RVGADIFANV IAGDAMAGKT RLLVTHSLNV LRSCDWIVHM EEGRITEQGT YAELVESKGR
VAELLLTHTK DHFEEEKKEP SKHPIDEIQE TAESILDAGS ASNRNSEASE STTTTVNAES
KDTSNAEGVT NKTEKKDLVA PPAQAKSKAL MQDEERFSGS VSRTTYLSYL NAAPLSILLP
LFLVAVLVFQ GSTIMSPVWL LWWQNGHFGL QQGVYMGIYA VFGITQSLGL LSMGVIFSTF
TIKSATTLHH RALQRVLHAP FSFFDTTPQG RITHRFSKDM DTLDNIIGEA MRTLIGTIVQ
VIGSIVLIAI LTPYFLIPVA VILVLYFWIA AYYRSTAREL RRIDAGLRSN MHEHFSESLH
GLVTIRAFGN VDAFIAENCR RIDKQNRAYW LAQTCQRWLS VRLDFLGSLL ILSVAILVVA
SRFDISPGET GVALSYILTA QSIFGWMIRH AAELENNMSA VERVLHYANH IEQEKPYHIP
QVDDALEARE WPERGEIRFE GVEAKYGSSE RNVLDKLDLH IAPGEKIAFC GRTGAGKSTL
VTTLLRTLEL SAGTITIDGI DIASMGLHRL RSSLSLIPQD AVIYSGTLRY NLDPLDQHED
ATLHDALQRT SLTDLSLDMT ITEEGGNLSA GQRSLISLAR AMVRKTRIVI LDEATASIDQ
ETDVQIQEVL RNEFDGITTL TVAHRIQTIL HSDRVCVLDK GVIVEIGSPA ELWAKEKGAF
RALCDSANIR YQDGEWK
