W4934_FUSPC
ID W4934_FUSPC Reviewed; 1305 AA.
AC K3VYH8;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=ABC transporter FPSE_09185 {ECO:0000303|PubMed:25412204};
DE AltName: Full=W493 A and B biosynthesis cluster protein FPSE_09185 {ECO:0000303|PubMed:25412204};
GN ORFNames=FPSE_09185;
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096;
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
RN [2]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=25412204; DOI=10.1021/np500436r;
RA Soerensen J.L., Sondergaard T.E., Covarelli L., Fuertes P.R., Hansen F.T.,
RA Frandsen R.J., Saei W., Lukassen M.B., Wimmer R., Nielsen K.F.,
RA Gardiner D.M., Giese H.;
RT "Identification of the biosynthetic gene clusters for the lipopeptides
RT fusaristatin A and W493 B in Fusarium graminearum and F.
RT pseudograminearum.";
RL J. Nat. Prod. 77:2619-2625(2014).
CC -!- FUNCTION: ABC transporter; part of the gene cluster that mediates the
CC biosynthesis of the lipopeptides W493 A and B (PubMed:25412204). W493 A
CC and B consist of six amino acid residues D-allo-thr, L-Ala, D-Ala, L-
CC Gln, D-Tyr, and L-Val/L-Ile linked to a 3-hydroxy-4-methyltetradecanoic
CC acid polyketide chain (PubMed:25412204). May be involved in excretion
CC or internal transport of W493 A and B (Probable).
CC {ECO:0000269|PubMed:25412204, ECO:0000305|PubMed:25412204}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
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; AFNW01000306; EKJ70675.1; -; Genomic_DNA.
DR RefSeq; XP_009260577.1; XM_009262302.1.
DR AlphaFoldDB; K3VYH8; -.
DR SMR; K3VYH8; -.
DR STRING; 101028.EKJ70675; -.
DR EnsemblFungi; EKJ70675; EKJ70675; FPSE_09185.
DR GeneID; 20367802; -.
DR KEGG; fpu:FPSE_09185; -.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_8_1; -.
DR InParanoid; K3VYH8; -.
DR Proteomes; UP000007978; Chromosome 1.
DR Proteomes; UP000007978; Unassembled WGS sequence.
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; -; 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; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 3.
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 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1305
FT /note="ABC transporter FPSE_09185"
FT /id="PRO_0000445366"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 737..757
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 780..800
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 851..873
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 877..899
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 964..984
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 DOMAIN 48..348
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 372..663
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 738..1025
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1062..1300
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 434..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 407..414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1096..1103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1040
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1066
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1075
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1305 AA; 143128 MW; 03DFA91BFE553021 CRC64;
MADHQARQSG SSQRTVIPDP QLAKEKSNLT NYLRVFAYAT RWDFCVYVVG ALASIGVGVT
MPLMNVVLGQ LVGDFSDTVQ DPYNMDLNNF KSMLQKQSLY IVGLFLGRWL LNSINKFCFR
MIGIRLSSAI RHHYLRSLFA QSIHVIDSMP PGAAATAITA TSNTLQIGVS ERLGTFVTYV
STIIAAIAVA FTRSWSLTIV SASLLVYIAI IIAIVVPIYL KANAATLKAD AQGTAVASEA
LQGIRLVNAC GAHERIISKY SKWVTKAMER SQRVAPIIGA QTGLVFFGIF GVFGLAFWYG
TQQFIHGVIK NVGVVIIVLT SVMLILFAFS YLEQPIMAIS QAMVAATELF KVIDAPLPPM
GSFTPDINSK DLIFKDVTFE YPSRPGARVL DGLSFRIQAG QNTALVGPSG SGKSTIVGLL
ERWYSLKHSP VLPEAATPRS SKEGERDNHD ERKYERSTYE VPIMVPTNLT GALSGSISIG
AHDLDDLEGK WWRAQIGLVQ QEPFLFNSSI FENVANGLLG TVWENESEAK KRKMVQDACQ
EAYAHEFICR LPDAYDTRVG DGGAKLSGGQ KQRIAIARSI VKRPQIMILD EATSAIDAKS
EKIVQAALDR AIKTRTTITI AHRLSTIQKA DHIVVLSKGR VVEEGTHKSL MEHENGVYYS
LVEAQSLRLS TTDDTDSDLP ATTYVAELKS AAVDIEQPLE VQNDEDNGPV VEPEVLRTLT
QSFVKLLEGL RDQSSSFLLI TIASMGVGAA TPLQAWLFAK AVIVFISPSD DLKKEGDFWG
FMWLALAGGV GVAYFFQCWI SLRLQYHVGA TTKQSYLRDM LYQELSFFDD DSRSSGTLIG
RIAGDPKQVE GVFGLNLASA TSSVFTIVGC LIISLTFGWK LGLVGLCVTV PIMMVSGFWK
FRHELQFDQM NAAVFAESSQ FASEAIGAMR TVSSLTMESA INNRYKQLLD GHVEAARRKA
QWTAVIFGFA ESATLGCQAL ILWYGGRLIS SGEYSLEAFM VSYMAIINGV EYAGQILGVA
PSAAQAAAAA NRILDVQDSN RSSQEAEKSG PTVEDTDGGV EIELCNVSFK YPTRNVSIYK
NLDLTIKKGQ YAALVGPSGC GKTTIISLLE RFYDLEPNHG EILWNGTNIN DFGVYQYREH
LSLVSQEPIL FRGTIRDNIL FGVADPSSVP EERIHEVCRD VFIHDVIVSL PDGYNTEVGA
MSLSGGQKQR IAIARALIRN PKLLLLDEAT SALDSESEKI VQAAFEKARK RRTMIAVAHR
LATIQDADII FVFDQGMVVE KGTHGELLQK RGIYWDMCQT QALDQ
