ABC16_GIBZE
ID ABC16_GIBZE Reviewed; 1476 AA.
AC I1RF50; A0A098D6L3; A0A1C3YIK3;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=ABC-type transporter FG02316 {ECO:0000303|PubMed:34292732};
DE AltName: Full=Fusahexin biosynthesis cluster protein FG02316 {ECO:0000303|PubMed:34292732};
GN ORFNames=FG02316, FGRAMPH1_01T05577;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP IDENTIFICATION.
RX PubMed=34292732; DOI=10.1021/acs.jnatprod.0c00947;
RA Westphal K.R., Bachleitner S., Severinsen M.M., Brundtoe M.L., Hansen F.T.,
RA Soerensen T., Wollenberg R.D., Lysoee E., Studt L., Soerensen J.L.,
RA Sondergaard T.E., Wimmer R.;
RT "Cyclic, hydrophobic hexapeptide fusahexin is the product of a nonribosomal
RT peptide synthetase in Fusarium graminearum.";
RL J. Nat. Prod. 84:2070-2080(2021).
CC -!- FUNCTION: ABC-type transporter; part of the gene cluster that mediates
CC the biosynthesis of the fusahexin, a cyclic hydrophobic hexapeptide
CC with the amino acid sequence cyclo-(D-Ala-L-Leu-D-allo-Thr-L-Pro-D-Leu-
CC L-Leu) that plays an important role in cell surface hydrophobicity.
CC {ECO:0000305|PubMed:34292732}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; HG970332; SCB64403.1; -; Genomic_DNA.
DR RefSeq; XP_011318225.1; XM_011319923.1.
DR STRING; 229533.I1RF50; -.
DR GeneID; 23549698; -.
DR KEGG; fgr:FGSG_02316; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G05577; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_5_1; -.
DR InParanoid; I1RF50; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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-UniRule.
DR CDD; cd18579; ABC_6TM_ABCC_D1; 1.
DR CDD; cd18580; ABC_6TM_ABCC_D2; 1.
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; IPR044746; ABCC_6TM_D1.
DR InterPro; IPR044726; ABCC_6TM_D2.
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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1476
FT /note="ABC-type transporter FG02316"
FT /id="PRO_0000455676"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 906..926
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 950..970
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1021..1041
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1045..1065
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1137..1157
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1167..1187
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 274..552
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 622..847
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 916..1195
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1232..1464
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 586..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 654..661
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1265..1272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 682
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 798
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 836
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1476 AA; 162639 MW; 67F86E97CC186E1C CRC64;
MNSSSCDRSF GPYAEGCRGG FDFTLLFEES ILVVPITALL LLAAPFRATY LLRKHSVKVE
HSYWLYCKII LCLLLLASQI AFLVCWTQSP VVTTKASLPA AALSIVASIT LLGLSYVEHV
YSYRPSTVLN LFLLFSVLFD ATRTRTLWLQ GYNRPAAITA LISTVVKILM LSAETIEKRG
FLRPEYRELP SEVTSGVFSH WFFSWQLPLF RVGYSHDLEI ESLFPLEKHF KSSYLQTLLQ
TAWAKAPKKG DYDLLLVVFK TLKRPILFII FPRLCFIGFT FCQPFLISAT LSWAEKDADS
NDMNQGYGLI GAWFLVFIGL AVTTGQYQHL TVRATTMVRG QLISMLYDKA SDLSITAANP
TAALTLMSAD IERIDSGWRT AHDVWANLIE IVIAVYLLGR QLGLACLIPV GAAIFSIVGS
VIAVSFVMAR QAMWLEAIER RISVTSQMLG SMKGVKMCGL SEVLGTRIQA MREEELHISG
KFRRLLIWNM VLAYLAPIFA PVLSFMTYSL LAQSQGGRGN LDTNRMFTSL SLFALLQEPL
ASFVTSLSSF MGSVGSFVRI QAFLKTDART DDRIIQYNGE TEHSLISGVS SSEEKHPVSP
IQESMMKTEP SGDSPDGNAF VIRNASFGYD RNETPTLSNI DAIIPSGKLT LVVGPVGSGK
STLMKALLGE VGIMQGSVHA SNSTVAYCDQ TPWHMNGTVR ESIIAFSRPD ERWYQKVLEA
CALKQDLTQL PRGDLSNIGS RGLVLSGGQS QRVSLARAVY AQKSTIILDD VFSGLDAHTE
NAVFNNLLGS HGILRDLNTT VIVVSSRVKR LPYADHIICL DGTGTGCVQG TFDKLNESDN
YVSHSDVSSP DGARSKAPSS GPASSSAPVP ESSAAALAEL DMELTESKKD GAGRRSGDVA
IYMYYMNAIG WIPTMVFVLA ICAYIFCQSF PTIWLNWWAA ANAKEPFTRL GYYLGVYAML
GALSIIFLVL STWQMIVTMV PLSGNNFHQS LLKTVLNAPM SFFAATDAGT TINRFSQDLQ
LIDMDLPLSA LNTFATFVLC IAEMILIAVG SYYTAIAFPF LLATLWVVQH TYLRTSRQLR
FMDLEAKSPL YALFTETVTG LATLRAFGWR DALEKKHHEL LDRSQRPFYL LYAVQRWLTL
VLDMIVTIIA VLVVVLVTQL RGKLPAGLIG VALVNIIQFS QHLKLLMTFW TTLETHIGAI
SRIKSFTSDT ASEHEPQEKE QPPSVWPSKG TILFDQVSAG YKESEDVLKN ISLNIEAGQK
VGICGRTGSG KSSMVSCLFR MIDLHGGRII VDGLDISTIP REEIRTRLVG VPQDAFLIDG
SSVRLNADPA GGLTDAAIED ALRAVELWDI VTDNGGLDTS IEELHLSHGQ RQLFCIGRAI
LRPSPIVVLD EATSSVDSRV DELVQRLVRE RFSNRTVISI VHKLQSALDD FDMVVVLDAG
KLQEIGHPQE LLAKGPDAST FASMYQSVAT EKKEDK
