GRA13_GIBZE
ID GRA13_GIBZE Reviewed; 1445 AA.
AC I1R9B3; A0A098D0D5;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=ABC-type transporter FGSG_00046 {ECO:0000303|PubMed:30395461};
DE AltName: Full=Gramillins biosynthetic cluster protein FGSG_00046 {ECO:0000303|PubMed:30395461};
GN ORFNames=FGRAMPH1_01T00151, FGSG_00046;
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 FUNCTION, AND PATHWAY.
RX PubMed=30395461; DOI=10.1021/jacs.8b10017;
RA Bahadoor A., Brauer E.K., Bosnich W., Schneiderman D., Johnston A.,
RA Aubin Y., Blackwell B., Melanson J.E., Harris L.J.;
RT "Gramillin A and B: cyclic lipopeptides identified as the nonribosomal
RT biosynthetic products of Fusarium graminearum.";
RL J. Am. Chem. Soc. 140:16783-16791(2018).
CC -!- FUNCTION: ABC-type transporter; part of the gene cluster that mediates
CC the biosynthesis of gramillins A and B, bicyclic lipopeptides that
CC induce cell death in maize leaves but not in wheat leaves
CC (PubMed:30395461). May be involved in the secretion of gramillins
CC (Probable). {ECO:0000269|PubMed:30395461, ECO:0000305|PubMed:30395461}.
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 {ECO:0000305}.
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DR EMBL; HG970332; CEF71875.1; -; Genomic_DNA.
DR RefSeq; XP_011315635.1; XM_011317333.1.
DR AlphaFoldDB; I1R9B3; -.
DR SMR; I1R9B3; -.
DR STRING; 229533.I1R9B3; -.
DR GeneID; 23547562; -.
DR KEGG; fgr:FGSG_00046; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G00151; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_5_1; -.
DR InParanoid; I1R9B3; -.
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-KW.
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; 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; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1445
FT /note="ABC-type transporter FGSG_00046"
FT /id="PRO_0000450579"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..277
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 868..888
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 912..932
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1004..1024
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1026..1046
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1116..1136
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1147..1167
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 259..541
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 595..821
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 974..1173
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1210..1441
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 803..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 627..634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1244..1251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1445 AA; 159765 MW; 9B0BCF9730BCC397 CRC64;
MDNTIGPRVD PSIRAFDFTA LFEECFLDIL PWSLFLLMLL VRLKFLLNRP KIIRVDRLCL
IKEALWTLYA VVKLAQLILW ASIAAFTTAG TVPAAALAFV GCMGGSVLSY FEHCRSRRPS
SLLGILTLLI LLCDVTRVRT MWLMDQPRAI SILTTAALPI NILLLVFESL TKTAVANEKE
ASRSKEEIVG ILNRSVFWWL NSLFILGRKH VLHMGNLPRV DSKVLTSYAA PKVYERWESK
PQSLMLQSLQ AYPMTLLRGG LCRLFTALFV TSQPLLLKRT IRWFSEPSTP VSDAEGYGLI
GAYLVVYGGR AVFTALAQHQ NYRLITMIRA SLVSLIYDRT LTLDLVEAKE SAALTLMSTD
VERIGQGLQF VHEIWATPAE FGVAIFLLQR EVALGSLAPV IIIIVAIVGT VLLSMKIDPH
QKEWIGAIER RIGSTTDMLR NMRGVKMSGF EDALTSILQA MRVEEVNISR ATKLLFIGCQ
VFSTATATIS PVLGFTIYVL MQRAQGKPGL ASSSAFTSLS LFSILSSSVY IFLTSVPAIF
SGISCFARVE NYLVSENITG PTDAEGQDSE ASSISAEKIS IIAPKIAPSD YLLVIRDGSV
RWKGQEKAVL SQINLCIEQG SFCVISGSVG SGKSSLLYAI LGEASLKADT FHISTTSIAY
CQQSPWLPDI SVKECVLNGR DWDEDLYKRV IHACALSEDL AQLSAGDHTK VGYEGGTLSG
GQRQRVALAR ALYSRRRLLL LDDTFSALDP KTEKSVSGNL FSSSGLLREL GTTVICTTGK
PGNSNKYADY TLDLNKEGEA QLRNTQKDMQ DDEIEASTYS REQNGPKKQE EDANHESNQS
PETSQEHELA QESVPTFSSM IFYLRSTGMG FFALSFSLSL VYSFWQNFPT IWVNLWTQHD
AKHPYGDLAK YIGVYILCAV LALVTHTVVT WFVNMACNGI DGAAVRAGPT RDTPENSGTA
SITGRGYVVF TNKHRAPMSY FESVDIGTIT NHFSQDMEKV DLEIPLTGVQ ALFAFTSALV
QLVMLSIGTK WMAITFPFII AILAIIQRQY LKTSRQLRLL DLEAKSPLYS HFTETLSGLA
TIRAFGTHKQ CQSINTERLD CSQGPFYLLY CAQRWLTLVL NLVIGAMAIL MMGVTIKLRG
STGAGYIGLA FVNLTTFSQS IQSLLTWWTM MEASIGAVHR VQQFEKETPQ EDVLGQVTSP
PHSWPKAGLI ELKELSASYL SSVSPVLRNV TFTVQPGQKV GICGRTGSGK TSLILCLQRM
IKINSGSILI DGLNTSHVPA KTLRERLICI PQDALIFNGT VRLNLDPQSS FTDKQLQDNL
RRVELWDLIS SKGGLDATMQ DGLLSHGQLQ LFCLSRVLQK KSPIVILDEV SSSADEESQR
LISKIIREDF KDRTVISIAH RLQQIADFDI ILVFSQGQLV EQGSPEDLLG RDVSLFQDLF
SQQDK
