FGM5_GIBZE
ID FGM5_GIBZE Reviewed; 1472 AA.
AC I1S2J9; A0A098E169;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=ABC transporter FGM5 {ECO:0000303|PubMed:30804501};
DE AltName: Full=C64 cluster protein NRPS5 {ECO:0000303|PubMed:25333987};
DE AltName: Full=Fg3_54 cluster protein FGM5 {ECO:0000303|PubMed:30804501};
DE AltName: Full=Fusaoctaxin A biosynthesis cluster protein FGM5 {ECO:0000303|PubMed:30804501};
GN Name=FGM5 {ECO:0000303|PubMed:30804501}; ORFNames=FG10995;
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.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RG EnsemblFungi;
RL Submitted (JAN-2017) to UniProtKB.
RN [5]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23266949; DOI=10.1105/tpc.112.105957;
RA Zhang X.W., Jia L.J., Zhang Y., Jiang G., Li X., Zhang D., Tang W.H.;
RT "In planta stage-specific fungal gene profiling elucidates the molecular
RT strategies of Fusarium graminearum growing inside wheat coleoptiles.";
RL Plant Cell 24:5159-5176(2012).
RN [6]
RP FUNCTION.
RX PubMed=24244413; DOI=10.1371/journal.pone.0079042;
RA Abou Ammar G., Tryono R., Doell K., Karlovsky P., Deising H.B.,
RA Wirsel S.G.;
RT "Identification of ABC transporter genes of Fusarium graminearum with roles
RT in azole tolerance and/or virulence.";
RL PLoS ONE 8:e79042-e79042(2013).
RN [7]
RP IDENTIFICATION, AND INDUCTION.
RX PubMed=25333987; DOI=10.1371/journal.pone.0110311;
RA Sieber C.M., Lee W., Wong P., Muensterkoetter M., Mewes H.W., Schmeitzl C.,
RA Varga E., Berthiller F., Adam G., Gueldener U.;
RT "The Fusarium graminearum genome reveals more secondary metabolite gene
RT clusters and hints of horizontal gene transfer.";
RL PLoS ONE 9:e110311-e110311(2014).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30804501; DOI=10.1038/s41467-019-08726-9;
RA Jia L.J., Tang H.Y., Wang W.Q., Yuan T.L., Wei W.Q., Pang B., Gong X.M.,
RA Wang S.F., Li Y.J., Zhang D., Liu W., Tang W.H.;
RT "A linear nonribosomal octapeptide from Fusarium graminearum facilitates
RT cell-to-cell invasion of wheat.";
RL Nat. Commun. 10:922-922(2019).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=31100892; DOI=10.3390/toxins11050277;
RA Westphal K.R., Nielsen K.A.H., Wollenberg R.D., Moellehoej M.B.,
RA Bachleitner S., Studt L., Lysoee E., Giese H., Wimmer R., Soerensen J.L.,
RA Sondergaard T.E.;
RT "Fusaoctaxin A, an example of a two-step mechanism for non-ribosomal
RT peptide assembly and maturation in fungi.";
RL Toxins 11:0-0(2019).
CC -!- FUNCTION: ABC transporter; part of the Fg3_54/C64 gene cluster that
CC mediates the biosynthesis of the octapeptide fusaoctaxin A, a virulence
CC factor that is required for cell-to-cell invasiveness of plant host
CC (PubMed:30804501). The 2 nonribosomal peptide synthetases NRPS9 and
CC NRPS5 form an assembly line which likely utilizes GABA as a starter
CC unit (loaded on the unique module M1 of NRPS9) and sequentially
CC incorporates seven extender units composed of the residues L-Ala, L-
CC allo-Ile, L-Ser, L-Val, L-Ser, L-Leu and L-Leu, respectively
CC (PubMed:30804501, PubMed:31100892). During the process, each of the
CC residues that are tethered on modules M3-M7 of NRPS5 containing an E
CC domain can undergo an epimerization reaction to produce a D-
CC configuration before the transpeptidation reaction occurs
CC (PubMed:30804501, PubMed:31100892). The elongation of the peptidyl
CC chain might be terminated by module M8-mediated L-Leu incorporation,
CC followed by R domain-catalyzed 4 electron reduction to release the
CC resulting octapeptide from the assembly line as an alcohol
CC (PubMed:30804501, PubMed:31100892). Fusaoctaxin A is cleaved by the
CC cluster specific ABC transporter FGM5 to the pentapeptide fusapentaxin
CC A and the tripeptide fusatrixin A (PubMed:31100892). The other enzymes
CC from the cluster, FGM1, FGM2, FGM3 and FGM9 seem not to be involved in
CC the biosynthesis of fusaoctaxin A and their functions have still to be
CC determined (Probable). {ECO:0000269|PubMed:30804501,
CC ECO:0000269|PubMed:31100892, ECO:0000305|PubMed:30804501}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:31100892}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor FGM4 and is induced during infection of
CC coleoptiles of wheat seedlings (PubMed:23266949, PubMed:25333987). The
CC fusaoctaxin A gene cluster is silenced by H3K27 trimethylation by the
CC histone methyltransferase KMT6 (PubMed:31100892).
CC {ECO:0000269|PubMed:23266949, ECO:0000269|PubMed:25333987,
CC ECO:0000269|PubMed:31100892}.
CC -!- DISRUPTION PHENOTYPE: Leads to reduced virulence (PubMed:23266949,
CC PubMed:30804501). Results in a substantial increase of fusaoctaxin A,
CC and abolishes the production of fusapentaxin A and fusatrixin A
CC (PubMed:31100892). {ECO:0000269|PubMed:23266949,
CC ECO:0000269|PubMed:30804501, ECO:0000269|PubMed:31100892}.
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; HG970334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_011325375.1; XM_011327073.1.
DR AlphaFoldDB; I1S2J9; -.
DR SMR; I1S2J9; -.
DR GeneID; 23557869; -.
DR KEGG; fgr:FGSG_10995; -.
DR HOGENOM; CLU_000604_27_5_1; -.
DR InParanoid; I1S2J9; -.
DR PHI-base; PHI:3924; -.
DR PHI-base; PHI:8224; -.
DR PHI-base; PHI:9036; -.
DR Proteomes; UP000070720; Chromosome 3.
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 GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 1.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Hydrolase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1472
FT /note="ABC transporter FGM5"
FT /id="PRO_0000449946"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 900..920
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 938..958
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1003..1023
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1024..1044
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 DOMAIN 284..551
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 605..834
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 900..1139
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1218..1468
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 638..645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1255..1262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
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 763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 784
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 843
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1472 AA; 162151 MW; 809A4BED1E531CAE CRC64;
MAVSGCTNDN SFGPIVQGCR GDFDFTLRFQ NIILGILPAA IFILLALTRV ATLAFRSRIV
GGKVLQFTKL AVIAATAALQ LVLLILSSTS NDESVDGDTF AVANSALGFS QWIVTLALSF
AEHSRAPRPS SILTLYLLLQ ILLDVTRCRS YWLLATSFQI TRYAGVFTAT IGLKVITLLL
ELQNKARWMT WRKEDHSPEE TSSLFNLGVY FWLIGIFRNG FKKTLSIKDD LYLLDHEMQS
KILLDRLTIS FAKSSANVGK RFRLAKALGR ALIVPLILPV VPRIAMIGFQ YAQPFFIHAL
LEYLIHKDVP KNDGYGLIGA ALIIYAGIAI SDALFWYFHQ RCLYMARGCL ASYVYRSTTQ
GKMTDIGDAA VLTLMSTDVE RIIYGFHGLH DFWANIIEIG LGCFLLQRQL GLAFISPIVV
ILLCVAATTA IAWAIGERQS RWMAKIESRV GLTSSIISNI KSLRISGITA PVRDLVQKMR
EQELSIGNKF RWLLIMTATV AFVPSAMSPV VAFAFTNEQL DTLKIFVSFS FITLLTNPLG
AMFQSVPAVI AAFVCLERIQ KFLEIEPRVD YRKSSRPLSP ADGSLLEQDD EKPLGLGQGA
SKSLISIVDG SFGWTSEKMT LTGISVDVPV GKLTLVVGPV ASGKSTFCKA LLGEVPFSSG
EVIVPSTEAP IGYCEQTPFL KNGSIRDNII WHSVYNQTRY EEVLDACLLR TDLDILPEGD
ATTIGSNGIM LSGGQKQRVS LARALYLETD FLLIDDILSG LDNSTGNDVF RRVFGPNGLM
RRRNATAILC THAIRYLPLA DHIIILATDG TVGEQGSFDK LAETGIYIPT LGLSDADDAS
STNSSIPVEE TVAATMPVPL TAFSTVSIGH LEAESRSTGD AKVYRHYYQS VNGWATMTCL
LSGIMYAVGR NFPSIWMGWW GSNSFDRTSS FYIGIMGLFR GLQIISLFLC ATAVVIFMTT
QSGKLLHNEI LNTLVNAPLR FFTTTDFGAV TNLFSQDMTL IDGELPISLL NTVIQIFDVF
AMAVVVAVGA PWLAIAYPVV FSIIYMLQMF YLRTSRQLRL LDLEAKSPLY AHFLDTIRGI
ATVRAQKLRD QEILFNQDLL NLSQRPAYLL AMAQRFLATF LNLIVMVLAV GVVAISTQLR
TNSGFAGSSL VTLMSWGESI SSLIQYYTQV EVSIGAVSRL KAFAQNVPSE NLDQEDLEPA
EEWPTQGDIA IRGVSASYKN DDESPASEDD EESPNLALED LTILVKPGQK VALCGRTGSG
KSSIILLLLR LLDPLSNQSE NIVIDGVPYN RVNRSILRRR LIAVPQDPVF LPDGSSIKEN
LDPFNVASDE ECLAVLEDVR LTKFATDHGS IHAGIRADEL SAGQKQLFSL GRAVLRRRVK
QRLFSIHGGV LLLDEVSSSV DSATDNLVQE IIKEEFADYT IVMVSHRLNI VMEYFDSVVV
LDRGRVVETG DPRDLAKTEG SWFSQLWAME KK
