ID   VERA_CLORO              Reviewed;        1261 AA.
AC   A0A1U9YI12;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=ABC-type transmembrane transporter verA {ECO:0000303|PubMed:28376389};
DE   AltName: Full=Verticillin biosynthesis cluster protein A {ECO:0000303|PubMed:28376389};
GN   Name=verA {ECO:0000303|PubMed:28376389};
OS   Clonostachys rogersoniana.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Bionectriaceae; Clonostachys.
OX   NCBI_TaxID=122658;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   PATHWAY.
RC   STRAIN=XZC04-CC-302;
RX   PubMed=28376389; DOI=10.1016/j.fgb.2017.03.007;
RA   Wang Y., Hu P., Pan Y., Zhu Y., Liu X., Che Y., Liu G.;
RT   "Identification and characterization of the verticillin biosynthetic gene
RT   cluster in Clonostachys rogersoniana.";
RL   Fungal Genet. Biol. 103:25-33(2017).
RN   [2]
RP   INDUCTION.
RX   PubMed=29058652; DOI=10.1099/mic.0.000557;
RA   Guo Z., Hao T., Wang Y., Pan Y., Ren F., Liu X., Che Y., Liu G.;
RT   "VerZ, a Zn(II)2Cys6 DNA-binding protein, regulates the biosynthesis of
RT   verticillin in Clonostachys rogersoniana.";
RL   Microbiology 163:1654-1663(2017).
CC   -!- FUNCTION: ABC-type transmembrane transporter; part of the gene cluster
CC       that mediates the biosynthesis of 11'-deoxyverticillin A, one of the
CC       dimeric epipolythiodioxopiperazines (ETPs) from the verticillin family
CC       that are toxic secondary metabolites (PubMed:28376389). The verA
CC       multidrug transporter is probably involved in the secretion of 11'-
CC       deoxyverticillin A (Probable). {ECO:0000269|PubMed:28376389,
CC       ECO:0000305|PubMed:28376389}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is regulated by the cluster-specific regulator
CC       verZ. {ECO:0000269|PubMed:29058652}.
CC   -!- DISRUPTION PHENOTYPE: Dicreases the production of 11'-deoxyverticillin
CC       A. {ECO:0000269|PubMed:28376389}.
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; KY359203; AQZ42156.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1U9YI12; -.
DR   SMR; A0A1U9YI12; -.
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   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   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; 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; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW   Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1261
FT                   /note="ABC-type transmembrane transporter verA"
FT                   /id="PRO_0000450159"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        686..706
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        734..754
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        808..828
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        830..850
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        913..933
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        950..970
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          41..334
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          374..618
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          691..976
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1017..1255
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         409..416
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1052..1059
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        396
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        463
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1007
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1021
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1261 AA;  138053 MW;  874D6EA5CFC963BD CRC64;
     MPIDAESEAE LRSEAEAPPG GFGKLMRVFT FATAVDRLIQ IGCAFAAVCS GAAMPLMALI
     LGRLTANFTD YGSSGDDKST AEFMKSVQTN ALWFVYLFIG KFTLVYLWSF GFTFTASRML
     QAMRLTCLDR ILDRTVAAND EETPGSLSNT VTSQCNSIQA ALSDRLGIMI QAFSMLLASF
     AVAFSQSWQL TLVMLGLVII TLGLIGFIVS SDQKIEAGLL KRYAECSIIA EDALGSIRTV
     IAFGAAHKFL AKYNEILKKT ETDGKKKGPF VGLMFACQYF FMFVGWAIGF YLGAYLFTKG
     MISDPGRILS VFFAMLIGLG AIMALGPNMP SFIKAIAAAD VAFKILDDGT DQNQDSESQK
     DASQPEKIAC QGHVELRDMS FAYRGREDRN ALDKINLSFE RGTSTAIVGP SGAGKSTLIS
     LLERWYEPTA GSIFLDGNDI FQLDPKWLRS QIALVQQEPQ LFNASIFDNI AYGLIGTEQE
     NLSPEDKQTL VHDACRHARA YEFITKLPES FDTMVGDRAS LISGGQKQRI AIARALVARR
     PILLMDEATS ALDNENSKVI EALMTNSIDR TTIFISHKIR AATKADRVVV LDHGKVSEQG
     THEELLSAGG LYKRLYDAQT EVESSDDEDP IKTITKTPIP TVVEKTEEAS GGPQASIAEP
     SDNLPQIPKR NLLANLWEIA KEQRRYWPIF LIGLVACVVT AQIFPVQAIL LGRVMQVFQG
     PPEKVSSDAN FWSLMFFVVG LGAMISYAIL GFFMTLLGVY LTRFYRLEYF RAVLQQPVEF
     FDRVASGTLL SRLSSDPSNL HELISINMGL LISIFVSVIS ASIIGLAYSW KFALVAIFAA
     MPAVFAAGYL RMKLDSSLAE EMEKISEESA RFVSDSLSAF RTVKAFTMET AVHHMYNECL
     VSFAGRLYRQ RAVMTLFFAF SESVELLASA LGFWYGGKLM GDGELSTEKF FTVFIAVVVG
     GQAAGALFGF SSNLGKAKIA ANNILGIRSQ VRAAAARDQS RQMAEENHSE KTENTVVDMQ
     NVTFAYPARP NVPVLKGISF KVYRGQTVGV VGTSGSGKST LLALLERFYE AQSGTVNVLG
     RPISAHDIDE YRKRLAIVPQ EPQLYNGTVR DNVILGLDED KVQEADVATA CEAAGLGEFI
     SSLPDGFNTQ CRGQGVSFSG GQKQRVAIAR ALIMHPELLL LDEPTSALDA ESEQLVRETL
     GNIQEGRTMI LVTHRLNIVR NAHVIIVMDG GRIVEQGTHT ELMAKQGNYF KMHESSNGGE
     A