ID   CLAG_PENCR              Reviewed;         743 AA.
AC   A0A481WQK1;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   05-JUN-2019, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=ABC-type transporter claG {ECO:0000303|PubMed:30811183};
DE   AltName: Full=Clavatol biosynthesis cluster protein G {ECO:0000303|PubMed:30811183};
GN   Name=claG {ECO:0000303|PubMed:30811183};
OS   Penicillium crustosum (Blue mold fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=36656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=PRB-2;
RX   PubMed=30811183; DOI=10.1021/jacs.9b00110;
RA   Fan J., Liao G., Kindinger F., Ludwig-Radtke L., Yin W.B., Li S.M.;
RT   "Peniphenone and penilactone formation in Penicillium crustosum via 1,4-
RT   Michael additions of ortho-quinone methide from hydroxyclavatol to gamma-
RT   butyrolactones from Crustosic Acid.";
RL   J. Am. Chem. Soc. 141:4225-4229(2019).
CC   -!- FUNCTION: ABC-type transporter; part of the cla gene cluster that
CC       produces clavatol and ortho-quinone methide (PubMed:30811183). The
CC       clavatol biosynthesis cluster cla and the terrestric acid cluster tra
CC       are both involved in the production of peniphenones and penilactones
CC       (PubMed:30811183). {ECO:0000269|PubMed:30811183}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC       {ECO:0000305}.
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DR   EMBL; MK360918; QBK15045.1; -; Genomic_DNA.
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; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR043926; ABCG_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF19055; ABC2_membrane_7; 2.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glycoprotein; Membrane; Nucleotide-binding; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..743
FT                   /note="ABC-type transporter claG"
FT                   /id="PRO_0000455059"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        507..527
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        560..580
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        611..631
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        636..656
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        661..681
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          200..439
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         234..241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   743 AA;  81201 MW;  75B0B9909DCECE22 CRC64;
     MSSNSSCLVT NQGGALPLTA TCLEGFYCPN NSLENPPEIC PPTPQCRLTR LQEYHNICDH
     AQGTYEPIVC QPGFYCPSGG KRQIPCPKGH FCPLGTVEPF KCFGLSSCAE GSEREIPLAG
     LLCSILLDIF LVIVVSWPFP FAWIRQLSRG KLRRGAGGND SESGVISAGR REISFSESKY
     HVSQFFTSDG SHGTAAGIEV EFSGISMRPT RSGIETLCLQ NGVIRAGSFV GVMGPSGSGK
     STLVKVLTGR AQPTTGSVLI NGDTCRAAEL RDLLALVPQD DIILPDLTVQ ENILYSSRVR
     IGSSRKDSEI EQYVDHLIIS LGLNKVRNRL IGEVGKRGLS GGERKRVNIA LELAAVPGII
     VLDEPTSGLD AMTALSVIEL LKSLTKQGVI VICVIHQPRL EIFAALDDLL LLNHGRQVYF
     GSAAAAKQCF QDAGYTFPLN SNPTDTMMDI MSCHDNLHLT DYPRNKPALP KQNLRIVLQS
     VKKIRAPWYC QVLLAFMRGT KQQTRQYPSF VLEILTGAGC GILIGLSNYE FKGHLFQGLF
     HLPFQLLSSP VSYRLLTEQG MLLCLTIGCA AGPAGVKTFG EEKLVFLRES CSGYSEGAYF
     LGKALSTLIR IFLSALHFTS FYLILTTPIV SFPNQLIVNL LYFYCIYGAA SMISAITSPK
     NGPLITMLTS VLFCALSGCA PRLASVKSWN LAWLWYICPA VWIAEANFNQ YTDPLAYLYD
     IKPAAEDAIR AWDRLSLHSL FIV