TR06_CURCL
ID TR06_CURCL Reviewed; 1338 AA.
AC A0A348AXX9;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=ABC-type transporter TR06 {ECO:0000303|PubMed:29686660};
DE AltName: Full=KK-1 biosynthesis cluster protein 6 {ECO:0000303|PubMed:29686660};
GN Name=TR06 {ECO:0000303|PubMed:29686660}; ORFNames=TRAF135006;
OS Curvularia clavata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Curvularia.
OX NCBI_TaxID=95742;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=BAUA-2787;
RX PubMed=29686660; DOI=10.3389/fmicb.2018.00690;
RA Yoshimi A., Yamaguchi S., Fujioka T., Kawai K., Gomi K., Machida M.,
RA Abe K.;
RT "Heterologous Production of a Novel Cyclic Peptide Compound, KK-1, in
RT Aspergillus oryzae.";
RL Front. Microbiol. 9:690-690(2018).
CC -!- FUNCTION: ABC transporter; part of the gene cluster that mediate the
CC biosynthesis of KK-1, a novel cyclic decapeptide compound with potent
CC antifungal activity (PubMed:29686660). Is probably directly involved in
CC the secretion of KK-1 (Probable). {ECO:0000269|PubMed:29686660,
CC ECO:0000305|PubMed:29686660}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:29686660};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LC371755; BBC83962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A348AXX9; -.
DR SMR; A0A348AXX9; -.
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 Gene3D; 1.20.1560.10; -; 1.
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; 3.
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; Hydrolase; Membrane; Nucleotide-binding;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1338
FT /note="ABC-type transporter TR06"
FT /id="PRO_0000450433"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 777..797
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 816..836
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 895..917
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 919..941
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 1037..1057
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 80..372
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 405..706
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 777..1063
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1096..1333
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 440..447
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1130..1137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1338 AA; 146396 MW; C5588150462B003E CRC64;
MSAIELPPLR SRSEEAARAE HNAQTLAHEN ANIAGYDESP AVQQVETDAP ETKGAPQASF
KNYFRVFSYG TKLDYFLISL CCFTSIGAGT AMPLMNIVFG KLVGNFTDYF IPGSNVTRQE
FEAEINKLAL YIFYLFIGKF AMSYISMLAI RISGMRISAA LRLAYLRALF AQPVSVIDTV
SPGKVANRIT TSSNIVQLAI SQHFATLFQS LAFTVGLYVV ALVKGWKLTL IASTGLPFIL
IVYGAMFPPF LRIHQITDKF QEEASAMAYE MFSSIRMIVA FGTESRLAKQ HGVMLSKAAS
NEKRAAPLMG LTMSPAMVAM YGIFGITFWF GIKEYTKGRI SSVGDITVVL FSVMMAVMNI
GRVASPIISI AKAATAATEL FVTIDASFHD TSGVMEPEVT GNAAITFINV AFSYPSRPGV
PILKGLDLTI TAGKVTAIVG PSGSGKSTIV GLIQRWYDLL GTTATAKKID ETEIPSSSTM
ASSPIEAVYD NTDKKSKKGK AGEEEEPEQD LGPNTCTGSL SVGRTNLRNV DVRWWRSQIG
MVQQEPFLFN DTIYNNIVFG LCGTRYEGLS KDEKKIMVDE ACREACAEEF ISRLPQGLDT
LVGESGIKLS GGQRQRIAIA RSIIKRPPIL ILDEATSAID VRTERIVQEA LDRVSKNRTT
IVIAHRLSTI KRADSIVVLR QGQLVEQGTH EELLKNGDGV YYGLVHAQEL EMDAEDDDDH
SSSLENIKMN DTKEDTASSG FEGHASREDS TYQNVGLLHS LGRLVVEQRH HWILYSVCCI
GILGAGAVYP LQAYIFARII NVFTLTGPEL VKQGNFWAGM FGVLAGGVGL SYYLLGAASH
LISVELTRKY RSEYLSNMIR KPILFFDDKV HSPGSLTSRL SSDSQQVQQL LSMEMSMALI
ACTNLLGCTI IAFVYGWKLS LVGLFAALPL ILGAGLVRTR LEIQLEAENA KVFENSSQFA
TEAVAGFRTV LSLLMEPMIR SRYDKLLKGH VVEALAKAKY GTIIFAASDS LELACMSLTF
WYGGKLLASR EYDLIQFFIV YTAIIQGATA AGIWFSFTPS MAQATGAANR ILSMRPTSTD
PSSYSPLPCS DEGVGIEFQH VSFKYQSRDV PVLSNLNLQI LPGQVAALVG SSGCGKSTTL
SLLERFYDAS SGHILYNGQD ITTFSPAEYR KQMSLVSQEP TLYQGSIREN ISLSVESASD
DDIKQACRDA QIHDFITSLP EGYETRLGPK GMSLSGGQRQ RISLARALLR KPKILLLDEA
TSSLDSESEK YVQEAIERAA SEGDRTVIIV AHRLATIQKA DVIFVLGSGK VLEKGDHQAL
LRKKGVYWQM CQAQALNR
