ECDL_ASPRU
ID ECDL_ASPRU Reviewed; 1479 AA.
AC K0E4D9;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=ABC transporter ecdL {ECO:0000303|PubMed:22998630};
DE AltName: Full=Echinocandin B biosynthetic cluster protein L {ECO:0000303|PubMed:22998630};
GN Name=ecdL {ECO:0000303|PubMed:22998630};
OS Aspergillus rugulosus (Emericella rugulosa).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41736;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 58397 / NRRL 11440;
RX PubMed=22998630; DOI=10.1021/ja307220z;
RA Cacho R.A., Jiang W., Chooi Y.H., Walsh C.T., Tang Y.;
RT "Identification and characterization of the echinocandin B biosynthetic
RT gene cluster from Emericella rugulosa NRRL 11440.";
RL J. Am. Chem. Soc. 134:16781-16790(2012).
CC -!- FUNCTION: ABC transporter; part of the gene cluster that mediates the
CC biosynthesis of echinocandin B, a fungal lipidated cyclic hexapeptide
CC that acts as an antifungal agent (PubMed:22998630).
CC {ECO:0000305|PubMed:22998630}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- BIOTECHNOLOGY: Due to their effectiveness as antifungal agents,
CC echinocandin derivatives can be used for the treatment of human
CC invasive candidiasis (PubMed:22998630). {ECO:0000269|PubMed:22998630}.
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; JX421684; AFT91383.1; -; Genomic_DNA.
DR AlphaFoldDB; K0E4D9; -.
DR SMR; K0E4D9; -.
DR TCDB; 3.A.1.208.41; the atp-binding cassette (abc) superfamily.
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; 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; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1479
FT /note="ABC transporter ecdL"
FT /id="PRO_0000443850"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 365..382
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 885..905
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 955..975
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1028..1048
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1052..1072
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1135..1155
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1165..1185
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 258..535
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 607..835
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 932..1193
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1230..1461
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1460..1479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 641..648
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1264..1271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 793
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1479 AA; 162954 MW; 45AF7AC776A9452F CRC64;
MDDSPWPQCD IRVQDTFGPQ VSGCYEDFDF TLLFEESILY LPPLLIAASV ALLRIWQLRS
TENLLKRSGL LSILKPTSTT RLSNAAIAIG FVASPIFAWL SFWEHARSLR PSTILNVYLL
GTIPMDAARA RTLFRMPGNS AIASIFATIV VCKVVLLVVE AMEKQRLLLD RGWAPEETAG
ILNRSFLWWF NPLLLSGYKQ ALTVDKLLAV DEDIGVEKSK DEIRRRWAQA VKQNASSLQD
VLLAVYRTEL WGGFLPRLCL IGVNYAQPFL VNRVVTFLGQ PDTSTSRGVA SGLIAAYAIV
YMGIAVATAA FHHRSYRMVM MVRGGLILLI YDHTLTLNAL SPSKNDSYTL ITADIERIVS
GLRSLHETWA SLIEIALSLW LLETKIRVSA VAAAMVVLVC LLVSGALSGL LGVHQNLWLE
AMQKRLNATL ATIGSIKGIK ATGRTNTLYE TILQLRRTEI QKSLKFRELL VALVTLSYLS
TTMAPTFAFG TYSILAKIRN MTPLLAAPAF SSLTIMTLLG QAVSGFVESL MGLRQAMASL
ERIRQYLVGK EAPEPSPNKP GVASTEGLVA WSASLDEPGL DPRVEMRRMS SLQHRFYNLG
ELQDGLIVLQ NHTASWEKAS KPVLTDINVT ITRGSFVIVI GPIGSGKSTL LHSILGEVPH
TTGIRTIQEV DTAFCAQTPW LTNTNVRDNI LGASHFDPAW YNAVVKACAL HRDFAQLPHG
DRSMIGSKGI LLSGGQKGRL ALARALYARK ALLVLDDVFA GLDPKTGQEV FTSLFGARGL
LRQGKTTTVL ATNSTQNLSM ADYIMVLGSE GRLIEQGTPT ELLNSGSSLR LEELVKTREG
KSKAEPERER PEYARALRNS VLGATPVAAR RRFSDMAIYK LYIRTIGWGS WWIFIVLCSG
FVVALTLSRE NTLALPSACA GVDLLTACLE EIWLKFWTEA NARNPHDRLG YYLSLFAVWS
ALAITFFLGA CLHLMLRMVP KAAKIFHGSL LQTVMRAPLV FFSKTDSGEI SNHFSQDLEL
IDMELPRALI GAVIALILCI SAMAVIVYSS NYLAATIPGL LGLLYLVQMF YLRTSQQLRV
LELETRAPLL SHYMETIQGL VSLRAFGWSK HFKDRHHGHL KVAQQSAYLL FCAQIWLTLT
LDIIVAFLAI ILVSIAVTVK NSSAASIGLA LVNLIAFGAN MKGLVYNWTA LENAMGAIAR
VRDFTTETPC EIQVGESHSP SPGWPQRGLI KFKSVTASYD FTSHPVLNDV TFTVQPGEKL
AICGRTGCGK SSLVSSLLRL LEVRNGAIEV DGIDISTLSR EDVRMSLNVL PQEPFFYHGT
IRQNLDPNCL SSDEEILETL ALLGLREVIS KKGGLDVAMD DGFLSHGQQQ LLCLARAILK
KSRILILDEV TSSVDQETET LITRVLRDRL QDQTVISIAH RLNTIMDYDK VIILDKGCIV
EQGNPQVLAL QRSIFASLLR SGDEEPGNGH KHESEGEEE
