LCSH_PURLI
ID LCSH_PURLI Reviewed; 1552 AA.
AC A0A179H0T5;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=ABC multidrug transporter lscH {ECO:0000303|PubMed:27416025};
DE AltName: Full=Leucinostatins biosynthesis cluster protein H {ECO:0000303|PubMed:27416025};
GN Name=lcsH {ECO:0000303|PubMed:27416025}; ORFNames=VFPBJ_02522;
OS Purpureocillium lilacinum (Paecilomyces lilacinus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX NCBI_TaxID=33203;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, FUNCTION,
RP AND INDUCTION.
RC STRAIN=PLBJ-1;
RX PubMed=27416025; DOI=10.1371/journal.ppat.1005685;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
CC -!- FUNCTION: ABC multidrug transporter; part of the gene cluster that
CC mediates the biosynthesis of the lipopeptide antibiotics leucinostatins
CC that show extensive biological activities, including antimalarial,
CC antiviral, antibacterial, antifungal, and antitumor activities, as well
CC as phytotoxic (PubMed:27416025). May be involved in the efflux of
CC leucinostatins (Probable). {ECO:0000269|PubMed:27416025,
CC ECO:0000305|PubMed:27416025}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is positively regulated by the leucinostatins
CC biosynthesis cluster-specific transcription regulator lcsF.
CC {ECO:0000269|PubMed:27416025}.
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; LSBH01000002; OAQ83754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A179H0T5; -.
DR SMR; A0A179H0T5; -.
DR EnsemblFungi; OAQ83754; OAQ83754; VFPBJ_02522.
DR Proteomes; UP000078240; Unassembled WGS sequence.
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; 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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1552
FT /note="ABC multidrug transporter lscH"
FT /id="PRO_0000446611"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 957..977
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1005..1025
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1076..1096
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1100..1120
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1184..1204
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1210..1230
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 280..559
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 639..884
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 963..1241
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1295..1538
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 573..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 676..683
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1328..1335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 719
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 834
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1028
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1552 AA; 169897 MW; 8158CA8D944E9859 CRC64;
MSAEAACSDD SFGPWAGATC RGGFDFTLLF EETILSILPS VLVIVVAPIP IIRLAREPPK
VRASALDWFK KISSICFITL SAALVGLWAR NSTITQTRAS TPSAVLTFVL SLVYVLLSTI
EHRLSLRPSS VLSFYLGLSV LFDIARTRTL FMLEDATHSA IPPVFASSLA LRVVMLLLES
TEKRSLLLAK YDNAAPESVG GPYNLGVFYW LSTLFFTGYR KILEIGDLYP LDDELRSTGL
AKKMSDAWRK VPDKAAPNVL FATWLKTFSK AMFMPVVPRL FQIGFTYAQP FLITAAIELA
ATPQTQPYNN NGYGLIGAYI LVYSGIAVSV GQYEWRNYRA ATMMRGSIIP LVYEKSLILD
SCSSATFHPT AALTLVSTDI ETITSGLVQI HETWSNLVEI GLAIYLLERQ LGAACVMSVG
FAIVVMVGTV FLARPTGTHL AAWIQASQVR VIETSKALAS IKWLKISGLT DVAFSVIQKL
RKQELVVSEK FRYLLGLSLI LSICTPILGP LLTFAVFAGI AAHGGSTLTI AKVFTAFSII
VLLNSPLAKI VQALPQISGS IASFQRIQDH LNAEERHDPR STTTGTSPES NNGSQQTLSD
KQATADGDTM ISISGKFSWR SETPAPGTGI TLVTGSDEGH LADTTPDANG DSRDAPVIDI
SPRLDIPRGA LTLILGPVGC GKSTLLKALL GELSSFDGVI EAKYSGAVTY CDQNPWLPNE
TVRDIIRGRS ATDTSDADSS EKADHDEDWY RVVVSACELQ RDMQIWPRGD RTPVGSKGIS
MSGGQKQRLS IARAVYARRA LVILDDVFSG LDANTEDVVF ENLLGNSGIL RKANMTVVLA
SSDVRRVPFA DKIVLLNQHG QVQHTGTPGD LKQVAELGWA DRDLDAQQEK PGKDELNHEH
GEYSESAPEK LRRSQTNHGA DNNAAVQEVL QAVESQADTA RQMGDSAVYK FYVKSAGWLT
ITIFVIAICV YAFCDSFPSV WLKWWAEANE KNPNSDLGKW LGVYAVLGVG AVAACLIGTW
QLFIITINRS GLYFHNLLVE TVSRAPMMFH STTDTGITVN RFSQDLQLID MELPSAALGV
VMALSFGIAQ FILVCVSSRY MAALLPFLLA VLYAIQHFYL RTARQLRLLD IEYKAPLYTQ
LMETISGVVT IRAFRWETQS TEKAIRILDT SQKPSYLLFC VQRWITFAVN MVIMMLAVIL
IVLTTTLREA IGPGYVGIAL SNILAFSATM QATITSWVTL EIALGAVARI RSFSMQVRSE
DDEARDGLAK AGLDARLVQP TPETVGERWP SQGRIELDNV TASYPSSGRV LHNITMIIEP
GQKVAICGRT GSGKSSLFLS LLGLIAQDSG SITIDSVDLA TLPREYLRSQ IVAVPQEAYI
LDGTVRLNAD PYHNKETLGS TDPPDSRDEQ IIDVLKRVGL WEKIATRGGL DMVIDDKFLS
QGQAQLMVLA RAMLRRDESR VLLLDEATSS LDEATTTLID EIVSTWFKDW TVLAIAHKLD
AILDYDRVAV LDAGRLVEYD QPRELLQRPT SIFKELYLLS TNQASLSSPD SN
