GLOK_GLAL2
ID GLOK_GLAL2 Reviewed; 1323 AA.
AC S3D778;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=ABC transporter gloK {ECO:0000303|PubMed:25270390};
DE AltName: Full=Pneumocandin biosynthesis cluster protein K {ECO:0000303|PubMed:25270390};
GN Name=gloK {ECO:0000303|PubMed:25270390};
GN Synonyms=GLTRT {ECO:0000303|PubMed:25879325}; ORFNames=GLAREA_10036;
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, AND
RP FUNCTION.
RC STRAIN=ATCC 20868 / MF5171;
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
RN [2]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=25270390; DOI=10.1002/cbic.201402175;
RA Houwaart S., Youssar L., Huettel W.;
RT "Pneumocandin biosynthesis: involvement of a trans-selective proline
RT hydroxylase.";
RL ChemBioChem 15:2365-2369(2014).
RN [3]
RP IDENTIFICATION.
RX PubMed=25879325; DOI=10.1021/acschembio.5b00013;
RA Li Y., Chen L., Yue Q., Liu X., An Z., Bills G.F.;
RT "Genetic manipulation of the pneumocandin biosynthetic pathway for
RT generation of analogues and evaluation of their antifungal activity.";
RL ACS Chem. Biol. 10:1702-1710(2015).
CC -!- FUNCTION: 3-isopropylmalate dehydratase large subunit; part of the gene
CC cluster that mediates the biosynthesis of pneumocandins,
CC lipohexapeptides of the echinocandin family that prevent fungal cell
CC wall formation by non-competitive inhibition of beta-1,3-glucan
CC synthase (PubMed:23688303, PubMed:25270390). Possibly secretes
CC antifungal pneumocandins, thus avoiding of intracellular accumulation
CC and ameliorating the toxicity to the producing cells (PubMed:23688303).
CC {ECO:0000305|PubMed:23688303, ECO:0000305|PubMed:25270390}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) 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; KE145356; EPE34342.1; -; Genomic_DNA.
DR RefSeq; XP_008078277.1; XM_008080086.1.
DR AlphaFoldDB; S3D778; -.
DR SMR; S3D778; -.
DR EnsemblFungi; EPE34342; EPE34342; GLAREA_10036.
DR GeneID; 19469083; -.
DR KEGG; glz:GLAREA_10036; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_5_1; -.
DR OrthoDB; 138195at2759; -.
DR Proteomes; UP000016922; 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 GO; GO:0016787; F:hydrolase activity; 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; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Hydrolase; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1323
FT /note="ABC transporter gloK"
FT /id="PRO_0000444492"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 748..768
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 795..815
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 821..841
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 859..879
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 891..910
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 976..996
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 1006..1026
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 142..380
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 471..697
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 752..1031
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1069..1300
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 503..510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1103..1110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1323 AA; 145672 MW; 02DDA7758D4FB21B CRC64;
MPENTAIASI FTAIVCFKFI ILTLEAKEKS NLIRPEFKHP SPEQAAGILN RSFFWWFNPL
LLTGSKQRLA VDDLFFNDDG LTFDAWRDII TRRWAKADIS KPHALLKVML ATFKGLLLAG
ILPRLCLTGP ETTTSNKVAY GLIAAYAIVY IGIAVMSTMS QHKNYRTIVA IRGSAVSLIY
QHTLRLTSSS TSTSSSLTLI NNDVERMGHG MREVHEIWAS LIEIALSLWL LEVRLGVSVV
AAVFVIIGNI CTLLGCVFGF VKMGLLLGDR QKVWLEAIEK RTSSTIATLG SIRGIKSTGA
TDIVQRITTR LRLDEIRISL KYRELLVGIV TLSYVSTTMA PVFAFATYSI ISNSRGTTPL
LAASAYTSLT IFSLLGQAVS KWISSSVDII TTIACLERVR QYLATNLRVD PRTIESYIKP
IDSSNSPRLR NSDISQTEML DMGSVDQSQY HPNSVGEVLR EVPLAKMMIT IRDCSACWSK
GSEMAISEIN LTILKGSLAM VIGPIGSGKS TLLKVILGEM PHTTGTVIVG RSEAAFCGQS
PWLTNVSVRN NIIGVSYLDA NWYNTVVNAC ALDRDFEQLP DGDNTVIGSK GVLLSGGQKS
RLALARALYA RNDLVILDDV FSGLDAKTEQ RVFESVLGSH GILRQGGTTT VLATNSVRNI
SLADHIVVMG SDGKITDQGT YQNLVFASSY LESLGTRQKT LNISDSEKSK DDTVSGLAVA
SAMHQPVDSD NRGDKDLTIY KYYIDTVGWV TWWVFVLLCS GFVFGLVFPQ IWIQFWTEAN
ARQANYRLAY YLSLYALWPL MAIVIFLGAC AWLMIRMVSK AAIQFHGILL NSALSAPLVY
FSTTDSGEVS NRFTQDLNLI DMELPTALIG TTVTFLSCIA QIGVIIYGSS YVAAAIPALI
VFLYYIQLFY LRTSRQLRLL ELEAKAPLLS HFMESIHGLV TIRAFGWTEK FTHQNHDLLE
RSQRPFYLLY CAQRWLNLTL ELAVAFLAII LVSIALTTRE SSGAKIGVAL LSIVGFGLNL
KTLVYTWTSL EIAMGAVSRI RHFAINTSSE DLPGEDRTLP PDWPHEGVIR FQSVSAAYSP
TSHPVLNDLS FTVKAGTKVA ICGRTGSGKS STLAALLRLI DLRSGAITID GIDISTVVRQ
DLRSKLITLP QEPFYYHASI RDNLDVRGQF STEELLDILE VVGMREVIDK KGGLDAMANA
DVLSHGQSQL LCLARAILRP NKILILDEAT SSVDKKTEEK MVDIIREKFQ DRTVISVAHN
LNTIMDYDEV IVLEAGRIIE QGKPLALALE PSFFASLLKA ADGESEDALE EETISNIASP
RSR
