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HPM6_HYPSB
ID   HPM6_HYPSB              Reviewed;         564 AA.
AC   B3FWS2;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Efflux pump hmp6 {ECO:0000303|PubMed:18567690};
DE   AltName: Full=Hypothemycin biosynthesis cluster protein hpm6 {ECO:0000303|PubMed:18567690};
GN   Name=hpm6 {ECO:0000303|PubMed:18567690};
OS   Hypomyces subiculosus (Nectria subiculosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Hypomyces.
OX   NCBI_TaxID=193393;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=DSM11931, and DSM11932;
RX   PubMed=18567690; DOI=10.1128/aem.00478-08;
RA   Reeves C.D., Hu Z., Reid R., Kealey J.T.;
RT   "Genes for the biosynthesis of the fungal polyketides hypothemycin from
RT   Hypomyces subiculosus and radicicol from Pochonia chlamydosporia.";
RL   Appl. Environ. Microbiol. 74:5121-5129(2008).
RN   [2]
RP   FUNCTION.
RX   PubMed=20222707; DOI=10.1021/ja100060k;
RA   Zhou H., Qiao K., Gao Z., Meehan M.J., Li J.W., Zhao X., Dorrestein P.C.,
RA   Vederas J.C., Tang Y.;
RT   "Enzymatic synthesis of resorcylic acid lactones by cooperation of fungal
RT   iterative polyketide synthases involved in hypothemycin biosynthesis.";
RL   J. Am. Chem. Soc. 132:4530-4531(2010).
CC   -!- FUNCTION: Efflux pump that might be required for efficient secretion of
CC       hypothemycin or other secondary metabolies produced by the hypothemycin
CC       gene cluster (PubMed:18567690). {ECO:0000269|PubMed:18567690}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC       family. {ECO:0000305}.
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DR   EMBL; EU520417; ACD39756.1; -; Genomic_DNA.
DR   EMBL; EU520418; ACD39765.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3FWS2; -.
DR   SMR; B3FWS2; -.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 2.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..564
FT                   /note="Efflux pump hmp6"
FT                   /id="PRO_0000437600"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        361..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        395..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        452..472
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        322
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   564 AA;  60346 MW;  E8CC53E2129DFEDC CRC64;
     MEKHAEPEKS LGDKEFQEKE LHEKPAPAAS EDISGDSSVN KEDGPDPIND NYLSGLRLAV
     VMFALCISNF LVALDTTILA TAVPKISSDF NSLQDVGWYT SSYLLTNCAF QLFYGKLYTR
     FKVKIVFTVA MIIFEIGSLL CGVAPNSPVF IFGRAIAGLG SAGAFSGALI IVIHSVQAEK
     RAQYSGMIVG MYGLASVAAP LIGGAFTDHV TWRWCFYINL PCGGVAIAGL LFFFHSPPQA
     AVKETAAGLW AKIAKFDPFG TFFFLCSMIC LLLALQMGGS TYPFTDARII VLLVLFGLLL
     VAFIVVQFFD KNATIPPRVM KNRSVAFGMI YMFCVGAQFL VLVTFMPIWF QGVRAMSATD
     SGIRSLPILL SNTFCVVLAG ALVSMTGYYI PFMWASVVLT SIGAGLLTTL TVDASTGKWV
     GYQIIAGIGG GLGYQQGISV AQTVLKGSDM TIGTAVMVFV QLLGGTILVS AANNILVTRL
     VENLERLAPH INPEIILRAG ASGIKTAVSE ADYPFVIEAY NIALTKTFQI ALIVSCLGAI
     GAAGVEWKRG SKKGDSDEPA IMAV
 
 
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