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Database: UniProt
Entry: A0A0A2W117_BEABA
LinkDB: A0A0A2W117_BEABA
Original site: A0A0A2W117_BEABA 
ID   A0A0A2W117_BEABA        Unreviewed;       729 AA.
AC   A0A0A2W117;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   13-SEP-2023, entry version 16.
DE   SubName: Full=Putative permease IIC component ywbA {ECO:0000313|EMBL:KGQ13856.1};
GN   ORFNames=BBAD15_g192 {ECO:0000313|EMBL:KGQ13856.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ13856.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ13856.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ13856.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA   Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGQ13856.1}.
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DR   EMBL; ANFO01000020; KGQ13856.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2W117; -.
DR   STRING; 1245745.A0A0A2W117; -.
DR   HOGENOM; CLU_379905_0_0_1; -.
DR   Proteomes; UP000030106; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR   CDD; cd04513; Glycosylasparaginase; 1.
DR   Gene3D; 3.60.20.30; (Glycosyl)asparaginase; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR000246; Peptidase_T2.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR004501; PTS_EIIC_3.
DR   InterPro; IPR004796; PTS_IIC_cello.
DR   NCBIfam; TIGR00359; cello_pts_IIC; 1.
DR   NCBIfam; TIGR00410; lacE; 1.
DR   PANTHER; PTHR33989; -; 1.
DR   PANTHER; PTHR33989:SF11; LICHENAN PERMEASE IIC COMPONENT; 1.
DR   Pfam; PF01112; Asparaginase_2; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51105; PTS_EIIC_TYPE_3; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        121..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        200..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        329..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        375..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..392
FT                   /note="PTS EIIC type-3"
FT                   /evidence="ECO:0000259|PROSITE:PS51105"
FT   ACT_SITE        562
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600246-1"
FT   BINDING         590..593
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600246-2"
FT   BINDING         613..616
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600246-2"
FT   SITE            561..562
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600246-3"
SQ   SEQUENCE   729 AA;  79575 MW;  BD3203EDD2A33B11 CRC64;
     MAQQRHLGAI RDAYISFMPF IIVGSILLVI SSFPSTHYQQ FMASVFGEGW SATVEIPFNA
     IFSTMAVFIS FLVAYRLAER YDIDRMSSGI LSLSCFLILT PFAKHPDVGN LIPMEWLGSK
     GLFVAMLGAL ASTELFAWML RQNWVIKMPD GVPPAVQKSF AALIPSLLIL IVALAVRVLF
     AKTDYHTIHQ FVYEVLATPI RHFGTSYIGA LFTCFSITSL WSVGINSGSM VNGILRPFWM
     ENQMDNLAAT QAGMPPPHVV TEQFYDMIWM GGAGATLSLV IAMLLFARSQ HIKNVSRLAV
     GSSIFNINEP VLFGLPVIMN PIMLIPFNLV PLVLVTVQYI AMSIGMVATT TGVYIPWTLP
     PVLSGFIVTG HLSGAVIQLI NLCIGALIYL PFLKVVDRQY RANESPAQVT EPNWGTIATW
     RMAWEGIGEA ADRLQRGSSA NDAVVHAVKC VEDYPFYKSV GFGGLPNEQG EVELDAAFMD
     GTSLALGAVA GVKNIANPIL VAKALSEERF NSFMVGQGAE AWAKDRGFES KTMLTERAYN
     HYLKRKRETL DRGLSPYTGH DTVGVIALDA QQRMSVATST SGLFMKRPGR VGDSPVSGSG
     FYADSEVGAA TATGLGEDLM KGCISYEIVS RMARGMSPQR AAESAVYDLE ARLIARYGRA
     GDLSVVCMNN RGEYGAATTI DNFSFSVATP AQPAQVFLTA RDGNRTVIRP ADREWLDAYQ
     QRITAEVIQ
//
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