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Database: UniProt
Entry: A0A1S2LI65_9BACI
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ID   A0A1S2LI65_9BACI        Unreviewed;       474 AA.
AC   A0A1S2LI65;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=PTS system mannitol-specific EIICB component {ECO:0000256|ARBA:ARBA00021825};
DE            EC=2.7.1.197 {ECO:0000256|ARBA:ARBA00011909};
DE   AltName: Full=EIICB-Mtl {ECO:0000256|ARBA:ARBA00033349};
GN   ORFNames=BKP37_14435 {ECO:0000313|EMBL:OIJ12076.1};
OS   Anaerobacillus alkalilacustris.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX   NCBI_TaxID=393763 {ECO:0000313|EMBL:OIJ12076.1, ECO:0000313|Proteomes:UP000179524};
RN   [1] {ECO:0000313|EMBL:OIJ12076.1, ECO:0000313|Proteomes:UP000179524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18345 {ECO:0000313|EMBL:OIJ12076.1,
RC   ECO:0000313|Proteomes:UP000179524};
RA   Bassil N.M., Lloyd J.R.;
RT   "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT   Anaerobacillus genus.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (sugar PTS), a major carbohydrate active transport system,
CC       catalyzes the phosphorylation of incoming sugar substrates
CC       concomitantly with their translocation across the cell membrane. The
CC       enzyme II CmtAB PTS system is involved in D-mannitol transport.
CC       {ECO:0000256|ARBA:ARBA00002434}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannitol(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC         mannitol 1-phosphate(in) + L-histidyl-[protein];
CC         Xref=Rhea:RHEA:33363, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC         ChEBI:CHEBI:16899, ChEBI:CHEBI:29979, ChEBI:CHEBI:61381,
CC         ChEBI:CHEBI:64837; EC=2.7.1.197;
CC         Evidence={ECO:0000256|ARBA:ARBA00001655};
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:OIJ12076.1}.
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DR   EMBL; MLQR01000033; OIJ12076.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S2LI65; -.
DR   OrthoDB; 9814222at2; -.
DR   Proteomes; UP000179524; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0022872; F:protein-N(PI)-phosphohistidine-mannitol phosphotransferase system transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   CDD; cd05567; PTS_IIB_mannitol; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   InterPro; IPR036095; PTS_EIIB-like_sf.
DR   InterPro; IPR013011; PTS_EIIB_2.
DR   InterPro; IPR003501; PTS_EIIB_2/3.
DR   InterPro; IPR029503; PTS_EIIB_mannitol.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013014; PTS_EIIC_2.
DR   InterPro; IPR004718; PTS_IIC_mtl.
DR   NCBIfam; TIGR00851; mtlA; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF52794; PTS system IIB component-like; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR   PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
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        20..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        57..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        91..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        138..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        166..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        274..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        318..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          18..335
FT                   /note="PTS EIIC type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51104"
FT   DOMAIN          387..474
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51099"
SQ   SEQUENCE   474 AA;  49860 MW;  8851B3E237256A81 CRC64;
     MMNNTSSNKG FRVKVQRFGS YLSGMIMPNI GAFIAWGLIT ALFIPTGWLP NESLAELVGP
     MIIYLLPLLI GFTGGKMIYD VRGGVVGATA TMGVIVGADI PMFLGAMIMG PLGGYLIKKF
     DQKIDGKVRQ GFEMLVNNFS AGILAGVLTL VAFKAIGPVV LGLNQFLAAG VEGIIGAGLL
     PVASIFIEPA KVLFLNNAIN HGILSPIGIE QAAQTGKSIL FLLETNPGPG LGILLAYMVF
     GKGMAKQSSP GAAIIHFFGG IHEIYFPYIL MKPALLIAAI AGGASGVFTF NLFSAGLVAA
     PSPGSIFALV AMTPRGDYFA VLSGVVVATA VSFVISSLIL KASKQNEETN DLANAAEKMQ
     GMKGKKSETA ASLVKEETKE INKENVRKVI FACDAGMGSS AMGASVLKNK FKKAGLDITV
     SNTSINNLPA DADLVVTHQD LTDRAKAKLP NAQHISVENF LNSPKYDELV ENLK
//
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