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Database: UniProt
Entry: A0A3M7TP63_9BACI
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ID   A0A3M7TP63_9BACI        Unreviewed;       479 AA.
AC   A0A3M7TP63;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=EBO34_11840 {ECO:0000313|EMBL:RNA67424.1};
OS   Alteribacter keqinensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacter.
OX   NCBI_TaxID=2483800 {ECO:0000313|EMBL:RNA67424.1, ECO:0000313|Proteomes:UP000278746};
RN   [1] {ECO:0000313|EMBL:RNA67424.1, ECO:0000313|Proteomes:UP000278746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KQ-3 {ECO:0000313|EMBL:RNA67424.1,
RC   ECO:0000313|Proteomes:UP000278746};
RA   Wang H.;
RT   "Bacillus Keqinensis sp. nov., a moderately halophilic bacterium isolated
RT   from a saline-alkaline lake.";
RL   Submitted (OCT-2018) 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:RNA67424.1}.
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DR   EMBL; RHIB01000002; RNA67424.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M7TP63; -.
DR   OrthoDB; 9814222at2; -.
DR   Proteomes; UP000278746; 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   Reference proteome {ECO:0000313|Proteomes:UP000278746};
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..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        84..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        137..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        273..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        316..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          17..353
FT                   /note="PTS EIIC type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51104"
FT   DOMAIN          392..479
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51099"
FT   REGION          365..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..386
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   479 AA;  50586 MW;  BB06DAAA661B4973 CRC64;
     MAEEKKKSSV KARVQKFGSF LSGMIMPNIG AFIAWGLITA LFIPTGWLPN ETFEQLVGPM
     ITYLLPLLIA YTGGKIIYDV RGGVVGAIAT MGVIIGADIP MFLGAMIMGP LAGFIIKKID
     NVFLPKVRQG FEMLYNNFSA GILGALLAML GVIGIGPVIV AFTTVLAGGV QVIVNAGLLP
     LVSIFIEPGK VLFLNNAINH GILSPLGAEQ ALQEGKSILF MLETNPGPGL GILLAYMVFG
     KGMARQSASG ASVIHFFGGI HEIYFPYILM KPLLILAAIG GGMSGIFVFT LFNAGLSSSP
     SPGSIIAYTL LTPQGNFLGV YAGVIVATVV SFLIASVILK RGAPDDEGDL QGAAAKMQDM
     KGKKSAAVGS QADSEKEEKE TVEHSKADAE VNKVVFACDA GMGSSAMGAS ILRNKFKKES
     IDIEVTNTSI SNLPADADIV ITHKDLTERA KDKLPDADHI SVDNFLGSPK YDELVKRLK
//
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