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Database: UniProt
Entry: A0A2C1YLZ3_9BACI
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ID   A0A2C1YLZ3_9BACI        Unreviewed;       475 AA.
AC   A0A2C1YLZ3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=COD92_30355 {ECO:0000313|EMBL:PGV46002.1};
OS   Bacillus sp. AFS037270.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2033499 {ECO:0000313|EMBL:PGV46002.1, ECO:0000313|Proteomes:UP000225442};
RN   [1] {ECO:0000313|EMBL:PGV46002.1, ECO:0000313|Proteomes:UP000225442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS037270 {ECO:0000313|EMBL:PGV46002.1,
RC   ECO:0000313|Proteomes:UP000225442};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT   roles of natural products in bacterial physiology.";
RL   Submitted (SEP-2017) 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:PGV46002.1}.
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DR   EMBL; NUNF01000104; PGV46002.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C1YLZ3; -.
DR   Proteomes; UP000225442; 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        21..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        57..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        137..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        222..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        255..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        320..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          21..352
FT                   /note="PTS EIIC type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51104"
FT   DOMAIN          387..475
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51099"
SQ   SEQUENCE   475 AA;  49889 MW;  79615BA3EF8020E1 CRC64;
     MKVPNETAKE KSDVKVKIQK FGSYLSGMVM PNIGAFIAWG LITALFIPTG WIPNKDLATL
     VGPMITFLLP LLIGFTGGRM VYDIRGGVVG ATATMGVIVG TDIPMFLGAM IMGPIGGLVI
     KKFDKLIEGK VKSGFEMLVN NFSAGILGGA LTLLAYKGVG PVVEALSKFL ASGVQFIVDH
     NMLPLANIFI EPAKVLFLNN AINHGILSPL GIEQATKAGK SILFLLETNP GPGLGILLAY
     WLFGKGTAKQ TAPGAVIIHF LGGIHEIYFP YILMKPMLIF AAMAGGVSGV FTFNILHAGL
     VAAPSPGSIF ALLAMTPKGG YFATLAGVIV ATAVSFAVAA LILRTSKATV EEDLSSAAAK
     MEAMKGKKSS VTSVLAIQDQ IKPENVNKIV FACDAGMGSS AMGASILRNK VNKAGLDVTV
     TNTAISNLPS DADVVVTHKD LTDRAKAKLP NAKHISVENF LNSPKYDELV NSLKK
//
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