ID A0A0H3EAJ4_BACA1 Unreviewed; 477 AA.
AC A0A0H3EAJ4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 OrderedLocusNames=BATR1942_20700 {ECO:0000313|EMBL:ADP35055.1};
OS Bacillus atrophaeus (strain 1942).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=720555 {ECO:0000313|EMBL:ADP35055.1, ECO:0000313|Proteomes:UP000006867};
RN [1] {ECO:0000313|Proteomes:UP000006867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1942 {ECO:0000313|Proteomes:UP000006867};
RA Gibbons H.S., Broomall S., McNew L.A., Daligault H., Chapman C., Bruce D.,
RA Karavis M., McGregor P., Hong C., Park K.H., Akmal A., Feldman A.,
RA Lin J.S., Chang W.E., Higgs B.W., Demirev P., Lindquist J., Liem A.,
RA Fochler E., Tapia R., Bishop-Lilly K., Detter C., Han C., Sozhamannan S.,
RA Rosenzweig C.N., Skowronski E.;
RT "Genomic signatures of strain selection and enhancement in Bacillus
RT atrophaeus subsp. Globigii, a historical biowarfare simulant.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADP35055.1, ECO:0000313|Proteomes:UP000006867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1942 {ECO:0000313|EMBL:ADP35055.1,
RC ECO:0000313|Proteomes:UP000006867};
RX PubMed=21464989; DOI=10.1371/journal.pone.0017836;
RA Gibbons H.S., Broomall S.M., McNew L.A., Daligault H., Chapman C.,
RA Bruce D., Karavis M., Krepps M., McGregor P.A., Hong C., Park K.H.,
RA Akmal A., Feldman A., Lin J.S., Chang W.E., Higgs B.W., Demirev P.,
RA Lindquist J., Liem A., Fochler E., Read T.D., Tapia R., Johnson S.,
RA Bishop-Lilly K.A., Detter C., Han C., Sozhamannan S., Rosenzweig C.N.,
RA Skowronski E.W.;
RT "Genomic signatures of strain selection and enhancement in Bacillus
RT atrophaeus var. globigii, a historical biowarfare simulant.";
RL PLoS ONE 6:E17836-E17836(2011).
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}.
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DR EMBL; CP002207; ADP35055.1; -; Genomic_DNA.
DR RefSeq; WP_004430323.1; NC_014639.1.
DR AlphaFoldDB; A0A0H3EAJ4; -.
DR GeneID; 23412567; -.
DR KEGG; bae:BATR1942_20700; -.
DR eggNOG; COG2213; Bacteria.
DR HOGENOM; CLU_028721_2_0_9; -.
DR OrthoDB; 9814222at2; -.
DR Proteomes; UP000006867; Chromosome.
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 Coiled coil {ECO:0000256|SAM:Coils};
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 30..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..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 275..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..357
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000259|PROSITE:PS51104"
FT DOMAIN 389..477
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000259|PROSITE:PS51099"
FT COILED 357..391
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 477 AA; 50315 MW; 703009B49744D1B1 CRC64;
MQQQDEQQAG MKVKIQRFGS YLSGMIMPNI GAFIAWGIIT ALFIPAGWLP NEQLNTLVSP
MITYLLPLLI AYTGGKMIYD HRGGVVGATA AIGVIVGSDI PMFLGAMIMG PLGGYLIKQI
DKLFKDKVRQ GFEMLINNFT AGIIGAILTI IAFYAIGPVV LSLNKILAAG VEVIVHANLL
PIASVFVEPA KVLFLNNAIN HGILSPIGIE QAANTGKSIL FLVEANPGPG LGILLAYMFF
GKGSSKSTAP GAAVIHFFGG IHEIYFPYIL MKPMLILAAI AGGASGLLTF SIFNAGLVAA
SSPGSIFAIL AMTPRGNYLG VIAGVIVATA VSFIVSAVIL KSSKAGEEDL TAAAEKMQAM
KGKNSQAAAA LTETEKEAAE AEVTHEDVNK IIFACDAGMG SSAMGASILR NKVKKAELDI
SVTNTAINNL PSDADIVITH KDLTERAKAK LPNVTHISVD NFLNSPKYDE LIEKLKK
//
