ID A0A060M0E1_9BACI Unreviewed; 573 AA.
AC A0A060M0E1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=BleG1_2926 {ECO:0000313|EMBL:AIC95490.1};
OS Shouchella lehensis G1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX NCBI_TaxID=1246626 {ECO:0000313|EMBL:AIC95490.1, ECO:0000313|Proteomes:UP000027142};
RN [1] {ECO:0000313|EMBL:AIC95490.1, ECO:0000313|Proteomes:UP000027142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:AIC95490.1,
RC ECO:0000313|Proteomes:UP000027142};
RX PubMed=24811681; DOI=10.1016/j.gene.2014.05.012;
RA Noor Y.M., Samsulrizal N.H., Jema'on N.A., Low K.O., Ramli A.N.,
RA Alias N.I., Damis S.I., Fuzi S.F., Isa M.N., Murad A.M., Raih M.F.,
RA Bakar F.D., Najimudin N., Mahadi N.M., Illias R.M.;
RT "A comparative genomic analysis of the alkalitolerant soil bacterium
RT Bacillus lehensis G1.";
RL Gene 545:253-261(2014).
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; CP003923; AIC95490.1; -; Genomic_DNA.
DR RefSeq; WP_038482398.1; NZ_CP003923.1.
DR AlphaFoldDB; A0A060M0E1; -.
DR STRING; 1246626.BleG1_2926; -.
DR KEGG; ble:BleG1_2926; -.
DR PATRIC; fig|1246626.3.peg.2914; -.
DR eggNOG; COG2213; Bacteria.
DR HOGENOM; CLU_028721_2_1_9; -.
DR OrthoDB; 9814222at2; -.
DR Proteomes; UP000027142; 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; 2.
DR Gene3D; 3.40.50.2300; -; 2.
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; 2.
DR SUPFAM; SSF52794; PTS system IIB component-like; 2.
DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 2.
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:UP000027142};
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..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..343
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000259|PROSITE:PS51104"
FT DOMAIN 378..473
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000259|PROSITE:PS51099"
FT DOMAIN 485..573
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000259|PROSITE:PS51099"
SQ SEQUENCE 573 AA; 60762 MW; BE09C3F23167D8C9 CRC64;
MTEKKSIRSR VQRFGSNLSS MIMPNIGAFI AFGTITAINA FFFIQILDNM VVPMIYYLLP
LLIAYTGGKL VHDMRGGVVG ATAVMGVIAA VPDAPMFIGA MIMGPLGGYA IKKFDQLVDG
KIRQGFEMLV NNFSAGLIGA ALAVIGSLLV APIVKGLTSA LGAGADFLIS TGLLPLVSII
IEPAKILFLN NAINHGVLVP LAATQFETLG KSIFYLLEAN PGPGLGILLA FMIFGKGVAR
GSAYGAGIIH FIGGIHEIYF PYVLMKPLMF LAVIFGGASG VFVFNLFQVG LVAPASPGSI
IPIMALTAQG DYLGVILGVL VATVVSFVIA SLILRFDKKG EEDNIEEAQA KMQDMKGKKS
SVVSTSGSKT GNGYENVSSI IFACDAGMGS SAMGASIMKD RVKKAGIEGV SVSNTSISNI
PDSADLVITH KDLTERAKQK NPSAIHVSVD NFMNSPRYNE IIEDLKGGQS IEEPVSSEAT
KEEVDKIIFA CDAGMGSSAM GASLLKNKFK KANIEGIHIS NTAINSIPSD ADIVITHKDL
TERAKQKQPN AEHISVENFM NSPKYDELIE RLK
//
