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Database: UniProt
Entry: D4K8Z1_9FIRM
LinkDB: D4K8Z1_9FIRM
Original site: D4K8Z1_9FIRM 
ID   D4K8Z1_9FIRM            Unreviewed;       549 AA.
AC   D4K8Z1;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=Mannitol-specific phosphotransferase enzyme IIA component {ECO:0000256|ARBA:ARBA00014783};
DE            EC=2.7.1.197 {ECO:0000256|ARBA:ARBA00011909};
DE   AltName: Full=EIIA {ECO:0000256|ARBA:ARBA00030956};
DE   AltName: Full=EIICBA-Mtl {ECO:0000256|ARBA:ARBA00030684};
DE   AltName: Full=EIII {ECO:0000256|ARBA:ARBA00030962};
DE   AltName: Full=PTS system mannitol-specific EIIA component {ECO:0000256|ARBA:ARBA00029908};
DE   AltName: Full=PTS system mannitol-specific EIICBA component {ECO:0000256|ARBA:ARBA00015039};
GN   ORFNames=FPR_09640 {ECO:0000313|EMBL:CBL01304.1};
OS   Faecalibacterium prausnitzii SL3/3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Faecalibacterium.
OX   NCBI_TaxID=657322 {ECO:0000313|EMBL:CBL01304.1, ECO:0000313|Proteomes:UP000007059};
RN   [1] {ECO:0000313|EMBL:CBL01304.1, ECO:0000313|Proteomes:UP000007059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL3/3 {ECO:0000313|EMBL:CBL01304.1,
RC   ECO:0000313|Proteomes:UP000007059};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Faecalibacterium prausnitzii SL3/3.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL01304.1, ECO:0000313|Proteomes:UP000007059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL3/3 {ECO:0000313|EMBL:CBL01304.1,
RC   ECO:0000313|Proteomes:UP000007059};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; FP929046; CBL01304.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4K8Z1; -.
DR   KEGG; fpa:FPR_09640; -.
DR   PATRIC; fig|657322.3.peg.843; -.
DR   eggNOG; COG2213; Bacteria.
DR   eggNOG; COG4668; Bacteria.
DR   HOGENOM; CLU_028721_1_0_9; -.
DR   Proteomes; UP000007059; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd00211; PTS_IIA_fru; 1.
DR   CDD; cd05567; PTS_IIB_mannitol; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
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   PANTHER; PTHR30181; MANNITOL PERMEASE IIC COMPONENT; 1.
DR   PANTHER; PTHR30181:SF2; PTS SYSTEM MANNITOL-SPECIFIC EIICBA COMPONENT; 1.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR   SUPFAM; SSF52794; PTS system IIB component-like; 1.
DR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR   PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR   PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE   4: Predicted;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
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        34..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        118..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        218..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..253
FT                   /note="PTS EIIC type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51104"
FT   DOMAIN          280..374
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51099"
FT   DOMAIN          412..549
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51094"
SQ   SEQUENCE   549 AA;  58029 MW;  CE4DD61E0095C02D CRC64;
     MLMGAMVMGP LAGWVIKQFD KKVEGHIPAG FEMLINNFSI GILGMLLAIL GYYVIGPFMT
     AILTVLTAGV DFLVAHSLLP LVSIFIEPAK VLFLNNAINH GIFSPIGASQ AAETGRSIMY
     MLEANPGPGL GVLLAYCFFC KDDTTRQSAP GAVIIHLLGG IHEIYFPYIL MNPVIIIAPI
     VGNFCAILFY SMTGAGLSGP ASPGSIIAYM AMAPRDSILT VLLGVVIAGA VSFILSSVIL
     KATSGHTKSL TDAQNEMKEM KAQAKGEIPE PTAVNVGQIR KIVFACDAGM GSSAMGATKF
     HNRIKAERPD LTVTNSSVDT IPADADVVVC QRVLADRAAK CAPQAQLVTL DNFLADPHLD
     ALYNALTSTT PALDAKAEAA ANEEIVSDLR NAAVAPLAAA VTEASKANGS VMKIQAEDIQ
     LGLPSVTKEE AIRAAGALLA KRGYVDDSYA DAMVEREKLV STYMGMGVAI PHGTSQKKGT
     VKKSGVVLLQ YPQGVDFGDE KAYLVFGIAG VGNDHLDLLG NVCEILEDED ALEQLKTTSD
     MNYVLEHLQ
//
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