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Database: UniProt
Entry: F9Q9I2_9PAST
LinkDB: F9Q9I2_9PAST
Original site: F9Q9I2_9PAST 
ID   F9Q9I2_9PAST            Unreviewed;       484 AA.
AC   F9Q9I2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=protein-N(pi)-phosphohistidine--D-fructose phosphotransferase {ECO:0000256|ARBA:ARBA00012799};
DE            EC=2.7.1.202 {ECO:0000256|ARBA:ARBA00012799};
GN   ORFNames=HMPREF9952_0685 {ECO:0000313|EMBL:EGV05672.1};
OS   Haemophilus pittmaniae HK 85.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=1035188 {ECO:0000313|EMBL:EGV05672.1, ECO:0000313|Proteomes:UP000006235};
RN   [1] {ECO:0000313|EMBL:EGV05672.1, ECO:0000313|Proteomes:UP000006235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HK 85 {ECO:0000313|EMBL:EGV05672.1,
RC   ECO:0000313|Proteomes:UP000006235};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-fructose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC         fructose 1-phosphate(in) + L-histidyl-[protein];
CC         Xref=Rhea:RHEA:49252, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC         ChEBI:CHEBI:29979, ChEBI:CHEBI:37721, ChEBI:CHEBI:58674,
CC         ChEBI:CHEBI:64837; EC=2.7.1.202;
CC         Evidence={ECO:0000256|ARBA:ARBA00001401};
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:EGV05672.1}.
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DR   EMBL; AFUV01000014; EGV05672.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9Q9I2; -.
DR   STRING; 1035188.HMPREF9952_0685; -.
DR   Proteomes; UP000006235; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005351; F:carbohydrate:proton symporter activity; IEA:InterPro.
DR   GO; GO:0022877; F:protein-N(PI)-phosphohistidine-fructose phosphotransferase system transporter activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   CDD; cd05569; PTS_IIB_fructose; 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; IPR003352; PTS_EIIC.
DR   InterPro; IPR013014; PTS_EIIC_2.
DR   InterPro; IPR003353; PTS_IIB_fruc.
DR   InterPro; IPR006327; PTS_IIC_fruc.
DR   NCBIfam; TIGR00829; FRU; 1.
DR   NCBIfam; TIGR01427; PTS_IIC_fructo; 1.
DR   PANTHER; PTHR30505; FRUCTOSE-LIKE PERMEASE; 1.
DR   PANTHER; PTHR30505:SF0; FRUCTOSE-LIKE PTS SYSTEM EIIBC COMPONENT-RELATED; 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, ECO:0000313|EMBL:EGV05672.1};
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        163..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        197..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        232..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        278..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        318..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        359..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        418..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        457..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          32..127
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51099"
FT   DOMAIN          152..484
FT                   /note="PTS EIIC type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51104"
SQ   SEQUENCE   484 AA;  49896 MW;  6BB1D6AD80E2E685 CRC64;
     MTLTNALEQA VDYVQPSSSV AGASSLSGVK NIVAVTACPT GVAHTFMSAE AIETYAKKQG
     WQVKVETRGQ VGAGNEITPE EVAAADLVFV AADIDVPLDK FQGKPMYRTS TGLALKKTAQ
     EFDKAFKEAK IYEGGAAKSS AKSEESGEKK GVYKHLMTGV SHMLPLVVAG GLLIAISFMF
     GIEAFKDETI FYGIPKALMG IGGGAAFHLM IAVFAGYVAF SIADRPGLAV GLIGGMLATT
     AGAGILGGII AGFLAGYVVK GLNAAIKLPA SLTSLKPILI LPLFGTLIVG LAMIYVINPP
     VSQIMTTLSD WLKSMGEVNA MVLGAIIGAM MCIDMGGPVN KAAYTFSVGM LASQVHTPMA
     AAMAAGMVPP IGMAIATWIA RSKFTSNQRD AGKASFVLGL CFISEGALPF VAADPLRVII
     SSVIGGATAG AISMALNISL QAPHGGLFVI PFVSEPLLYL GAIAIGALLT GVVYALIKPR
     VRAE
//
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