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Database: UniProt
Entry: A0A1V3JY79_9PAST
LinkDB: A0A1V3JY79_9PAST
Original site: A0A1V3JY79_9PAST 
ID   A0A1V3JY79_9PAST        Unreviewed;       558 AA.
AC   A0A1V3JY79;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=BKL51_04205 {ECO:0000313|EMBL:OOF65744.1};
OS   Rodentibacter sp. Ppn85.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Rodentibacter.
OX   NCBI_TaxID=1908525 {ECO:0000313|EMBL:OOF65744.1, ECO:0000313|Proteomes:UP000189325};
RN   [1] {ECO:0000313|EMBL:OOF65744.1, ECO:0000313|Proteomes:UP000189325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ppn85 {ECO:0000313|EMBL:OOF65744.1,
RC   ECO:0000313|Proteomes:UP000189325};
RA   Christensen H.;
RT   "Rodentibacter gen. nov. and new species.";
RL   Submitted (OCT-2016) 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:OOF65744.1}.
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DR   EMBL; MLHS01000020; OOF65744.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V3JY79; -.
DR   STRING; 1908525.BKL51_04205; -.
DR   OrthoDB; 9782569at2; -.
DR   Proteomes; UP000189325; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 2.
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        237..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        275..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        306..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        352..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        392..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        433..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        492..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        531..551
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          107..202
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51099"
FT   DOMAIN          226..558
FT                   /note="PTS EIIC type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51104"
SQ   SEQUENCE   558 AA;  57784 MW;  8B845145D98F8292 CRC64;
     MKLFLTQSDN IGSAKAYLLR EVFRAAAQKA EDISLVENLA EADIVLIVGS KLPNNSALVG
     KKVLLVSEES AMNAPETILT NAQTQAVDYV APESAVSFNG VSKVKNIVAV TACPTGVAHT
     FMSAEAIEAY AKKQGWKVKV ETRGQVGAGN EITPEEVAAA DLVFVAADID VPLDKFKGKP
     MYRTSTGLAL KKTAQEFDKA FKEAKVFEGV SSKAANTEEN GEKKGVYKHL MTGVSHMLPL
     VVAGGLLIAI SFMFGIEAFK DETVFHGLPK ALMDIGGGAA FALMIAVFAG YVAFSIADRP
     GLAVGLIGGM LASTAGAGIL GGIVAGIVAG YVVKGLNAAI KLPVSLTSLK PILILPLLGS
     LIVGLAMIYV INPPVSQVMN ALTEWLKSMG EVNAIVLGTL IGAMMCIDMG GPVNKAAYTF
     SVGMIASQVY TPMAAAMAAG MVPPIGMAIA TWIARNKFTA NQRDAGKASF ILGLCFISEG
     ALPFVAADPI RVIISSVVGG ATAGAISMAS DITLQAPHGG LFVIPFVSEP VRYLAAIAAG
     ALVTGVIYAV IKPKATTE
//
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