ID C1CYR7_DEIDV Unreviewed; 632 AA.
AC C1CYR7;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
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 OrderedLocusNames=Deide_20770 {ECO:0000313|EMBL:ACO47097.1};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO47097.1, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO47097.1, ECO:0000313|Proteomes:UP000002208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC {ECO:0000313|Proteomes:UP000002208};
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
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}.
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DR EMBL; CP001114; ACO47097.1; -; Genomic_DNA.
DR RefSeq; WP_012694218.1; NC_012526.1.
DR AlphaFoldDB; C1CYR7; -.
DR STRING; 546414.Deide_20770; -.
DR PaxDb; 546414-Deide_20770; -.
DR KEGG; ddr:Deide_20770; -.
DR eggNOG; COG1299; Bacteria.
DR eggNOG; COG1445; Bacteria.
DR HOGENOM; CLU_013155_4_2_0; -.
DR OrthoDB; 9782569at2; -.
DR Proteomes; UP000002208; Chromosome.
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; 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; 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; 2.
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; 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:UP000002208};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACO47097.1};
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 288..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 411..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 487..512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 550..572
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..99
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000259|PROSITE:PS51099"
FT DOMAIN 143..240
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000259|PROSITE:PS51099"
FT DOMAIN 277..622
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000259|PROSITE:PS51104"
SQ SEQUENCE 632 AA; 63407 MW; 25B4DEA486CBE8AB CRC64;
MAKLVAVTAG PSGIAHTFMA AEALRRAAQA AGHLLRVETQ AGAAPQDPLS AAEIAAADAV
ILVTDVPLDE ARFAGKTVVR GSTQDAIRRA PELIAQATGS APVQPVTSTL AETGAPGPAA
TVSAASAATG TNAQSAPTSQ APLKVVGITS CPTGIAHTFM AAEGLEGGAR ALGYQAKIET
QGSVGAGNAL TPQDIAEADV VVIAADTNVD LSRFAGKRVY QTGTKPAIKD GSAVIRTALS
DAQVYGSAPS ADAGGAGDYV AQAASAKAAK NAGVPSFYKH LMTGVSHMLP FVVAGGLLIA
LAFAIGSFQF GDQGIFIYED RYAGTLGNTL FKIGANGAFG LFVPVLAGFI AFSIADRPGL
APGMVGGFLA GLTGSGFLGG IIAGFLAGYA VRWLTRNIRL PRTLEGLKPT LILPLLGTLI
VGLLMMLVIG RPVAAALGAT TAWLQGLGNT SAGVLGAVLG SMMAFDMGGP INKAAYTFST
GLLGEKVYGP IAAAMAAGMT PPLALFLATL VFRNRFTRDE VQAGKAAGVL GISFITEGAI
PFAARDPLRV IPALIAGSAV AGAISMAAGC LLRAPHGGIF VLFIPNAVTN LPMYIVALVA
GTLVSTALLG VLKKPLPQEA AVVSQETAAA TA
//
