ID A0A494T0F6_9NOCA Unreviewed; 690 AA.
AC A0A494T0F6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=D8W71_15770 {ECO:0000313|EMBL:AYJ49530.1};
OS Rhodococcus sp. P1Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1302308 {ECO:0000313|EMBL:AYJ49530.1, ECO:0000313|Proteomes:UP000277147};
RN [1] {ECO:0000313|Proteomes:UP000277147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1Y {ECO:0000313|Proteomes:UP000277147};
RA Belimov A., Safronova V.I., Ismailov T.;
RT "Complete genome sequence of the abscisic acid utilizing strain Rhodococcus
RT sp. P1Y.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000277147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1Y {ECO:0000313|Proteomes:UP000277147};
RA Nikolaichik Y.A., Gogoleva N.E., Khlopko Y.A., Gogolev Y.V.;
RL Submitted (OCT-2018) 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: 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; CP032762; AYJ49530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494T0F6; -.
DR OrthoDB; 9782569at2; -.
DR Proteomes; UP000277147; Chromosome.
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; cd00211; PTS_IIA_fru; 1.
DR CDD; cd05569; PTS_IIB_fructose; 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; IPR003352; PTS_EIIC.
DR InterPro; IPR013014; PTS_EIIC_2.
DR InterPro; IPR004715; PTS_IIA_fruc.
DR InterPro; IPR003353; PTS_IIB_fruc.
DR InterPro; IPR006327; PTS_IIC_fruc.
DR NCBIfam; TIGR00829; FRU; 1.
DR NCBIfam; TIGR00848; fruA; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000277147};
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 336..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 505..524
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 585..604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 616..641
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 647..668
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..153
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000259|PROSITE:PS51094"
FT DOMAIN 198..293
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000259|PROSITE:PS51099"
FT DOMAIN 326..678
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000259|PROSITE:PS51104"
FT REGION 159..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 690 AA; 69963 MW; 2BE70645CCC50EDF CRC64;
MSTPTHDPAI IVEELVLLDA DLGESKDAVI SRLSTLLAEN GRATDADPLR DAALAREAQS
ATGLPGGIAI PHCRADAVTT ASLGFARLNP KVDFGAPDGP ADLVFLIAAP AGAGSAHMKL
LSSLARALVK PAFVTSLREA PTAAAIVALV DGVINPAPKA APAKAVPEST PETAAVSTAK
HSAPETAPTA SAETPKHIVA VTACPTGIAH TYMAADSLVA AGERAGVTVH VETQGSSGST
PLDPALIASA EAVIFATDVG VKNKERFAGK PVISSGVKRA INEPDVMVTE ALRASNDPNA
ARVSGTAAAA GANNSGAGEL GWGTRIRQIL LTGVSYMIPF VAAGGLLIAL GFLLGGYEIS
SNAEEIVINN SITALPDGGL KAYLGAVLFQ IGALSFSFLV PALAGYISYA IADRPGLAPG
FTAGAVAVLV GAGFIGGLVG GLIAGFVALW ISRWKIPALL RGLMPVVIIP LFATLIVGAL
MFLVLGKPLA AITSGLTDWL NGLTGTSIII LGIILGLMMC FDLGGPVNKA AYAFATAGLS
VTDVASLRIM AAVMAAGMVP PLAMALASLV RPRLFTEAER ENGKAAWFLG AAFISEGAIP
FAAADPFRVI PSMMAGGALT GALIMATDVT LSAPHGGLIV FFAIGKFLWF LVALVAGTLL
SAFLVVFAKQ FLRGKNAPTE ESLDPDLVAA
//