ID A0A0L0K0R5_9ACTN Unreviewed; 674 AA.
AC A0A0L0K0R5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=IQ63_26750 {ECO:0000313|EMBL:KND31339.1};
OS Streptomyces acidiscabies.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=42234 {ECO:0000313|EMBL:KND31339.1, ECO:0000313|Proteomes:UP000037151};
RN [1] {ECO:0000313|Proteomes:UP000037151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-2014) 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}.
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:KND31339.1}.
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DR EMBL; JPPY01000151; KND31339.1; -; Genomic_DNA.
DR RefSeq; WP_050372913.1; NZ_KQ257826.1.
DR AlphaFoldDB; A0A0L0K0R5; -.
DR PATRIC; fig|42234.21.peg.5517; -.
DR OrthoDB; 9782569at2; -.
DR Proteomes; UP000037151; 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; 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:UP000037151};
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 316..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 396..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 438..461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 473..494
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 526..547
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 586..604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 624..645
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..146
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000259|PROSITE:PS51094"
FT DOMAIN 183..278
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000259|PROSITE:PS51099"
FT DOMAIN 308..655
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000259|PROSITE:PS51104"
FT REGION 141..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 674 AA; 69024 MW; 65A2F97E975F5297 CRC64;
MSDMITADLV DLDLSAENKE AAARSLAVRM VTQGRVTDLD GFLADVAARE AQMPTGLDGG
IGIPHCRSAH VTEPTLAFGR ATPGIDFGAP DGPADLIFLI AAPAGADDAH LTILSALARQ
LMNTEFTDAL RAVADPETAA ALIRGDRSPR DAGRHGADED SAAAPVAAST GAAAAEPAAP
FRIVAVTSCP TGIAHTYMAA ESLENAAREA GVQLTVETQG SAGFTRLDPN LIADADGVIF
AHDVPVRDKD RFAGKPTVDV GVKAGINRPS ELIAEVKDKA ARGVVTTGSA PTPVERAGDS
TEGYGTKLRK WLMSGVSYMV PFVAAGGLLI ALGFAIGGYK INKAPSVMDH FLWTQADSWA
ALLFQVGAVS FGFLVPVLAG YIAYGMADRP GLVPGFVGGM IASTINAGFL GGLAAGLIAG
GVVIGIQRVK IPTALRGIMP VVVIPLISTA IVGFLMFVVI GKPIASAQKG MTDWLNGLTG
SNAILLGALL GLMMCFDLGG PVNKVAYTFA TAGIAVTDPS DSAMKVMAAV MAAGMVPPLA
MALATTLRAK LFTETERENG KAAWVLGASF ISEGAIPFAA ADPLRVIPAS MVGGAATGAL
SMAFDATLRA PHGGIFVVPL IGNPFLYLIA LAAGVAITTT LVILLKGLRK ATPTAPRPEE
PLTQPADRKH PIAA
//
