PTFC_ECOL6
ID PTFC_ECOL6 Reviewed; 415 AA.
AC Q8FFD5;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Fructose-like permease IIC component;
DE AltName: Full=PTS system fructose-like EIIC component;
GN Name=fryC; OrderedLocusNames=c2925;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (PTS), a major carbohydrate active -transport system, catalyzes
CC the phosphorylation of incoming sugar substrates concomitant with their
CC translocation across the cell membrane. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00427}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00427}.
CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site.
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DR EMBL; AE014075; AAN81375.1; -; Genomic_DNA.
DR RefSeq; WP_000985305.1; NC_004431.1.
DR AlphaFoldDB; Q8FFD5; -.
DR STRING; 199310.c2925; -.
DR EnsemblBacteria; AAN81375; AAN81375; c2925.
DR KEGG; ecc:c2925; -.
DR eggNOG; COG1299; Bacteria.
DR HOGENOM; CLU_013155_0_2_6; -.
DR OMA; QIMMAAI; -.
DR BioCyc; ECOL199310:C2925-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013014; PTS_EIIC_2.
DR Pfam; PF02378; PTS_EIIC; 1.
DR PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Phosphoprotein;
KW Phosphotransferase system; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..415
FT /note="Fructose-like permease IIC component"
FT /id="PRO_0000186705"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 68..101
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 123..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 148..157
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 179..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 219..237
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 259..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 298..318
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 340..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 363..378
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 400..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..415
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
SQ SEQUENCE 415 AA; 44006 MW; 2D4ED9FE8979D97F CRC64;
MAIKKRSATV VHGASGAAAA VKNPQASKSS FWGELPQHVM SGISRMVPTL IMGGVILAFS
QLIAYSWLKI PADIGIMDAL NSGKFSGFDL SLLKFAWLSQ SFGGVLFGFA IPMFAAFVAN
SIGGKLAFPA GFIGGLMSTQ PTQLLNFDPS TMQWATSSPV PSTFIGALII SIVAGYLVKW
MNQKIQLPDF LLAFKTTFLL PILSAIFVML AMYYVITPFG GWINGGIRTV LTAAGEKGAL
MYAMGIAAAT AIDLGGPINK AAGFVAFSFT TDHVLPVTAR SIAIVIPPIG LGLATIIDRR
LTGKRLFNAQ LYPQGKTAMF LAFMGISEGA IPFALESPIT AIPSYMVGAI VGSTAAVWLG
AVQWFPESAI WAWPLVTNLG VYMAGIALGA IITALMVVFL RLMMFRKGKL LIESL
