PTFC_ECO57
ID PTFC_ECO57 Reviewed; 415 AA.
AC Q8XBP8;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Fructose-like permease IIC component;
DE AltName: Full=PTS system fructose-like EIIC component;
GN Name=fryC; OrderedLocusNames=Z3652, ECs3266;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG57512.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36689.1; -; Genomic_DNA.
DR PIR; B91037; B91037.
DR PIR; D85881; D85881.
DR RefSeq; NP_311293.1; NC_002695.1.
DR RefSeq; WP_000985336.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XBP8; -.
DR STRING; 155864.EDL933_3555; -.
DR EnsemblBacteria; AAG57512; AAG57512; Z3652.
DR EnsemblBacteria; BAB36689; BAB36689; ECs_3266.
DR GeneID; 66673743; -.
DR GeneID; 915632; -.
DR KEGG; ece:Z3652; -.
DR KEGG; ecs:ECs_3266; -.
DR PATRIC; fig|386585.9.peg.3410; -.
DR eggNOG; COG1299; Bacteria.
DR HOGENOM; CLU_013155_0_2_6; -.
DR OMA; QIMMAAI; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; Sugar transport;
KW Transferase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..415
FT /note="Fructose-like permease IIC component"
FT /id="PRO_0000186706"
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..410
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
SQ SEQUENCE 415 AA; 43952 MW; 03B2ECE59AC247A3 CRC64;
MAIKKRSATV VPGASGAAAA VKNPQASKSS FWGELPQHVM SGISRMVPTL IMGGVILAFS
QLIAYSWLKI PAEIGIMDAL 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 VITALMVVFL RLMMFRKGKL LIDSL
