PTFC_SHIFL
ID PTFC_SHIFL Reviewed; 415 AA.
AC Q83QP2;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Fructose-like permease IIC component;
DE AltName: Full=PTS system fructose-like EIIC component;
GN Name=fryC; OrderedLocusNames=SF2452, S2591;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN43960.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17771.1; -; Genomic_DNA.
DR RefSeq; NP_708253.1; NC_004337.2.
DR AlphaFoldDB; Q83QP2; -.
DR STRING; 198214.SF2452; -.
DR EnsemblBacteria; AAN43960; AAN43960; SF2452.
DR EnsemblBacteria; AAP17771; AAP17771; S2591.
DR GeneID; 1025577; -.
DR KEGG; sfl:SF2452; -.
DR KEGG; sfx:S2591; -.
DR PATRIC; fig|198214.7.peg.2930; -.
DR HOGENOM; CLU_013155_0_2_6; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000186707"
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"
FT CONFLICT 24
FT /note="L -> P (in Ref. 2; AAP17771)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 43982 MW; 94C42EA33717873D CRC64;
MAIKKRSATV VPGASGAAAA VKNLQASKSS 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 IITALMVVFL RLMMFRKGKL LIDSL
