PTFC2_ECOLI
ID PTFC2_ECOLI Reviewed; 359 AA.
AC P32672; Q2M8P4;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Fructose-like permease IIC component 2;
DE AltName: Full=PTS system fructose-like EIIC component 2;
GN Name=frwC; Synonyms=yijJ; OrderedLocusNames=b3949, JW3921;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP DISCUSSION OF SEQUENCE.
RX PubMed=7773398; DOI=10.1099/13500872-141-4-961;
RA Reizer J., Reizer A., Saier M.H. Jr.;
RT "Novel phosphotransferase system genes revealed by bacterial genome
RT analysis -- a gene cluster encoding a unique Enzyme I and the proteins of a
RT fructose-like permease system.";
RL Microbiology 141:961-971(1995).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00427,
CC ECO:0000269|PubMed:15919996}.
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; U00006; AAC43055.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76931.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77362.1; -; Genomic_DNA.
DR PIR; H65201; H65201.
DR RefSeq; NP_418384.1; NC_000913.3.
DR RefSeq; WP_001004446.1; NZ_SSZK01000014.1.
DR AlphaFoldDB; P32672; -.
DR BioGRID; 4262060; 5.
DR ComplexPortal; CPX-5994; Frw fuctose-like enzyme II complex.
DR STRING; 511145.b3949; -.
DR TCDB; 4.A.2.1.10; the pts fructose-mannitol (fru) family.
DR PaxDb; P32672; -.
DR PRIDE; P32672; -.
DR EnsemblBacteria; AAC76931; AAC76931; b3949.
DR EnsemblBacteria; BAE77362; BAE77362; BAE77362.
DR GeneID; 66672141; -.
DR GeneID; 948448; -.
DR KEGG; ecj:JW3921; -.
DR KEGG; eco:b3949; -.
DR PATRIC; fig|1411691.4.peg.2756; -.
DR EchoBASE; EB1852; -.
DR eggNOG; COG1299; Bacteria.
DR HOGENOM; CLU_013155_0_1_6; -.
DR OMA; QGQNGIQ; -.
DR PhylomeDB; P32672; -.
DR BioCyc; EcoCyc:FRWC-MON; -.
DR BioCyc; MetaCyc:FRWC-MON; -.
DR PRO; PR:P32672; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IEA:InterPro.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR InterPro; IPR013014; PTS_EIIC_2.
DR InterPro; IPR006327; PTS_IIC_fruc.
DR TIGRFAMs; TIGR01427; PTS_IIC_fructo; 1.
DR PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..359
FT /note="Fructose-like permease IIC component 2"
FT /id="PRO_0000186506"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 11..344
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
SQ SEQUENCE 359 AA; 37086 MW; 1CB60AF9FF6CCDAD CRC64;
MNELVQILKN TRQHLMTGVS HMIPFVVSGG ILLAVSVMLY GKGAVPDAVA DPNLKKLFDI
GVAGLTLMVP FLAAYIGYSI AERSALAPCA IGAWVGNSFG AGFFGALIAG IIGGIVVHYL
KKIPVHKVLR SVMPIFIIPI VGTLITAGIM MWGLGEPVGA LTNSLTQWLQ GMQQGSIVML
AVIMGLMLAF DMGGPVNKVA YAFMLICVAQ GVYTVVAIAA VGICIPPLGM GLATLIGRKN
FSAEERETGK AALVMGCVGV TEGAIPFAAA DPLRVIPSIM VGSVCGAVTA ALVGAQCYAG
WGGLIVLPVV EGKLGYIAAV AVGAVVTAVC VNVLKSLARK NGSSTDEKED DLDLDFEIN
