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PTFC1_ECOLI
ID   PTFC1_ECOLI             Reviewed;         415 AA.
AC   P77579; P78196;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Fructose-like permease IIC component 1;
DE   AltName: Full=PTS system fructose-like EIIC component 1;
GN   Name=fryC; Synonyms=ypdG; OrderedLocusNames=b2386, JW2383;
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 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
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   TOPOLOGY [LARGE SCALE ANALYSIS].
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; Multi-pass membrane protein.
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; U00096; AAC75445.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16256.1; -; Genomic_DNA.
DR   PIR; G65012; G65012.
DR   RefSeq; NP_416887.1; NC_000913.3.
DR   RefSeq; WP_000985359.1; NZ_LN832404.1.
DR   AlphaFoldDB; P77579; -.
DR   BioGRID; 4260562; 9.
DR   STRING; 511145.b2386; -.
DR   TCDB; 4.A.2.1.11; the pts fructose-mannitol (fru) family.
DR   PaxDb; P77579; -.
DR   PRIDE; P77579; -.
DR   EnsemblBacteria; AAC75445; AAC75445; b2386.
DR   EnsemblBacteria; BAA16256; BAA16256; BAA16256.
DR   GeneID; 949111; -.
DR   KEGG; ecj:JW2383; -.
DR   KEGG; eco:b2386; -.
DR   PATRIC; fig|1411691.4.peg.4342; -.
DR   EchoBASE; EB3906; -.
DR   eggNOG; COG1299; Bacteria.
DR   HOGENOM; CLU_013155_0_2_6; -.
DR   OMA; QIMMAAI; -.
DR   PhylomeDB; P77579; -.
DR   BioCyc; EcoCyc:MON0-6; -.
DR   PRO; PR:P77579; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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; ISA:EcoCyc.
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   1: Evidence at protein level;
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 1"
FT                   /id="PRO_0000186704"
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;  43966 MW;  76C2CB5EBF0946B3 CRC64;
     MAIKKRSATV VPGASGAAAA VKNPQASKTS 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
 
 
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