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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
DOI=10.1073/pnas.252529799; PubMed=12471157 [NCBI, ExPASy, EBI, Israel, Japan]
Welch R.A.,
Burland V.,
Plunkett G. III,
Redford P.,
Roesch P.,
Rasko D.,
Buckles E.L.,
Liou S.-R.,
Boutin A.,
Hackett J.,
Stroud D.,
Mayhew G.F.,
Rose D.J.,
Zhou S.,
Schwartz D.C.,
Perna N.T.,
Mobley H.L.T.,
Donnenberg M.S.,
Blattner F.R.;
"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in mannose transport (By similarity).
- CATALYTIC ACTIVITY: Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine.
- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.
- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.
- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain.
- SIMILARITY: Contains 1 PTS EIIA type-4 domain.
- SIMILARITY: Contains 1 PTS EIIB type-4 domain.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 323 AA [This is the length of the unprocessed precursor] |
Molecular weight: 35048 Da [This is the MW of the unprocessed precursor] |
CRC64: A446B79421B8C040 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MTIAIVIGTH GWAAEQLLKT AEMLLGEQEN VGWIDFVPGE NAETLIEKYN AQLAKLDTTK
70 80 90 100 110 120
GVLFLVDTWG GSPFNAASRI VVDKEHYEVI AGVNIPMLVE TLMARDDDPS FDELVALAVE
130 140 150 160 170 180
TGREGVKALK AKPVEKAAPA PAAAAPKAAP TPAKPMGPND YMVIGLARID DRLIHGQVAT
190 200 210 220 230 240
RWTKETNVSR IIVVSDEVAA DTVRKTLLTQ VAPPGVTAHV VDVAKMIRVY NNPKYAGERV
250 260 270 280 290 300
MLLFTNPTDV ERLVEGGVKI TSVNVGGMAF RQGKTQVNNA VSVDEKDIEA FKKLNARGIE
310 320
LEVRKVSTDP KLKMMDLISK IDK
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P69798 in FASTA format |
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