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| Entry name |
PTIBC_ECOLI |
| Primary accession number |
P24241 |
| Secondary accession numbers |
Q2MAB4 Q46880 Q6BF64 |
| Integrated into Swiss-Prot on |
March 1, 1992 |
| Sequence was last modified on |
October 11, 2004 (Sequence version 3) |
| Annotations were last modified on |
November 25, 2008 (Entry version 82) |
| Name and origin of the protein |
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| Protein name |
PTS system arbutin-, cellobiose-, and salicin-specific EIIBC component |
| Synonyms |
EIIBC-Asc
EII-Asc
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| Includes |
Arbutin-, cellobiose-, and salicin-specific phosphotransferase enzyme IIB component
(EC 2.7.1.69)
(PTS system arbutin-, cellobiose-, and salicin-specific EIIB component)
Arbutin, cellobiose, and salicin permease IIC component
(PTS system arbutin-, cellobiose-, and salicin-specific EIIC component)
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| Gene name |
| Name: | ascF |
| OrderedLocusNames: | b2715, JW5435 |
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| From |
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| Taxonomy |
Bacteria;
Proteobacteria;
Gammaproteobacteria;
Enterobacteriales;
Enterobacteriaceae;
Escherichia.
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| Protein existence |
4: Predicted; |
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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=1630307 [NCBI, ExPASy, EBI, Israel, Japan]
Hall B.G.,
Xu L.;
"Nucleotide sequence, function, activation, and evolution of the cryptic asc operon of Escherichia coli K12.";
Mol. Biol. Evol. 9:688-706(1992).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R.,
Plunkett G. III,
Bloch C.A.,
Perna N.T.,
Burland V.,
Riley M.,
Collado-Vides J.,
Glasner J.D.,
Rode C.K.,
Mayhew G.F.,
Gregor J.,
Davis N.W.,
Kirkpatrick H.A.,
Goeden M.A.,
Rose D.J.,
Mau B.,
Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
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[3]
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SEQUENCE REVISION TO 167-170.
DOI=10.1093/nar/gkj405; PubMed=16397293 [NCBI, ExPASy, EBI, Israel, Japan]
Riley M.,
Abe T.,
Arnaud M.B.,
Berlyn M.K.B.,
Blattner F.R.,
Chaudhuri R.R.,
Glasner J.D.,
Horiuchi T.,
Keseler I.M.,
Kosuge T.,
Mori H.,
Perna N.T.,
Plunkett G. III,
Rudd K.E.,
Serres M.H.,
Thomas G.H.,
Thomson N.R.,
Wishart D.,
Wanner B.L.;
"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005.";
Nucleic Acids Res. 34:1-9(2006).
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[4]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K.,
Morooka N.,
Yamamoto Y.,
Fujita K.,
Isono K.,
Choi S.,
Ohtsubo E.,
Baba T.,
Wanner B.L.,
Mori H.,
Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
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[5]
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SUBCELLULAR LOCATION.
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.1109730; PubMed=15919996 [NCBI, ExPASy, EBI, Israel, Japan]
Daley D.O.,
Rapp M.,
Granseth E.,
Melen K.,
Drew D.,
von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane proteome.";
Science 308:1321-1323(2005).
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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 arbutin, cellobiose, and salicin transport.
- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.
- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
- 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.
- DOMAIN: The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.
- SIMILARITY: Contains 1 PTS EIIB type-1 domain.
- SIMILARITY: Contains 1 PTS EIIC type-1 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: 485 AA [This is the length of the unprocessed precursor] |
Molecular weight: 51026 Da [This is the MW of the unprocessed precursor] |
CRC64: E53627EB31B9523C [This is a checksum on the sequence] |
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10 20 30 40 50 60
MAKNYAALAR SVIAALGGVD NISAVTHCMT RLRFVIKDDA LIDSPTLKTI PGVLGVVRSD
70 80 90 100 110 120
NQCQVIIGNT VSQAFQEVVS LLPGDMQPAQ PVGKPKLTLR RIGAGILDAL IGTMSPLIPA
130 140 150 160 170 180
IIGGSMVKLL AMILEMSGVL TKGSPTLTIL NVIGDGAFFF LPLMVAASAA IKFKTNMSLA
190 200 210 220 230 240
IAIAGVLVHP SFIELMAKAA QGEHVEFALI PVTAVKYTYT VIPALVMTWC LSYIERWVDS
250 260 270 280 290 300
ITPAVTKNFL KPMLIVLIAA PLAILLIGPI GIWIGSAISA LVYTIHGYLG WLSVAIMGAL
310 320 330 340 350 360
WPLLVMTGMH RVFTPTIIQT IAETGKEGMV MPSEIGANLS LGGSSLAVAW KTKNPELRQT
370 380 390 400 410 420
ALAAAASAIM AGISEPALYG VAIRLKRPLI ASLISGFICG AVAGMAGLAS HSMAAPGLFT
430 440 450 460 470 480
SVQFFDPANP MSIVWVFAVM ALAVVLSFIL TLLLGFEDIP VEEAAAQARK YQSVQPTVAK
EVSLN
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P24241 in FASTA format |
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