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P24241 (PTIBC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PTS system arbutin-, cellobiose-, and salicin-specific EIIBC component
Alternative name(s):
EIIBC-Asc
Short name=EII-Asc

Including the following 2 domains:

  1. Arbutin-, cellobiose-, and salicin-specific phosphotransferase enzyme IIB component
    EC=2.7.1.69
    Alternative name(s):
    PTS system arbutin-, cellobiose-, and salicin-specific EIIB component
  2. Arbutin, cellobiose, and salicin permease IIC component
    Alternative name(s):
    PTS system arbutin-, cellobiose-, and salicin-specific EIIC component
Gene names
Name:ascF
Ordered Locus Names:b2715, JW5435
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Protein existencePredicted

General annotation (Comments)

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 Ref.5.

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.

The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.

Sequence similarities

Contains 1 PTS EIIB type-1 domain.

Contains 1 PTS EIIC type-1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 485485PTS system arbutin-, cellobiose-, and salicin-specific EIIBC component
PRO_0000186498

Regions

Transmembrane102 – 12221Helical; Potential
Transmembrane147 – 16721Helical; Potential
Transmembrane177 – 19721Helical; Potential
Transmembrane207 – 22721Helical; Potential
Transmembrane254 – 27421Helical; Potential
Transmembrane285 – 30521Helical; Potential
Transmembrane330 – 35021Helical; Potential
Transmembrane363 – 38321Helical; Potential
Transmembrane389 – 40921Helical; Potential
Transmembrane433 – 45321Helical; Potential
Domain1 – 8888PTS EIIB type-1
Domain108 – 470363PTS EIIC type-1

Sites

Active site281Phosphocysteine intermediate; for EIIB activity By similarity

Experimental info

Sequence conflict167 – 1704ASAA → HLPR in AAA69225. Ref.2
Sequence conflict1671A → Q in AAA16429. Ref.1
Sequence conflict3111R → H in AAA16429. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P24241 [UniParc].

Last modified October 11, 2004. Version 3.
Checksum: E53627EB31B9523C

FASTA48551,026
        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

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence, function, activation, and evolution of the cryptic asc operon of Escherichia coli K12."
Hall B.G., Xu L.
Mol. Biol. Evol. 9:688-706(1992) [PubMed: 1630307] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005."
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.
Nucleic Acids Res. 34:1-9(2006) [PubMed: 16397293] [Abstract]
Cited for: SEQUENCE REVISION TO 167-170.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed: 15919996] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M73326 Unassigned DNA. Translation: AAA16429.1.
U29579 Genomic DNA. Translation: AAA69225.1.
U00096 Genomic DNA. Translation: AAT48150.1.
AP009048 Genomic DNA. Translation: BAE76792.1.
PIRG65051.
RefSeqYP_026182.1. NC_000913.2.

3D structure databases

ProteinModelPortalP24241.
SMRP24241. Positions 4-82.
ModBaseSearch...

Protein family/group databases

TCDB4.A.1.2.3. PTS glucose-glucoside (Glc) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000003392; EBESCP00000003392; EBESCG00000002780.
EBESCT00000016996; EBESCP00000016287; EBESCG00000016055.
GeneID947154.
GenomeReviewsGene locus JW5435 in contig AP009048_GR.
Gene locus b2715 in contig U00096_GR.
KEGGecj:JW5435.
eco:b2715.
PATRIC32120830. VBIEscCol129921_2807.

Organism-specific databases

EchoBASEEB0084.
EcoGeneEG10086. ascF.

Phylogenomic databases

eggNOGCOG1263.
GeneTreeEBGT00050000009157.
HOGENOMHBG673521.
OMAPANPMTI.
PhylomeDBP24241.
ProtClustDBPRK09796.

Enzyme and pathway databases

BioCycEcoCyc:ASCF-MONOMER.

Gene expression databases

GenevestigatorP24241.

Family and domain databases

InterProIPR018113. PTrfase_EIIB/Cys_phosph_CS.
IPR004719. PTrfase_sys_maltose/Glc-sp_IIC.
IPR001996. PTS_EIIB_1.
IPR003352. PTS_EIIC.
IPR013013. PTS_EIIC_1.
[Graphical view]
Gene3DG3DSA:3.30.1360.60. PTS_EIIB. 1 hit.
KOK02752.
K02753.
PfamPF00367. PTS_EIIB. 1 hit.
PF02378. PTS_EIIC. 1 hit.
[Graphical view]
SUPFAMSSF55604. PTS_EIIB. 1 hit.
TIGRFAMsTIGR00852. Pts-Glc. 1 hit.
PROSITEPS51098. PTS_EIIB_TYPE_1. 1 hit.
PS01035. PTS_EIIB_TYPE_1_CYS. 1 hit.
PS51103. PTS_EIIC_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTIBC_ECOLI
AccessionPrimary (citable) accession number: P24241
Secondary accession number(s): Q2MAB4, Q46880, Q6BF64
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents