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Protein

N,N'-diacetylchitobiose-specific phosphotransferase enzyme IIB component

Gene

chbB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 N,N'-diacetylchitobiose transport.1 Publication

Catalytic activityi

[Protein]-N(pi)-phospho-L-histidine + N,N'-diacetylchitobiose(Side 1) = [protein]-L-histidine + N,N'-diacetylchitobiose 6'-phosphate(Side 2).3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei10 – 101Phosphocysteine intermediateBy similarity

GO - Molecular functioni

GO - Biological processi

  • carbohydrate transmembrane transport Source: GOC
  • N,N'-diacetylchitobiose import Source: EcoCyc
  • phosphoenolpyruvate-dependent sugar phosphotransferase system Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Phosphotransferase system, Sugar transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:CELA-MONOMER.
ECOL316407:JW1727-MONOMER.
MetaCyc:CELA-MONOMER.

Protein family/group databases

TCDBi4.A.3.2.1. the pts lactose-n,n'-diacetylchitobiose--glucoside (lac) family.

Names & Taxonomyi

Protein namesi
Recommended name:
N,N'-diacetylchitobiose-specific phosphotransferase enzyme IIB component (EC:2.7.1.1963 Publications)
Alternative name(s):
PTS system N,N'-diacetylchitobiose-specific EIIB component
Gene namesi
Name:chbB
Synonyms:celA
Ordered Locus Names:b1738, JW1727
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10140. chbB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 106106N,N'-diacetylchitobiose-specific phosphotransferase enzyme IIB componentPRO_0000186489Add
BLAST

Proteomic databases

PaxDbiP69795.

Expressioni

Inductioni

By N,N'-diacetylchitobiose.

Interactioni

Subunit structurei

Monomer; in both its unphosphorylated and phosphorylated forms.1 Publication

Protein-protein interaction databases

BioGridi4260316. 10 interactions.
IntActiP69795. 1 interaction.
STRINGi511145.b1738.

Structurei

Secondary structure

1
106
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 118Combined sources
Helixi13 – 2917Combined sources
Beta strandi34 – 407Combined sources
Helixi41 – 433Combined sources
Helixi44 – 485Combined sources
Beta strandi52 – 565Combined sources
Helixi58 – 636Combined sources
Helixi64 – 707Combined sources
Beta strandi71 – 744Combined sources
Beta strandi76 – 783Combined sources
Helixi81 – 855Combined sources
Helixi89 – 10416Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E2BNMR-A1-106[»]
1H9CNMR-A1-106[»]
1IIBX-ray1.80A/B1-106[»]
2WWVNMR-D3-105[»]
2WY2NMR-D3-105[»]
ProteinModelPortaliP69795.
SMRiP69795. Positions 3-93.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69795.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 106104PTS EIIB type-3PROSITE-ProRule annotationAdd
BLAST

Domaini

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.

Sequence similaritiesi

Contains 1 PTS EIIB type-3 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105VZJ. Bacteria.
COG1440. LUCA.
HOGENOMiHOG000224223.
InParanoidiP69795.
KOiK02760.
OMAiYKIWAVS.
OrthoDBiEOG6DVJZD.
PhylomeDBiP69795.

Family and domain databases

InterProiIPR003501. PTS_EIIB_2/3.
IPR013012. PTS_EIIB_3.
[Graphical view]
PfamiPF02302. PTS_IIB. 1 hit.
[Graphical view]
SUPFAMiSSF52794. SSF52794. 1 hit.
TIGRFAMsiTIGR00853. pts-lac. 1 hit.
PROSITEiPS51100. PTS_EIIB_TYPE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P69795-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKKHIYLFC SAGMSTSLLV SKMRAQAEKY EVPVIIEAFP ETLAGEKGQN
60 70 80 90 100
ADVVLLGPQI AYMLPEIQRL LPNKPVEVID SLLYGKVDGL GVLKAAVAAI

KKAAAN
Length:106
Mass (Da):11,427
Last modified:May 10, 2005 - v1
Checksum:iDE4AADE300D18F53
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52890 Genomic DNA. Translation: CAA37069.1.
U00096 Genomic DNA. Translation: AAC74808.1.
AP009048 Genomic DNA. Translation: BAA15519.1.
PIRiS10870.
RefSeqiNP_416252.1. NC_000913.3.
WP_000412169.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74808; AAC74808; b1738.
BAA15519; BAA15519; BAA15519.
GeneIDi945339.
KEGGiecj:JW1727.
eco:b1738.
PATRICi32118785. VBIEscCol129921_1810.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52890 Genomic DNA. Translation: CAA37069.1.
U00096 Genomic DNA. Translation: AAC74808.1.
AP009048 Genomic DNA. Translation: BAA15519.1.
PIRiS10870.
RefSeqiNP_416252.1. NC_000913.3.
WP_000412169.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E2BNMR-A1-106[»]
1H9CNMR-A1-106[»]
1IIBX-ray1.80A/B1-106[»]
2WWVNMR-D3-105[»]
2WY2NMR-D3-105[»]
ProteinModelPortaliP69795.
SMRiP69795. Positions 3-93.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260316. 10 interactions.
IntActiP69795. 1 interaction.
STRINGi511145.b1738.

Protein family/group databases

TCDBi4.A.3.2.1. the pts lactose-n,n'-diacetylchitobiose--glucoside (lac) family.

Proteomic databases

PaxDbiP69795.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74808; AAC74808; b1738.
BAA15519; BAA15519; BAA15519.
GeneIDi945339.
KEGGiecj:JW1727.
eco:b1738.
PATRICi32118785. VBIEscCol129921_1810.

Organism-specific databases

EchoBASEiEB0138.
EcoGeneiEG10140. chbB.

Phylogenomic databases

eggNOGiENOG4105VZJ. Bacteria.
COG1440. LUCA.
HOGENOMiHOG000224223.
InParanoidiP69795.
KOiK02760.
OMAiYKIWAVS.
OrthoDBiEOG6DVJZD.
PhylomeDBiP69795.

Enzyme and pathway databases

BioCyciEcoCyc:CELA-MONOMER.
ECOL316407:JW1727-MONOMER.
MetaCyc:CELA-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP69795.
PROiP69795.

Family and domain databases

InterProiIPR003501. PTS_EIIB_2/3.
IPR013012. PTS_EIIB_3.
[Graphical view]
PfamiPF02302. PTS_IIB. 1 hit.
[Graphical view]
SUPFAMiSSF52794. SSF52794. 1 hit.
TIGRFAMsiTIGR00853. pts-lac. 1 hit.
PROSITEiPS51100. PTS_EIIB_TYPE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization and nucleotide sequence of the cryptic cel operon of Escherichia coli K12."
    Parker L.L., Hall B.G.
    Genetics 124:455-471(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "The cellobiose permease of Escherichia coli consists of three proteins and is homologous to the lactose permease of Staphylococcus aureus."
    Reizer J., Reizer A., Saier M.H. Jr.
    Res. Microbiol. 141:1061-1067(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, CATALYTIC ACTIVITY.
  6. "Wild-type Escherichia coli grows on the chitin disaccharide, N,N'-diacetylchitobiose, by expressing the cel operon."
    Keyhani N.O., Roseman S.
    Proc. Natl. Acad. Sci. U.S.A. 94:14367-14371(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF CHB OPERON.
  7. "The chitin disaccharide, N,N'-diacetylchitobiose, is catabolized by Escherichia coli and is transported/phosphorylated by the phosphoenolpyruvate:glycose phosphotransferase system."
    Keyhani N.O., Wang L.-X., Lee Y.C., Roseman S.
    J. Biol. Chem. 275:33084-33090(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  8. "The transport/phosphorylation of N,N'-diacetylchitobiose in Escherichia coli. Characterization of phospho-IIB(Chb) and of a potential transition state analogue in the phosphotransfer reaction between the proteins IIA(Chb) and IIB(Chb)."
    Keyhani N.O., Bacia K., Roseman S.
    J. Biol. Chem. 275:33102-33109(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, CATALYTIC ACTIVITY.
  9. "Analytical sedimentation of the IIAChb and IIBChb proteins of the Escherichia coli N,N'-diacetylchitobiose phosphotransferase system. Demonstration of a model phosphotransfer transition state complex."
    Keyhani N.O., Rodgers M.E., Demeler B., Hansen J.C., Roseman S.
    J. Biol. Chem. 275:33110-33115(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  10. "Enzyme IIBcellobiose of the phosphoenol-pyruvate-dependent phosphotransferase system of Escherichia coli: backbone assignment and secondary structure determined by three-dimensional NMR spectroscopy."
    Ab E., Schuurman-Wolters G.K., Saier M.H. Jr., Reizer J., Jacuinod M., Roepstorff P., Dijkstra K., Scheek R.M., Robillard G.T.
    Protein Sci. 3:282-290(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  11. "The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli."
    Ab E., Schuurman-Wolters G.K., Reizer J., Saier M.H. Jr., Dijkstra K., Scheek R.M., Robillard G.T.
    Protein Sci. 6:304-314(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF MUTANT SER-10.
  12. "The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases."
    van Montfort R.L.M., Pijning T., Kalk K.H., Reizer J., Saier M.H. Jr., Thunnissen M.M.G.M., Robillard G.T., Dijkstra B.W.
    Structure 5:217-225(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Entry informationi

Entry nameiPTQB_ECOLI
AccessioniPrimary (citable) accession number: P69795
Secondary accession number(s): P17409
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 10, 2005
Last modified: May 11, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally (PubMed:2092358) characterized as part of a cryptic cel operon for a cellobiose degradation system. The Cel+ phenotype is due to mutations making expression chitobiose-independent and altering the substrate specificity.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.