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Reviewed, UniProtKB/Swiss-Prot P55901 (PTEB_AERHY)

Last modified September 22, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cellobiose-specific phosphotransferase enzyme IIB component
    EC=2.7.1.69
Alternative name(s):
    PTS system cellobiose-specific EIIB component
    EIIB-Cel
Gene names
Name: celA
OrganismAeromonas hydrophila
Taxonomic identifier644 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Protein attributes

Sequence length88 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
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 cellobiose transport.

Catalytic activity

Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.

Subcellular location

Cytoplasm Potential.

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.

Sequence similarities

Contains 1 PTS EIIB type-3 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›88›88Cellobiose-specific phosphotransferase enzyme IIB component
PRO_0000186488

Regions

Domain3 – ›88›86PTS EIIB type-3

Sites

Active site101Phosphocysteine intermediate By similarity

Experimental info

Non-terminal residue881

Sequences

Sequence LengthMass (Da)Tools
P55901-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 2EA61F78BD1F30DF

FASTA889,716
        10         20         30         40         50         60 
MEKKRIYLFC SAGMSTSLLV SKMKAQAEKY DVPVLIDAYP ETLAGEKGQD ADLVLLGPQI 

        70         80 
AYMLPEIQQQ LPGKPVEVID TLLYGKVD 

« Hide

References

[1]"Isolation and analysis of eight exe genes and their involvement in extracellular protein secretion and outer membrane assembly in Aeromonas hydrophila."
Howard S.P., Critch J., Bedi A.
J. Bacteriol. 175:6695-6703(1993) [PubMed: 8407845] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Ah65.
[2]"Novel phosphotransferases system genes revealed by bacterial genome analysis: operons encoding homologues of sugar-specific permease domains of the phosphotransferase system and pentose catabolic enzymes."
Reizer J., Charbit A., Reizer A., Saier M.H. Jr.
Genome Sci. Technol. 1:53-75(1996)
Cited for: IDENTIFICATION.

Cross-references

Sequence databases

X66504 Genomic DNA. No translation available.
PIRH49905.

3D structure databases

HSSPHSSP built from PDB template 1H9C based on UniProtKB P17409.
SMRP55901. Positions 3-88.
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.7.1.69. 3060.

Family and domain databases

InterProIPR014350. PTrfase_system_EIIB_3_subgr.
IPR013012. PTS_EIIB_3.
IPR003501. PTS_IIB_lac.
[Graphical view]
PfamPF02302. PTS_IIB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00853. pts-lac. 1 hit.
PROSITEPS51100. PTS_EIIB_TYPE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTEB_AERHY
AccessionPrimary (citable) accession number: P55901
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 22, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents