Reviewed, UniProtKB/Swiss-Prot Q45399 (PTEB_BACST)

Names and origin

Protein names

Recommended 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

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	100 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Predicted.

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.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cytoplasm
Molecular function	Kinase Transferase
Gene Ontology (GO)
Biological process	phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein-N(PI)-phosphohistidine-sugar phosphotransferase activity Inferred from electronic annotation. Source: EC sugar binding Inferred from electronic annotation. Source: InterPro sugar:hydrogen symporter activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 100	100	Cellobiose-specific phosphotransferase enzyme IIB component		PRO_0000186486
Regions
	Domain	1 – 100	100	PTS EIIB type-3
Sites
	Active site	7	1	Phosphocysteine intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q45399-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 7CCD2F32C72F1747	FASTA	100	10,737
	10 20 30 40 50 60 MNILLICAAG MSTSLLVTKM KEAAKQKGIE ANIWAVSADE AKSHLDQADV VLIGPQIRYK 70 80 90 100 LAAFKKEGEA RGIPVDVINP ADYGRVNGAG VLDFALRLKK

References

[1]

"Cloning and sequencing of a cellobiose phosphotransferase system operon from Bacillus stearothermophilus XL-65-6 and functional expression in Escherichia coli." Lai X., Ingram L.O. J. Bacteriol. 175:6441-6450(1993) [PubMed: 8407820] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: XL-65-6.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U07818 Unassigned DNA. Translation: AAA17389.1.
PIR	B49898.
3D structure databases
HSSP	HSSP built from PDB template 1IIB based on UniProtKB P17409.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.7.1.69. 266715.
Family and domain databases
InterPro	IPR014350. PTrfase_system_EIIB_3_subgr. IPR013012. PTS_EIIB_3. IPR003501. PTS_IIB_lac. [Graphical view]
Pfam	PF02302. PTS_IIB. 1 hit. [Graphical view]
TIGRFAMs	TIGR00853. pts-lac. 1 hit.
PROSITE	PS51100. PTS_EIIB_TYPE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PTEB_BACST

Accession

Primary (citable) accession number: Q45399

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)