Reviewed, UniProtKB/Swiss-Prot P69816 (PTFB2_ECOLI)

Names and origin

Protein names

Recommended name:
    Fructose-like phosphotransferase enzyme IIB component 2
    EC=2.7.1.69
Alternative name(s):
    PTS system fructose-like EIIB component 2

Gene names

Name:	frwB
Synonyms:	yijK
Ordered Locus Names:	b3950, JW3922

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	106 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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 By similarity.
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-2 domain.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cytoplasm
Molecular function	Kinase Transferase
Technical term	Complete proteome
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 membrane Inferred from electronic annotation. Source: InterPro
Molecular function	kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein-N(PI)-phosphohistidine-sugar phosphotransferase activity Inferred from electronic annotation. Source: EC sugar:hydrogen symporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
nadE	P18843	1	EBI-1134271,EBI-548960

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 106	106	Fructose-like phosphotransferase enzyme IIB component 2		PRO_0000186501
Regions
	Domain	1 – 103	103	PTS EIIB type-2
Sites
	Active site	10	1	Phosphocysteine intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P69816-1 [UniParc]. Last modified May 10, 2005. Version 1. Checksum: F712189F18489D3D	FASTA	106	11,248
	10 20 30 40 50 60 MTKIIAVTAC PSGVAHTYMA AEALESAAKA KGWEVKVETQ GSIGLENELT AEDVASADMV 70 80 90 100 ILTKDIGIKF EERFAGKTIV RVNISDAVKR ADAIMSKIEA HLAQTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[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]	"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.
[4]	"Novel phosphotransferase system genes revealed by bacterial genome analysis -- a gene cluster encoding a unique Enzyme I and the proteins of a fructose-like permease system." Reizer J., Reizer A., Saier M.H. Jr. Microbiology 141:961-971(1995) [PubMed: 7773398] [Abstract] Cited for: DISCUSSION OF SEQUENCE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00006 Genomic DNA. Translation: AAC43056.1. U00096 Genomic DNA. Translation: AAC76932.1. AP009048 Genomic DNA. Translation: BAE77361.1.
PIR	A65202.
RefSeq	AP_003860.1. NP_418385.1.
3D structure databases
SMR	P69816. Positions 2-100.
ModBase	Search...
Protein-protein interaction databases
IntAct	P69816. 1 interaction.
STRING	P69816.
Protein family/group databases
TCDB	4.A.2.1.10. PTS fructose-mannitol (Fru) family.
Genome annotation databases
GeneID	948447.
GenomeReviews	Gene locus JW3922 in contig AP009048_GR. Gene locus b3950 in contig U00096_GR.
KEGG	ecj:JW3922. eco:b3950.
Organism-specific databases
EchoBASE	EB1853.
EcoGene	EG11909. frwB.
CMR	Search...
Phylogenomic databases
eggNOG	COG1445.
HOGENOM	HBG564028.
OMA	IENQLTP.
Enzyme and pathway databases
BioCyc	EcoCyc:FRWB-MONOMER. ECOL168927:B3950-MONOMER.
Gene expression databases
Genevestigator	P69816.
Family and domain databases
InterPro	IPR013011. PTS_EIIB_2. IPR003501. PTS_EIIB_2/3. IPR003353. PTS_IIB_fruc. [Graphical view]
Pfam	PF02302. PTS_IIB. 1 hit. [Graphical view]
TIGRFAMs	TIGR00829. FRU. 1 hit.
PROSITE	PS51099. PTS_EIIB_TYPE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PTFB2_ECOLI

Accession

Primary (citable) accession number: P69816
Secondary accession number(s): P32673, Q2M8P5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	May 10, 2005
Last modified:	February 9, 2010
This is version 43 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)