Skip Header

Contribute Send feedback
Read comments (?) or add your own

P44714 (PTFBC_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 91. Feed History...

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

Including the following 2 domains:

  1. Fructose-specific phosphotransferase enzyme IIB component
    EC=2.7.1.69
    Alternative name(s):
    EIII-Fru
    PTS system fructose-specific EIIB component
  2. Fructose permease IIC component
    Alternative name(s):
    PTS system fructose-specific EIIC component
Gene names
Name:fruA
Ordered Locus Names:HI_0446
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length556 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 fructose 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 By similarity.

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-2 domain.

Contains 1 PTS EIIC type-2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 556556PTS system fructose-specific EIIBC component
PRO_0000186509

Regions

Transmembrane237 – 25721Helical; Potential
Transmembrane275 – 29521Helical; Potential
Transmembrane302 – 32221Helical; Potential
Transmembrane324 – 34421Helical; Potential
Transmembrane349 – 36921Helical; Potential
Transmembrane390 – 41021Helical; Potential
Transmembrane431 – 45121Helical; Potential
Transmembrane468 – 48821Helical; Potential
Transmembrane490 – 51021Helical; Potential
Transmembrane529 – 54921Helical; Potential
Domain106 – 20196PTS EIIB type-2
Domain224 – 556333PTS EIIC type-2

Sites

Active site1121Phosphocysteine intermediate; for EIIB activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P44714 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 31D8E77BFDBA7E42

FASTA55657,706
        10         20         30         40         50         60 
MKLFLTQSAN VGDVKAYLLH EVFRAAAQKA NVSIVGTPAE ADLVLVFGSV LPNNPDLVGK 

        70         80         90        100        110        120 
KVFIIGEAIA MISPEVTLAN ALANGADYVA PKSAVSFTGV SGVKNIVAVT ACPTGVAHTF 

       130        140        150        160        170        180 
MSAEAIEAYA KKQGWNVKVE TRGQVGAGNE ITVEEVAAAD LVFVAADIDV PLDKFKGKPM 

       190        200        210        220        230        240 
YRTSTGLALK KTEQEFDKAF KEAKIFDGGN NAGTKEESRE KKGVYKHLMT GVSHMLPLVV 

       250        260        270        280        290        300 
AGGLLIAISF MFSFNVIENT GVFQDLPNML INIGSGVAFK LMIAVFAGYV AFSIADRPGL 

       310        320        330        340        350        360 
AVGLIAGMLA SEAGAGILGG IIAGFLAGYV VKGLNVIIRL PASLTSLKPI LILPLLGSMI 

       370        380        390        400        410        420 
VGLTMIYLIN PPVAEIMKEL SNWLTSMGEV NAIVLGAIIG AMMCIDMGGP VNKAAYTFSV 

       430        440        450        460        470        480 
GLIASQVYTP MAAAMAAGMV PPIGMTVATW IARNKFTVSQ CDAGKASFVL GLCFISEGAL 

       490        500        510        520        530        540 
PFVAADPIRV IISSVIGGAV AGAISMGLNI TLQAPHGGLF VIPFVSEPLK YLGAIAIGAL 

       550 
STGVVYAIIK SKNNAE

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42023 Genomic DNA. Translation: AAC22105.1.
PIRI64068.
RefSeqNP_438607.1. NC_000907.1.

3D structure databases

ProteinModelPortalP44714.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID949670.
GenomeReviewsGene locus HI_0446 in contig L42023_GR.
KEGGhin:HI0446.
NMPDRfig|71421.1.peg.420.
PATRIC20189447. VBIHaeInf48452_0466.
TIGRHI_0446.

Phylogenomic databases

HOGENOMHBG704192.
OMAINHALLY.
ProtClustDBCLSK892369.

Enzyme and pathway databases

BioCycHINF71421:HI_0446-MONOMER.

Family and domain databases

InterProIPR013011. PTS_EIIB_2.
IPR003501. PTS_EIIB_2/3.
IPR003352. PTS_EIIC.
IPR013014. PTS_EIIC_2.
IPR003353. PTS_IIB_fruc.
IPR006327. PTS_IIC_fruc.
[Graphical view]
KOK02769.
K02770.
PfamPF02378. PTS_EIIC. 1 hit.
PF02302. PTS_IIB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00829. FRU. 1 hit.
TIGR01427. PTS_IIC_fructo. 1 hit.
PROSITEPS51099. PTS_EIIB_TYPE_2. 1 hit.
PS51104. PTS_EIIC_TYPE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTFBC_HAEIN
AccessionPrimary (citable) accession number: P44714
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 25, 2012
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

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