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Reviewed, UniProtKB/Swiss-Prot P23355 (PTFBC_XANCP)

Last modified June 16, 2009. Version 77. 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:
    PTS system fructose-specific EIIBC component
Alternative name(s):
    EIIBC-Fru
      Short name=EII-Fru
Including the following 2 domains:
    1- Recommended name:
            Fructose-specific phosphotransferase enzyme IIB component
              EC=2.7.1.69
        Alternative name(s):
            PTS system fructose-specific EIIB component
    2- Recommended name:
            Fructose permease IIC component
        Alternative name(s):
            PTS system fructose-specific EIIC component
Gene names
Name: fruA
Ordered Locus Names: XCC2372
OrganismXanthomonas campestris pv. campestris [Complete proteome] [HAMAP]
Taxonomic identifier340 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length580 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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. 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 membrane; Multi-pass membrane protein.

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 – 580580PTS system fructose-specific EIIBC component
PRO_0000186515

Regions

Transmembrane254 – 27421 Potential
Transmembrane289 – 30921 Potential
Transmembrane332 – 35221 Potential
Transmembrane369 – 38921 Potential
Transmembrane410 – 43021 Potential
Transmembrane451 – 47121 Potential
Transmembrane483 – 50321 Potential
Transmembrane509 – 52921 Potential
Transmembrane549 – 57123 Potential
Domain120 – 21596PTS EIIB type-2
Domain243 – 580338PTS EIIC type-2

Sites

Active site1261Phosphocysteine intermediate; for EIIB activity By similarity

Experimental info

Sequence conflict1501Q → H in AAA27602. Ref.1
Sequence conflict260 – 2645AGGLL → LAACW in AAA27602. Ref.1
Sequence conflict3501V → L in AAA27602. Ref.1
Sequence conflict408 – 4092GS → AG in AAA27602. Ref.1
Sequence conflict494 – 4952VT → DS in AAA27602. Ref.1
Sequence conflict5681L → V in AAA27602. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P23355-1 [UniParc].

Last modified July 11, 2002. Version 2.
Checksum: E6A3B52A7F45662B

FASTA58058,647
        10         20         30         40         50         60 
MSSSIVVIAA GERSTEAVLA AEALRRAATA AGRSVTIEIR SDQGVLGALP TELTNGAAHV 

        70         80         90        100        110        120 
LIVGDADADT ARFGDAQLLH LSLGAVLDDP AAAVSQLAAT TAPASTSATT DASGAGGKRI 

       130        140        150        160        170        180 
VAITSCPTGI AHTFMAAEGL QQAAKKLGYQ MRVETQGSVG AQDALTDEEI RAADVVIIAA 

       190        200        210        220        230        240 
DREVDLARFG GKRLFKSGTK PAINDGPALI QKALAEAGVH GGAAPVAGAN ATSDAKGNAR 

       250        260        270        280        290        300 
TGAYKHLMTG VSFMLPFVTA GGLLIALAFA LGGIYAGDDA HQGTLAWSLF QIGAKAGFTL 

       310        320        330        340        350        360 
MVPALAGYIA YSIADRPGIA PGMIGGLVAA NLNAGFLGGI IAGFIAGYGV AALNRYIKLP 

       370        380        390        400        410        420 
RNLEGLKPVL ILPVLGTLLV GLAMMYVFGQ PVADLLAWLT AWLRGMQGSS ALLLGLLLGG 

       430        440        450        460        470        480 
MMAFDMGGPV NKAAYAFSTG LIASQVYTPM AAAMVAGMTP PLGIALATWV FRNRFTVEER 

       490        500        510        520        530        540 
GSATAAGVLG LAFVTEGAIP YAARDPLRTI PALVIGSAVA GAISMTAGAE LKAPHGGIFV 

       550        560        570        580 
LLIPNAVTHL LNYVLALVVG VVVTAVALRL LKKPVADVIA 

« Hide

References

« Hide 'large scale' references
[1]"Fructose catabolism in Xanthomonas campestris pv. campestris. Sequence of the PTS operon, characterization of the fructose-specific enzymes."
de Crecy-Lagard V., Bouvet O.M., Lejeune P., Danchin A.
J. Biol. Chem. 266:18154-18161(1991) [PubMed: 1655739] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13951 / NCIB 11803 / NRRL B-1459.
[2]"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities."
da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. expand/collapse author list , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.
Nature 417:459-463(2002) [PubMed: 12024217] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33913 / NCPPB 528 / LMG 568.
[3]"Identification of two fructose transport and phosphorylation pathways in Xanthomonas campestris pv. campestris."
de Crecy-Lagard V., Lejeune P., Bouvet O.M., Danchin A.
Mol. Gen. Genet. 227:465-472(1991) [PubMed: 1650911] [Abstract]
Cited for: PROTEIN SEQUENCE OF 404-547.

Cross-references

Sequence databases

M69242 Genomic DNA. Translation: AAA27602.1.
AE012346 Genomic DNA. Translation: AAM41650.1.
PIRB40944.
RefSeqNP_637726.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID998895.
GenomeReviewsGene locus XCC2372 in contig AE008922_GR.
KEGGxcc:XCC2372.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP23355.
OMAP23355. TGLVMIY.

Enzyme and pathway databases

BioCycXCAM190485:XCC2372-MON.
BRENDA2.7.1.69. 281360.

Family and domain databases

InterProIPR013011. PTS_EIIB_2.
IPR003352. PTS_EIIC.
IPR013014. PTS_EIIC_2.
IPR003353. PTS_IIB_fruc.
IPR006327. PTS_IIC_fruc.
[Graphical view]
PfamPF02378. PTS_EIIC. 1 hit.
PF02379. PTS_IIB_fruc. 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_XANCP
AccessionPrimary (citable) accession number: P23355
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: July 11, 2002
Last modified: June 16, 2009
This is version 77 of the entry and version 2 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