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Reviewed, UniProtKB/Swiss-Prot P45597 (PTFAX_XANCP)

Last modified November 3, 2009. Version 86. 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:
    Multiphosphoryl transfer protein
      Short name=MTP
Including the following 3 domains:
    1- Recommended name:
            Phosphoenolpyruvate-protein phosphotransferase
              EC=2.7.3.9
        Alternative name(s):
            Phosphotransferase system enzyme I
    2- Recommended name:
            Phosphocarrier protein HPr
                Short name=Protein H
    3- Recommended name:
            Fructose-specific phosphotransferase enzyme IIA component
              EC=2.7.1.-
        Alternative name(s):
            PTS system fructose-specific EIIA component
            EIII-Fru
Gene names
Name: fruB
Ordered Locus Names: XCC2370
OrganismXanthomonas campestris pv. campestris [Complete proteome] [HAMAP]
Taxonomic identifier340 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length838 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine.

Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.

Subcellular location

Cytoplasm Potential.

Domain

The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.

Sequence similarities

Belongs to the PEP-utilizing enzyme family.

Contains 1 HPr domain.

Contains 1 PTS EIIA type-2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 838838Multiphosphoryl transfer protein
PRO_0000186514

Regions

Domain7 – 147141PTS EIIA type-2
Domain161 – 25393HPr
Region274 – 838565PTS EI
Compositional bias700 – 7056Poly-Ala

Sites

Active site671Tele-phosphohistidine intermediate; for EIIA activity By similarity
Active site1751Pros-phosphohistidine intermediate; for HPr activity By similarity
Active site4601Tele-phosphohistidine intermediate; for PTS EI activity By similarity

Experimental info

Sequence conflict1151L → V in CAA85482. Ref.1
Sequence conflict4121P → A in CAA85482. Ref.1
Sequence conflict5051L → Q in CAA85482. Ref.1
Sequence conflict561 – 5622EG → N in CAA85482. Ref.1
Sequence conflict5861Q → H in CAA85482. Ref.1
Sequence conflict5931R → Q in CAA85482. Ref.1
Sequence conflict5961D → N in CAA85482. Ref.1
Sequence conflict6181L → S in CAA85482. Ref.1
Sequence conflict634 – 6352LL → SS in CAA85482. Ref.1
Sequence conflict6451L → S in CAA85482. Ref.1
Sequence conflict6801R → A in CAA85482. Ref.1
Sequence conflict6861D → H in CAA85482. Ref.1
Sequence conflict7411D → S in CAA85482. Ref.1
Sequence conflict8201Q → H in CAA85482. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P45597-1 [UniParc].

Last modified July 11, 2002. Version 3.
Checksum: 78C87FDBA2E4DF42

FASTA83888,747
        10         20         30         40         50         60 
MSSPSIAPVT PDLVRLRATA RDKDDAIAQA AQLLVAAGCV APGYDASMRR REGLANTFLG 

        70         80         90        100        110        120 
HGLAIPHGVG EDRHLVRRDG IAVLQLPEGV EWNPGQTTRL VVGIAAQSDT HITLLRRLTR 

       130        140        150        160        170        180 
LIQDPAQLEA LFTTDDPAVI VAALTGDRAP DTSAAPATDL AERFEWTIAY PSGLHARPAT 

       190        200        210        220        230        240 
RWAETARGFS ARAQVRAGDQ AADAKSLVGL LQLGLRAGDS ITVSAKGSDA PALLKRLRAV 

       250        260        270        280        290        300 
MDSLTAQEKA DAERAAQRRA APVIGWTPPQ AQPAIVGIGA SPGVAIGIVH RLRAAQTEVA 

       310        320        330        340        350        360 
DQPIGLGDGG VLLHDALTRT RQQLAAIQDD TQRRLGASDA AIFKAQAELL NDTDLITRTC 

       370        380        390        400        410        420 
QLMVEGHGVA WSWHQAVEQI ASGLAALGNP VLAGRAADLR DVGRRVLAQL DPAAAGAGLT 

       430        440        450        460        470        480 
DLPEQPCILL AGDLSPSDTA NLDTDCVLGL ATAQGGPTSH TAILSRTLGL PALVAAGGQL 

       490        500        510        520        530        540 
LDIEDGVTAI IDGSSGRLYI NPSELDLDAA RTHIAEQQAI REREAAQRAL PAETTDGHHI 

       550        560        570        580        590        600 
DIGANVNLPE QVAMALTQGA EGVGLMRTEF LFLERGSTPT EDEQYQTYLA MARALDGRPL 

       610        620        630        640        650        660 
IVRALDIGGD KQVAHLELPH EENPFLGVRG ARLLLRRPDL LEPQLRALYR AAKDGARLSI 

       670        680        690        700        710        720 
MFPMITSVPE LISLREICAR IRAELDAPEL PIGIMIEVPA AAAQADVLAR HADFFSIGTN 

       730        740        750        760        770        780 
DLTQYVLAID RQNPELAAEA DSLHPAVLRM IRSTIDGARK HDRWVGVCGG LAGDPFGASL 

       790        800        810        820        830 
LAGLGVQELS MTPNDIPAVK ARLRGRALSA LQQLAEQALQ CETAEQVRAL EAQREGQA 

« Hide

References

« Hide 'large scale' references
[1]"Fructose phosphotransferase system of Xanthomonas campestris pv. campestris: characterization of the fruB gene."
de Crecy-Lagard V., Binet M., Danchin A.
Microbiology 141:2253-2260(1995) [PubMed: 7496537] [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]"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] OF 825-838.
Strain: ATCC 13951 / NCIB 11803 / NRRL B-1459.

Cross-references

Sequence databases

Z37113 Genomic DNA. Translation: CAA85482.1.
AE008922 Genomic DNA. Translation: AAM41648.1.
M69242 Genomic DNA. Translation: AAA27600.1.
PIRC40944.
S51680.
RefSeqNP_637724.1.

3D structure databases

HSSPHSSP built from PDB template 1POH based on UniProtKB P07006.
ModBaseSearch...

Genome annotation databases

GeneID998532.
GenomeReviewsGene locus XCC2370 in contig AE008922_GR.
KEGGxcc:XCC2370.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP45597.
OMAGVCGELA.

Enzyme and pathway databases

BioCycXCAM190485:XCC2370-MON.
BRENDA2.7.3.9. 281360.

Family and domain databases

InterProIPR008279. PEP_mobile.
IPR018274. PEP_mobile_CS.
IPR006318. PEP_P_trans.
IPR000121. PEP_utilizers.
IPR002178. PTS_EIIA_2.
IPR001020. PTS_HPr_His_P_site.
IPR005698. PTS_HPr_prot.
IPR000032. PTS_HPr_prot-like.
IPR002114. PTS_HPr_Ser_P_site.
IPR008731. PTS_PEP_utilis_N.
IPR015813. Pyrv/PenolPyrv_Kinase_cat.
[Graphical view]
Gene3DG3DSA:3.40.930.10. PTS_EIIA_2. 1 hit.
G3DSA:3.30.1340.10. PTS_HPr_protein. 1 hit.
G3DSA:1.10.274.10. PTS_PEP_utilis_N. 1 hit.
G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
PfamPF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
PF00381. PTS-HPr. 1 hit.
PF00359. PTS_EIIA_2. 1 hit.
[Graphical view]
PRINTSPR00107. PHOSPHOCPHPR.
PR01736. PHPHTRNFRASE.
ProDomPD002238. HPr_protein. 1 hit.
PD000940. PEP_utilizers. 1 hit.
PD001689. PTS_EIIA_2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01003. PTS_HPr_family. 1 hit.
TIGR01417. PTS_I_fam. 1 hit.
PROSITEPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
PS51094. PTS_EIIA_TYPE_2. 1 hit.
PS00372. PTS_EIIA_TYPE_2_HIS. 1 hit.
PS51350. PTS_HPR_DOM. 1 hit.
PS00369. PTS_HPR_HIS. 1 hit.
PS00589. PTS_HPR_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTFAX_XANCP
AccessionPrimary (citable) accession number: P45597
Secondary accession number(s): Q03397
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 11, 2002
Last modified: November 3, 2009
This is version 86 of the entry and version 3 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