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P71012 (PTF3A_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PTS system fructose-specific EIIABC component
Alternative name(s):
EIIABC-Fru

Including the following 3 domains:

  1. Fructose-specific phosphotransferase enzyme IIA component
    EC=2.7.1.-
    Alternative name(s):
    EII-Fru
    PTS system fructose-specific EIIA component
  2. Fructose-specific phosphotransferase enzyme IIB component
    EC=2.7.1.69
    Alternative name(s):
    EIII-Fru
    PTS system fructose-specific EIIB component
  3. Fructose permease IIC component
    Alternative name(s):
    PTS system fructose-specific EIIC component
Gene names
Name:fruA
Ordered Locus Names:BSU14400
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length635 AA.
Sequence statusComplete.
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 By similarity.

Catalytic activity

Protein EIIA N(pi)-phospho-L-histidine + protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-histidine/cysteine.

Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate.

Subcellular location

Cell membrane; Multi-pass membrane protein Potential.

Domain

The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB 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 EIIA type-2 domain.

Contains 1 PTS EIIB type-2 domain.

Contains 1 PTS EIIC type-2 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ykoTO347553EBI-5242378,EBI-5242987

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 635635PTS system fructose-specific EIIABC component
PRO_0000360665

Regions

Transmembrane312 – 33221Helical; Potential
Transmembrane350 – 37021Helical; Potential
Transmembrane392 – 41221Helical; Potential
Transmembrane428 – 44821Helical; Potential
Transmembrane470 – 49021Helical; Potential
Transmembrane511 – 53121Helical; Potential
Transmembrane544 – 56421Helical; Potential
Transmembrane569 – 58921Helical; Potential
Transmembrane608 – 62821Helical; Potential
Domain5 – 149145PTS EIIA type-2
Domain172 – 26796PTS EIIB type-2
Domain301 – 635335PTS EIIC type-2

Sites

Active site671Tele-phosphohistidine intermediate; for EIIA activity By similarity
Active site1781Phosphocysteine intermediate; for EIIB activity By similarity

Secondary structure

1 ................. 635
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P71012 [UniParc].

Last modified June 1, 1998. Version 2.
Checksum: 753F12C2AFDD7F84

FASTA63567,184
        10         20         30         40         50         60 
MKITELLTKH TIKLNIESKE KENVIDEMVT VLDKAGKLND RQAYKEAILN RESQSSTGIG 

        70         80         90        100        110        120 
EGIAIPHAKT ASVINPAIAF GRSKDGVDYE SLDGQPAHLV FMIAATEGAN NTHLEALSRL 

       130        140        150        160        170        180 
STLLMREEIR KQLLEAESED AIIDIINQHD KDDDEEEEEE EAAPAPAGKG KILAVTACPT 

       190        200        210        220        230        240 
GIAHTFMAAD ALKEKAKELG VEIKVETNGS SGIKHKLTAQ EIEDAPAIIV AADKQVEMER 

       250        260        270        280        290        300 
FKGKRVLQVP VTAGIRRPQE LIEKAMNQDA PIYQGSGGGS AASNDDEEAK GKSGSGIGNT 

       310        320        330        340        350        360 
FYKHLMSGVS NMLPFVVGGG ILVAISFFWG IHSADPNDPS YNTFAAALNF IGGDNALKLI 

       370        380        390        400        410        420 
VAVLAGFIAM SIADRPGFAP GMVGGFMATQ ANAGFLGGLI AGFLAGYVVI LLKKVFTFIP 

       430        440        450        460        470        480 
QSLDGLKPVL IYPLFGIFIT GVLMQFVVNT PVAAFMNFLT NWLESLGTGN LVLMGIILGG 

       490        500        510        520        530        540 
MMAIDMGGPL NKAAFTFGIA MIDAGNYAPH AAIMAGGMVP PLGIALATTI FRNKFTQRDR 

       550        560        570        580        590        600 
EAGITCYFMG AAFVTEGAIP FAAADPLRVI PAAVVGAAVA GGLTEFFRVT LPAPHGGVFV 

       610        620        630 
AFITNHPMLY LLSIVIGAVV MAIILGIVKK PVTEK

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of the mobA-ampS region of the Bacillus subtilis chromosome."
Caldwell R.M., Ferrari E.
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"The structure of a domain of fruA from Bacillus subtilis."
Midwest center for structural genomics (MCSG)
Submitted (SEP-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 171-273.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF012285 Genomic DNA. Translation: AAC24915.1.
AL009126 Genomic DNA. Translation: CAB13313.1.
PIRH69626.
RefSeqNP_389323.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2R4QX-ray1.60A171-273[»]
ProteinModelPortalP71012.
SMRP71012. Positions 3-147, 170-273.
ModBaseSearch...

Protein-protein interaction databases

IntActP71012. 36 interactions.

Protein family/group databases

TCDB4.A.2.1.4. PTS fructose-mannitol (Fru) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000001398; EBBACP00000001398; EBBACG00000001396.
GeneID938757.
GenomeReviewsGene locus BSU14400 in contig AL009126_GR.
KEGGbsu:BSU14400.
NMPDRfig|224308.1.peg.1442.
PATRIC18974669. VBIBacSub10457_1526.

Organism-specific databases

GenoListBSU14400. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000000031.
HOGENOMHBG704192.
OMAMPGFVGG.
PhylomeDBP71012.
ProtClustDBCLSK887234.

Enzyme and pathway databases

BioCycBSUB:BSU14400-MONOMER.

Family and domain databases

InterProIPR016152. PTrfase/Anion_transptr.
IPR002178. PTS_EIIA_2.
IPR013011. PTS_EIIB_2.
IPR003501. PTS_EIIB_2/3.
IPR003352. PTS_EIIC.
IPR013014. PTS_EIIC_2.
IPR004715. PTS_IIA_fruc.
IPR003353. PTS_IIB_fruc.
IPR006327. PTS_IIC_fruc.
[Graphical view]
Gene3DG3DSA:3.40.930.10. PTS_EIIA_2. 1 hit.
KOK02768.
K02769.
K02770.
PfamPF00359. PTS_EIIA_2. 1 hit.
PF02378. PTS_EIIC. 1 hit.
PF02302. PTS_IIB. 1 hit.
[Graphical view]
SUPFAMSSF55804. PTrfase/Anion_transptr. 1 hit.
TIGRFAMsTIGR00829. FRU. 1 hit.
TIGR00848. FruA. 1 hit.
TIGR01427. PTS_IIC_fructo. 1 hit.
PROSITEPS51094. PTS_EIIA_TYPE_2. 1 hit.
PS00372. PTS_EIIA_TYPE_2_HIS. 1 hit.
PS51099. PTS_EIIB_TYPE_2. 1 hit.
PS51104. PTS_EIIC_TYPE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTF3A_BACSU
AccessionPrimary (citable) accession number: P71012
Secondary accession number(s): Q7BVR6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: June 1, 1998
Last modified: January 25, 2012
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents