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P75039 (PTF3A_MYCPN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:MPN_078
ORF Names:MP077
OrganismMycoplasma pneumoniae (strain ATCC 29342 / M129) [Reference proteome] [HAMAP]
Taxonomic identifier272634 [NCBI]
Taxonomic lineageBacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma ›

Protein attributes

Sequence length694 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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 694694PTS system fructose-specific EIIABC component
PRO_0000186511

Regions

Transmembrane318 – 33821Helical; Potential
Transmembrane364 – 38421Helical; Potential
Transmembrane390 – 41021Helical; Potential
Transmembrane422 – 44221Helical; Potential
Transmembrane461 – 48121Helical; Potential
Transmembrane502 – 52221Helical; Potential
Transmembrane542 – 56221Helical; Potential
Transmembrane576 – 59621Helical; Potential
Transmembrane602 – 62221Helical; Potential
Transmembrane655 – 67521Helical; Potential
Domain4 – 149146PTS EIIA type-2
Domain179 – 27597PTS EIIB type-2
Domain310 – 687378PTS EIIC type-2

Sites

Active site681Tele-phosphohistidine intermediate; for EIIA activity By similarity
Active site1851Phosphocysteine intermediate; for EIIB activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P75039 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 919E12BFBCC5FF6A

FASTA69475,164
        10         20         30         40         50         60 
MFKPLLSAEL FFNWTAKDFK DKTSFLKQAC RVLQDKNCIK EEQIALTALK EREAQITTGI 

        70         80         90        100        110        120 
MSKLALPHMQ SATVLKPFVA VFKVNNVDWQ SLDNQPVKLI FLIGVPKDQG NLHLEFISQF 

       130        140        150        160        170        180 
SKLMLQDEFA NKVPNIRSFN GLINLIDSFQ QTAVASQPVV NEAAAQTEEP KDTNTQYDFV 

       190        200        210        220        230        240 
AVTACPTGIA HTFMAKEALE KFARDHNLKV KVETQGTDGI QNQLTESDLN NTKGIILACD 

       250        260        270        280        290        300 
RLIDLTRFYG HANVVEVSTT KAIKTPQTVY DQVVKKEGKL LGNKSSDSAS QTELKETTEQ 

       310        320        330        340        350        360 
LSFKDFHKRI YRAILSGVSY MLPFVVFGGI LIAIAFLIDI NNAGNAGKQF GSKDPIANWF 

       370        380        390        400        410        420 
KTLGGLSFGL IVPILSAYIA FALVGRQGLL PGFIVGLISA GKFLLNIDIV TGKIDWATES 

       430        440        450        460        470        480 
KVSSGFFGAI FGGLLAAVLI IVQQRYIYRK LPQALQGIKN ILFIPLLGTL VTAALFWVIN 

       490        500        510        520        530        540 
IPLIYLNYGL SKFLQIMDKP YLAPLLGLVI GLMMCFDLGG PVNKAAYVFG VVSLESQNSG 

       550        560        570        580        590        600 
TVAMASAILS GMVPPLGIAI AATIRKQCFD KEELPAAYAC YVMGLSFISE GAIPFVAKRP 

       610        620        630        640        650        660 
KIMLAANLIG GAVCGVLTGA FALTIRAPHG GVFVFALLKT NLEGIAGNTL QIGAGVGLAL 

       670        680        690 
LALIVSSFIS AGIIIGHNLL VVRKKTKQLV NTNA

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References

[1]"Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae."
Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.
Nucleic Acids Res. 24:4420-4449(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29342 / M129.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U00089 Genomic DNA. Translation: AAB95725.1.
PIRS73403.
RefSeqNP_109766.1. NC_000912.1.

3D structure databases

ProteinModelPortalP75039.
ModBaseSearch...

Protein-protein interaction databases

STRING272634.MPN078.

Proteomic databases

PaxDbP75039.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB95725; AAB95725; MPN_078.
GeneID877051.
KEGGmpn:MPN078.
PATRIC20021437. VBIMycPne110_0079.

Phylogenomic databases

eggNOGCOG1445.
KOK02768.
K02769.
K02770.
OMAMMSIDMG.
ProtClustDBCLSK542128.

Enzyme and pathway databases

BioCycMPNE272634:GJ6Z-81-MONOMER.

Family and domain databases

Gene3D3.40.930.10. 1 hit.
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]
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.
PS51099. PTS_EIIB_TYPE_2. 1 hit.
PS51104. PTS_EIIC_TYPE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTF3A_MYCPN
AccessionPrimary (citable) accession number: P75039
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Mycoplasma pneumoniae

Mycoplasma pneumoniae (strain M129): 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