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P75168 (PT1_MYCPN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. 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

Names and origin

Protein namesRecommended name:
Phosphoenolpyruvate-protein phosphotransferase

EC=2.7.3.9
Alternative name(s):
Phosphotransferase system, enzyme I
Gene names
Name:ptsI
Ordered Locus Names:MPN_627
ORF Names:MP215
OrganismMycoplasma pneumoniae (strain ATCC 29342 / M129) [Reference proteome] [HAMAP]
Taxonomic identifier272634 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length572 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr) By similarity.

Catalytic activity

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

Cofactor

Magnesium By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Domain

The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site By similarity.

Miscellaneous

The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain By similarity.

Sequence similarities

Belongs to the PEP-utilizing enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 572572Phosphoenolpyruvate-protein phosphotransferase
PRO_0000147077

Sites

Active site1901Tele-phosphohistidine intermediate By similarity
Active site4981Proton donor By similarity
Metal binding4271Magnesium By similarity
Metal binding4511Magnesium By similarity
Binding site2971Substrate By similarity
Binding site3331Substrate By similarity
Binding site4271Substrate By similarity
Binding site4481Substrate; via carbonyl oxygen By similarity
Binding site4491Substrate; via amide nitrogen By similarity
Binding site4501Substrate By similarity
Binding site4511Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P75168 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 5B12EF54B0CB80CB

FASTA57263,950
        10         20         30         40         50         60 
MKKLSGIGVS DGMALAKAFL VKTPEFAVNK YLKHQLTKAQ AKRLLDSAFK KAVKDLEEIK 

        70         80         90        100        110        120 
EITVNNINTE AGMIFDAHIQ MLNDPTITEQ LEQQLAQNVH PVIAVDTVFS QTATMFSQMQ 

       130        140        150        160        170        180 
DKYFQERAAD ILDLRQRLLA YLTGQKPHDL VKIKSDVIIV AHDLTPSQTA TLNKKYVKGF 

       190        200        210        220        230        240 
LTEIGGRTSH AAIMARSLEI PAVVGIKGIT TKVKDGQIVG VDGRKGIAGL DLNSKDTTEW 

       250        260        270        280        290        300 
KKQKALEEKY QQELKQYTNK ETVTLDGHAV VVAANIGNVK DMELACQYNT NGVGLFRTEF 

       310        320        330        340        350        360 
LYMNSQEWPD EETQYQAYKA VLEQAHGDLV IIRTLDIGGD KKLNYYEFPH EDNPFLGYRA 

       370        380        390        400        410        420 
LRLTLDKQDI FKTQLRALLR AADHGQLGIM FPMVATLDEL LQAKQLLNQV HQELGGNKQF 

       430        440        450        460        470        480 
KLGIMIEIPA AVLAANTLSH HVDFFSIGTN DLIQYSFAAD RMNKNVSYLY QPLNPALLKL 

       490        500        510        520        530        540 
IYLTIEGGKV NDIWTGMCGE MAGEPLAIPL LLGLGLKEFS MSASSMFKAR MIIAKLNYTE 

       550        560        570 
CQTLAQKALT LANAKEVEKL VEKFFKKKDI FI 

« Hide

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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00089 Genomic DNA. Translation: AAB95863.1.
PIRS73541.
RefSeqNP_110316.1. NC_000912.1.

3D structure databases

ProteinModelPortalP75168.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP75168. 1 interaction.
STRING272634.MPN627.

Proteomic databases

PaxDbP75168.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB95863; AAB95863; MPN_627.
GeneID876731.
KEGGmpn:MPN627.
PATRIC20022737. VBIMycPne110_0691.

Phylogenomic databases

eggNOGCOG1080.
KOK08483.
OMAWQISSIV.
OrthoDBEOG657JBQ.

Enzyme and pathway databases

BioCycMPNE272634:GJ6Z-673-MONOMER.

Family and domain databases

Gene3D1.10.274.10. 1 hit.
3.20.20.60. 1 hit.
3.50.30.10. 1 hit.
InterProIPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR006318. PEP_util_enz.
IPR024692. PTS_EI.
IPR008731. PTS_EIN.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamPF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]
PIRSFPIRSF000732. PTS_enzyme_I. 1 hit.
PRINTSPR01736. PHPHTRNFRASE.
SUPFAMSSF47831. SSF47831. 1 hit.
SSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
TIGRFAMsTIGR01417. PTS_I_fam. 1 hit.
PROSITEPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePT1_MYCPN
AccessionPrimary (citable) accession number: P75168
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: July 9, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Mycoplasma pneumoniae

Mycoplasma pneumoniae (strain M129): entries and gene names