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Reviewed, UniProtKB/Swiss-Prot O84340 (PT1_CHLTR)

Last modified November 3, 2009. Version 59. 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:
    Phosphoenolpyruvate-protein phosphotransferase
    EC=2.7.3.9
Alternative name(s):
    Phosphotransferase system, enzyme I
Gene names
Name: ptsI
Ordered Locus Names: CT_336
OrganismChlamydia trachomatis [Complete proteome] [HAMAP]
Taxonomic identifier813 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia

Protein attributes

Sequence length571 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Subcellular location

Cytoplasm By similarity.

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 – 571571Phosphoenolpyruvate-protein phosphotransferase
PRO_0000147066

Sites

Active site2071Tele-phosphohistidine intermediate By similarity
Active site5061Proton donor By similarity
Metal binding4351Magnesium By similarity
Metal binding4591Magnesium By similarity
Binding site3121Substrate By similarity
Binding site3481Substrate By similarity
Binding site4351Substrate By similarity
Binding site4561Substrate; via carbonyl oxygen By similarity
Binding site4571Substrate; via amide nitrogen By similarity
Binding site4581Substrate By similarity
Binding site4591Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
O84340-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 73EBFEEE7C457067

FASTA57163,787
        10         20         30         40         50         60 
MSVTGQDNKE LQQEFVIVGE PIVPGIGLGK ALLLGKSSLR IRELTLPQEE VEHEISRYYK 

        70         80         90        100        110        120 
ALKRSRSDLA ALEKEAKGKQ GYQEIASILQ AHLEIIKDPL LTEEVVKTIR KDRKNAEFVF 

       130        140        150        160        170        180 
SSVMGEIEKS LCAVQKTTAT RVDRVQDIHD ISNRVIGHLC CQHKSSLGEF DQNLIVFSEE 

       190        200        210        220        230        240 
LTPSEAANAN PEYIRGFVSL EGAKTSHTAI VSLAKNIPYV ANFTTELWDT IKEFSGTLVL 

       250        260        270        280        290        300 
INGDKGEITF NPQLSTIQTY YRKQASVSVT VPVQVQTGKN LPLISLSAQI VSTEELPMIE 

       310        320        330        340        350        360 
RESPGTSVGL FRSEFMAFSL GRLPCVEEQA DQYAQLVQFQ CSDIHVLRLF DFGEDKECPC 

       370        380        390        400        410        420 
ISSSHRSVRW LLEQEKVLKE QLQAIAIVSR IGRLKVLIPG VIDASEIALV KRLFQEEIRL 

       430        440        450        460        470        480 
LKGISENILW GSMIEIPSAV WMIEEILQES SFVALGTNDL AQYTLGTSRE RSLLGERSRV 

       490        500        510        520        530        540 
PHPSVIRMIH HVVEQAKQKN VPVSVCGEMA GDPALLPMFL GLGVKELSAV IPAINSLKMR 

       550        560        570 
LLDLNSRECS RLTKQLLRAK TYEEVHQLLY V 

« Hide

References

[1]"Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis."
Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.
Science 282:754-759(1998) [PubMed: 9784136] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D/UW-3/Cx.

Cross-references

Sequence databases

AE001273 Genomic DNA. Translation: AAC67931.1.
PIRC71528.
RefSeqNP_219843.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID884783.
GenomeReviewsGene locus CT_336 in contig AE001273_GR.
KEGGctr:CT336.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO84340.
OMAIFRASHY.

Enzyme and pathway databases

BioCycCTRA315277:CT336-MON.
BRENDA2.7.3.9. 108.

Family and domain databases

InterProIPR008279. PEP_mobile.
IPR018274. PEP_mobile_CS.
IPR006318. PEP_P_trans.
IPR000121. PEP_utilizers.
IPR008731. PTS_PEP_utilis_N.
IPR015813. Pyrv/PenolPyrv_Kinase_cat.
[Graphical view]
Gene3DG3DSA:3.50.30.10. PEP_mobile. 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.
[Graphical view]
PRINTSPR01736. PHPHTRNFRASE.
ProDomPD000940. PEP_utilizers. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01417. PTS_I_fam. 1 hit.
PROSITEPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePT1_CHLTR
AccessionPrimary (citable) accession number: O84340
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: November 1, 1998
Last modified: November 3, 2009
This is version 59 of the entry and version 1 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