Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9Z9E3 (PT1_CHLPN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
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:CPn_0038, CP_0737, CpB0042
OrganismChlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP]
Taxonomic identifier83558 [NCBI]
Taxonomic lineageBacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia

Protein attributes

Sequence length571 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.

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_0000147065

Sites

Active site2031Tele-phosphohistidine intermediate By similarity
Active site5001Proton donor By similarity
Metal binding4291Magnesium By similarity
Metal binding4531Magnesium By similarity
Binding site3061Substrate By similarity
Binding site3421Substrate By similarity
Binding site4291Substrate By similarity
Binding site4501Substrate; via carbonyl oxygen By similarity
Binding site4511Substrate; via amide nitrogen By similarity
Binding site4521Substrate By similarity
Binding site4531Substrate; via amide nitrogen By similarity

Natural variations

Natural variant191V → I in strain: CWL029 and TW-183.

Experimental info

Sequence conflict71I → T in AAD18191. Ref.1
Sequence conflict4131Q → R in AAD18191. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Z9E3 [UniParc].

Last modified June 1, 2001. Version 2.
Checksum: E217C64AD57A4CB3

FASTA57163,479
        10         20         30         40         50         60 
MDTQSSIGNE EWRIAGTSVV SGMALGKVFF LGTSPLHVRE LTLPQEEVEH EIHRYYKALN 

        70         80         90        100        110        120 
RSKSDIVALE QEVTGQQGLQ EVSSILQAHL EIMKDPLLTE EVVNTIRKDR KNAEYVFSSV 

       130        140        150        160        170        180 
MGKIEESLTA VRGMPSVVDR VQDIHDISNR VIGHLCCQHK SSLGESDQNL IIFSEELTPS 

       190        200        210        220        230        240 
EVASANSAYI RGFVSLVGAA TSHTAIVSRA KSIPYLANIS EELWNIAKRY NGKLVLIDGY 

       250        260        270        280        290        300 
RGELIFNPKP ATLQSCYKKE LSVVAHTSQR LVRKSLHPIV SSHAGSDKDV EDLLENFPQT 

       310        320        330        340        350        360 
SIGLFRSEFL AVILGRLPTL REQVDLYEKL ARFPGDSPSV LRLFDFGEDK PCPGIKNKKE 

       370        380        390        400        410        420 
RSIRWLLDYS VILEDQLQAI AKASLQGSIK VLIPGVSDVS EIIEVKKKWE TIQTRFPKGH 

       430        440        450        460        470        480 
KVSWGTMIEF PSAVWMIEEI LPECDFLSIG TNDLVQYTLG ISRESALPKH LNVTLPPAVI 

       490        500        510        520        530        540 
RMIHHVLQAA KQNQVPVSIC GEAAGQLSLT PLFIGLGVQE LSVAMPVINR LRNHIALLEL 

       550        560        570 
NSCLEITEAL LQAKTCSEVE ELLNRNNKIT S

« Hide

References

[1]"Comparative genomes of Chlamydia pneumoniae and C. trachomatis."
Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S.
Nat. Genet. 21:385-389(1999) [PubMed: 10192388] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CWL029.
[2]"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39."
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. expand/collapse author list , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.
Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AR39.
[3]"Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
Nucleic Acids Res. 28:2311-2314(2000) [PubMed: 10871362] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J138.
[4]"The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW-183.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE001363 Genomic DNA. Translation: AAD18191.1.
AE002161 Genomic DNA. Translation: AAF38542.1.
BA000008 Genomic DNA. Translation: BAA98250.1.
AE009440 Genomic DNA. Translation: AAP97975.1.
PIRA72127.
E81544.
H86495.
RefSeqNP_224246.1. NC_000922.1.
NP_300099.1. NC_002491.1.
NP_445279.1. NC_002179.2.
NP_876318.1. NC_005043.1.

3D structure databases

ProteinModelPortalQ9Z9E3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1466725.
895213.
918830.
963169.
GenomeReviewsGene locus CPn_0038 in contig AE001363_GR.
Gene locus CP_0737 in contig AE002161_GR.
Gene locus CpB0042 in contig AE009440_GR.
Gene locus ptsI in contig BA000008_GR.
KEGGcpa:CP0737.
cpn:CPn0038.
cpt:CpB0042.
TIGRCP_0737.

Phylogenomic databases

HOGENOMHBG414040.
ProtClustDBCLSK871320.

Enzyme and pathway databases

BioCycCPNE115711:CP_0737-MONOMER.
CPNE115713:CPN0038-MONOMER.
CPNE138677:CPJ0038-MONOMER.
CPNE182082:CPB0042-MONOMER.

Family and domain databases

InterProIPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR006318. PEP_util_enz.
IPR008731. PTS_PEP_utilis_N.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]
Gene3DG3DSA:3.50.30.10. PEP_mobile. 1 hit.
G3DSA:1.10.274.10. PTS_PEP_utilis_N. 1 hit.
G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
KOK08483.
PANTHERPTHR22931:SF10. PTHR22931:SF10. 1 hit.
PfamPF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]
PRINTSPR01736. PHPHTRNFRASE.
SUPFAMSSF47831. PEP-utilisers_N. 1 hit.
SSF52009. PEP_mobile. 1 hit.
SSF51621. Pyrv/PenolPyrv_Kinase_cat. 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_CHLPN
AccessionPrimary (citable) accession number: Q9Z9E3
Secondary accession number(s): Q9JRU4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: January 25, 2012
This is version 87 of the entry and version 2 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

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