Phosphoenolpyruvate-protein phosphotransferase

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Reviewed, UniProtKB/Swiss-Prot Q9PK57 (PT1_CHLMU)

Last modified February 9, 2010. Version 61. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Phosphoenolpyruvate-protein phosphotransferase
    EC=2.7.3.9
Alternative name(s):
    Phosphotransferase system, enzyme I

Gene names

Name:	ptsI
Ordered Locus Names:	TC_0613

Organism

Chlamydia muridarum [Complete proteome] [HAMAP]

Taxonomic identifier

83560 [NCBI]

Taxonomic lineage

Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia

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Protein attributes

Sequence length	567 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

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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.

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Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	kinase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoenolpyruvate-protein phosphotransferase activity Inferred from electronic annotation. Source: EC sugar:hydrogen symporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 567

567

Phosphoenolpyruvate-protein phosphotransferase

PRO_0000147064

Sites

Active site

205

Tele-phosphohistidine intermediate By similarity

Active site

502

Proton donor By similarity

Metal binding

431

Magnesium By similarity

Metal binding

455

Magnesium By similarity

Binding site

308

Substrate By similarity

Binding site

344

Substrate By similarity

Binding site

431

Substrate By similarity

Binding site

452

Substrate; via carbonyl oxygen By similarity

Binding site

453

Substrate; via amide nitrogen By similarity

Binding site

454

Substrate By similarity

Binding site

455

Substrate; via amide nitrogen By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9PK57-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: EFC064A3404F4BB4
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FASTA

567

63,311

        10         20         30         40         50         60 
MGATSQKELQ QEFVIVGEPV VPGIGLGKSL LLGKSSLRIR ELTLPQEEVE HEINRYYKAL 

        70         80         90        100        110        120 
KESRSDLAAL EKKAKGKQGY QEIASILQAH LEIIKDPLLT EEVVKTIRKD RKNAEFVFSS 

       130        140        150        160        170        180 
VMGEIEKSLC AVQKTTAIAV DRIQDIHDIS NRVIGHLCCQ HKSSLGESDQ NLIVFSEELT 

       190        200        210        220        230        240 
PSEAANANPK YIRGFVSLEG SKTSHTAIVS LAKNIPYVAN FSAESWQRIR EYNGNLVLIN 

       250        260        270        280        290        300 
GEKGEITFNP KLSTIQAYYR KQSAVSMTVP IQIEKTQPLI SLSAQIVGVD ELGSISREFP 

       310        320        330        340        350        360 
GTTIGLFRSE FMAFSLGRLP FVEEQVAEYT KLVQFSCSDI NVLRLFDFGE DKVCPFIASA 

       370        380        390        400        410        420 
HRSVRWLLEQ ETILRGQLQA IAIASRQGKL KVLIPGVLDA SEIILVKQMF QEEVQLQNGI 

       430        440        450        460        470        480 
SENIIWGSMI EIPSAVWMIE EILQESSFIA LGTNDLAQYT LGMSRERSLP GNWKQVPHPS 

       490        500        510        520        530        540 
VIRMIHYVAA RAKQRNIPVS VCGEMAGDHL LLPMFIGFGV RELSVVAPAI HSLKMRLLAL 

       550        560 
NSKECSRLAK QLLRARTYEE VHKLLNM

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References

[1]

"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.

Fraser C.M.
Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MoPn / Nigg.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AE002160 Genomic DNA. Translation: AAF39444.1.
PIR	F81682.
RefSeq	NP_296989.1.
3D structure databases
SMR	Q9PK57. Positions 15-566.
ModBase	Search...
Genome annotation databases
GeneID	1245975.
GenomeReviews	Gene locus TC_0613 in contig AE002160_GR.
KEGG	cmu:TC0613.
TIGR	TC_0613.
Phylogenomic databases
HOGENOM	HBG414040.
OMA	MAERADD.
Enzyme and pathway databases
BioCyc	CMUR243161:TC_0613-MONOMER.
BRENDA	2.7.3.9. 256349.
Family and domain databases
InterPro	IPR008279. PEP-utiliz_enz_mobile_dom. IPR006318. PEP_P_trans. IPR000121. PEP_utilisers. IPR008731. PTS_PEP_utilis_N. IPR015813. Pyrv/PenolPyrv_Kinase_cat. [Graphical view]
Gene3D	G3DSA:3.50.30.10. PEP_mobile. 1 hit. G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
Pfam	PF05524. PEP-utilisers_N. 1 hit. PF00391. PEP-utilizers. 1 hit. PF02896. PEP-utilizers_C. 1 hit. [Graphical view]
PRINTS	PR01736. PHPHTRNFRASE.
TIGRFAMs	TIGR01417. PTS_I_fam. 1 hit.
PROSITE	PS00742. PEP_ENZYMES_2. 1 hit. PS00370. PEP_ENZYMES_PHOS_SITE. False negative. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

PT1_CHLMU

Accession

Primary (citable) accession number: Q9PK57

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents