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Q5HQ85 (PT1_STAEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:SERP0670
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

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).

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_0000147089

Sites

Active site1911Tele-phosphohistidine intermediate By similarity
Active site5041Proton donor By similarity
Metal binding4331Magnesium By similarity
Metal binding4571Magnesium By similarity
Binding site2981Substrate By similarity
Binding site3341Substrate By similarity
Binding site4331Substrate By similarity
Binding site4541Substrate; via carbonyl oxygen By similarity
Binding site4551Substrate; via amide nitrogen By similarity
Binding site4561Substrate By similarity
Binding site4571Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HQ85 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 51C95D705D8B3474

FASTA57263,362
        10         20         30         40         50         60 
MSKLIKGIAA SDGVAIAKAY LIVEPDLSYD SNEKVTDIES EVEKFNDAIE ASKIELTKIR 

        70         80         90        100        110        120 
NNAEAQLGAD KAAIFDAHLL VLDDPELIQP IQDKIRNDKV NAATGLDEVT TQFISIFESM 

       130        140        150        160        170        180 
DNEYMKERAA DIRDVSKRVL AHILGVDLPN PSLINESAVI VGNDLTPSDT AQLNKEFVQG 

       190        200        210        220        230        240 
FVTNIGGRTS HSAIMSRSLE IAAVVGTKSI TEEVKQGDMI IVDGMSGDVI IDPTEDELIA 

       250        260        270        280        290        300 
YQNKRERFFE DKKELQKLRD ADTVTVDGVH AELAANIGTP DDLSGVIDNG AQGIGLYRTE 

       310        320        330        340        350        360 
FLYMGRDQMP TEEEQFEAYK KVLETMDGKR VVVRTLDIGG DKELPYLDLP KEMNPFLGYR 

       370        380        390        400        410        420 
AIRLCLAQPE IFRPQLRALL RASVYGKLNI MFPMVATIKE FRDAKSMLLE EKENLLREGY 

       430        440        450        460        470        480 
EVSDDIELGI MVEIPATAAL ADVFAKEVDF FSIGTNDLIQ YTLAADRMSE RVSYLYQPYN 

       490        500        510        520        530        540 
PSILRLVKQV IEASHKEGKW TGMCGEMAGD QTAVPLLLGL GLDEFSMSAT SILKARRQIN 

       550        560        570 
GLSKNEMAEL ANRAVECSTQ EEVVDLVNQL AK

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000029 Genomic DNA. Translation: AAW54027.1.
RefSeqYP_188255.1. NC_002976.3.

3D structure databases

ProteinModelPortalQ5HQ85.
SMRQ5HQ85. Positions 5-572.
ModBaseSearch...

Protein-protein interaction databases

STRING176279.SERP0670.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW54027; AAW54027; SERP0670.
GeneID3241135.
KEGGser:SERP0670.
PATRIC19612211. VBIStaEpi130894_0649.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1080.
HOGENOMHOG000278513.
KOK08483.
OMAQVFEAHL.
ProtClustDBCLSK885128.

Enzyme and pathway databases

BioCycSEPI176279:GJJB-695-MONOMER.

Family and domain databases

Gene3D1.10.274.10. 1 hit.
3.20.20.60. 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_enz_I.
IPR008731. PTS_PEP_utilis_N.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]
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]
PIRSFPIRSF000732. PTS_enzyme_I. 1 hit.
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_STAEQ
AccessionPrimary (citable) accession number: Q5HQ85
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 15, 2005
Last modified: May 1, 2013
This is version 59 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

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