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Q97QS2 (ENO_STRPN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Enolase
EC=4.2.1.11
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
2-phosphoglycerate dehydratase
Gene names
Name:eno
Ordered Locus Names:SP_1128
OrganismStreptococcus pneumoniae [Complete proteome] [HAMAP]
Taxonomic identifier1313 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. Binds plasminogen when expressed at the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity, which in turn contributes to the degradation of the extracellular matrix and transmigration of the bacteria. HAMAP MF_00318

Catalytic activity

2-phospho-D-glycerate = phosphoenolpyruvate + H2O. Ref.3

Cofactor

Magnesium. Required for catalysis and for stabilizing the dimer By similarity.

Enzyme regulation

The covalent binding to the substrate of a small fraction of enolase causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein By similarity. HAMAP MF_00318

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP MF_00318

Subunit structure

Homooctamer. Forms a ring-shaped structure.

Subcellular location

Cytoplasm. Secreted. Cell surface. Note: Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the bacterial cell surface, probably in complex with plasminogen. Ref.2 Ref.3

Sequence similarities

Belongs to the enolase family.

Biophysicochemical properties

Kinetic parameters:

Catalytically active also when expressed on the bacterial cell surface.

KM=4.5 mM for 2-phospho-D-glycerate Ref.2

Vmax=2.792 µmol/min/mg enzyme

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 434434Enolase HAMAP MF_00318
PRO_0000133980

Regions

Region55 – 639Antigenic epitope HAMAP MF_00318
Region370 – 3734Substrate binding By similarity
Motif248 – 2569Plasminogen-binding HAMAP MF_00318

Sites

Active site2051Proton donor By similarity
Active site3431Proton acceptor By similarity
Metal binding2421Magnesium By similarity
Metal binding2911Magnesium By similarity
Metal binding3181Magnesium By similarity
Binding site1551Substrate By similarity
Binding site1641Substrate By similarity
Binding site2911Substrate By similarity
Binding site3181Substrate By similarity
Binding site3431Substrate (covalent); in inhibited form By similarity
Binding site3941Substrate By similarity

Amino acid modifications

Modified residue2851Phosphotyrosine By similarity

Experimental info

Mutagenesis2511K → L: Great decrease in ability to bind plasminogen. Decrease in virulence; when associated with G-252 and L-254. Ref.4
Mutagenesis2521E → G: Great decrease in ability to bind plasminogen. Decrease in virulence; when associated with L-251 and L-254. Ref.4
Mutagenesis2541K → L: Great decrease in ability to bind plasminogen. Decrease in virulence; when associated with L-251 and G-252. Ref.4
Mutagenesis4331K → L: Decrease in ability to bind plasminogen under denaturing conditions. No effect on ability to bind plasminogen under non-denaturing conditions. Loss of ability to form homooctamers. Decrease in virulence; when associated with L-434. Ref.2 Ref.4
Mutagenesis4341K → L: Decrease in ability to bind plasminogen under denaturing conditions. No effect on ability to bind plasminogen under non-denaturing conditions. Ref.2 Ref.4
Mutagenesis4341K → L: Decrease in ability to bind plasminogen under denaturing conditions. No effect on ability to bind plasminogen under non-denaturing conditions. Loss of ability to form homooctamers. Decrease in virulence; when associated with L-433.
Sequence conflict21Missing AA sequence Ref.2
Sequence conflict201T → P AA sequence Ref.2
Sequence conflict241E → G AA sequence Ref.3

Secondary structure

1 ...................................................................... 434
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q97QS2 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 0D64F8F04BBB99C4

FASTA43447,103
        10         20         30         40         50         60 
MSIITDVYAR EVLDSRGNPT LEVEVYTESG AFGRGMVPSG ASTGEHEAVE LRDGDKSRYG 

        70         80         90        100        110        120 
GLGTQKAVDN VNNIIAEAII GYDVRDQQAI DRAMIALDGT PNKGKLGANA ILGVSIAVAR 

       130        140        150        160        170        180 
AAADYLEIPL YSYLGGFNTK VLPTPMMNII NGGSHSDAPI AFQEFMILPV GAPTFKEALR 

       190        200        210        220        230        240 
YGAEIFHALK KILKSRGLET AVGDEGGFAP RFEGTEDGVE TILAAIEAAG YVPGKDVFIG 

       250        260        270        280        290        300 
FDCASSEFYD KERKVYDYTK FEGEGAAVRT SAEQIDYLEE LVNKYPIITI EDGMDENDWD 

       310        320        330        340        350        360 
GWKALTERLG KKVQLVGDDF FVTNTDYLAR GIQEGAANSI LIKVNQIGTL TETFEAIEMA 

       370        380        390        400        410        420 
KEAGYTAVVS HRSGETEDST IADIAVATNA GQIKTGSLSR TDRIAKYNQL LRIEDQLGEV 

       430 
AEYRGLKSFY NLKK

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of a virulent isolate of Streptococcus pneumoniae."
Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L. expand/collapse author list , Lewis M.R., Radune D., Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.
Science 293:498-506(2001) [PubMed: 11463916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-334 / TIGR4.
[2]"Alpha-enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface."
Bergmann S., Rohde M., Chhatwal G.S., Hammerschmidt S.
Mol. Microbiol. 40:1273-1287(2001) [PubMed: 11442827] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-20, SUBCELLULAR LOCATION, BINDING TO PLASMINOGEN, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-433 AND LYS-434.
Strain: ATCC 11733 / Seroytpe 2.
[3]"Purification of native alpha-enolase from Streptococcus pneumoniae that binds plasminogen and is immunogenic."
Whiting G.C., Evans J.T., Patel S., Gillespie S.H.
J. Med. Microbiol. 51:837-843(2002) [PubMed: 12435062] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-31, ENZYMATIC ACTIVITY, SUBCELLULAR LOCATION, BINDING TO PLASMINOGEN, IMMUNOGENICITY.
[4]"Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae."
Bergmann S., Wild D., Diekmann O., Frank R., Bracht D., Chhatwal G.S., Hammerschmidt S.
Mol. Microbiol. 49:411-423(2003) [PubMed: 12828639] [Abstract]
Cited for: PLASMINOGEN-BINDING MOTIF, MUTAGENESIS OF LYS-251; GLU-252; LYS-254; LYS-433 AND LYS-434.
Strain: ATCC 11733 / Seroytpe 2 and D39 / Serotype 2.
[5]"The nine residue plasminogen-binding motif of the pneumococcal enolase is the major cofactor of plasmin-mediated degradation of extracellular matrix, dissolution of fibrin and transmigration."
Bergmann S., Rohde M., Preissner K.T., Hammerschmidt S.
Thromb. Haemost. 94:304-311(2005) [PubMed: 16113819] [Abstract]
Cited for: ROLE OF PLASMINOGEN-BINDING MOTIF ON DEGRADATION OF EXTRACELLULAR MATRIX.
Strain: D39 / Serotype 2.
[6]"Streptococcus pneumoniae enolase is important for plasminogen binding despite low abundance of enolase protein on the bacterial cell surface."
Kolberg J., Aase A., Bergmann S., Herstad T.K., Roedal G., Frank R., Rohde M., Hammerschmidt S.
Microbiology 152:1307-1317(2006) [PubMed: 16622048] [Abstract]
Cited for: EPITOPE MAPPING, ANTIGENICITY.
Strain: ATCC 11733 / Seroytpe 2.
[7]"Plasmin(ogen)-binding alpha-enolase from Streptococcus pneumoniae: crystal structure and evaluation of plasmin(ogen)-binding sites."
Ehinger S., Schubert W.-D., Bergmann S., Hammerschmidt S., Heinz D.W.
J. Mol. Biol. 343:997-1005(2004) [PubMed: 15476816] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Strain: ATCC 11733 / Seroytpe 2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005672 Genomic DNA. Translation: AAK75238.1.
PIRE95130.
RefSeqNP_345598.1. NC_003028.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W6TX-ray2.10A/B1-434[»]
ProteinModelPortalQ97QS2.
SMRQ97QS2. Positions 1-432.
ModBaseSearch...

Protein-protein interaction databases

IntActQ97QS2. 16 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000025245; EBSTRP00000024337; EBSTRG00000025245.
GeneID931642.
GenomeReviewsGene locus SP_1128 in contig AE005672_GR.
KEGGspn:SP_1128.
PATRIC19706667. VBIStrPne105772_1178.
TIGRSP_1128.

Phylogenomic databases

GeneTreeEBGT00050000028180.
HOGENOMHBG726599.
OMAQEYMIMP.
ProtClustDBPRK00077.

Enzyme and pathway databases

BioCycSPNE170187-1:SP_1128-MONOMER.
BRENDA4.2.1.11. 5946.

Family and domain databases

HAMAPMF_00318. Enolase.
[Tree]
InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]
KOK01689.
PANTHERPTHR11902. Enolase. 1 hit.
PfamPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF001400. Enolase. 1 hit.
PRINTSPR00148. ENOLASE.
TIGRFAMsTIGR01060. Eno. 1 hit.
PROSITEPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameENO_STRPN
AccessionPrimary (citable) accession number: Q97QS2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: October 1, 2001
Last modified: January 25, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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