Reviewed, UniProtKB/Swiss-Prot Q97QS2 (ENO_STRPN)

Names and origin

Protein names

Recommended name:
    Enolase
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase
    2-phospho-D-glycerate hydro-lyase

Gene names

Name:	eno
Ordered Locus Names:	SP_1128

Organism

Streptococcus pneumoniae [Complete proteome] [HAMAP]

Taxonomic identifier

1313 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP MF_00318
Subunit structure	Homooctamer. Forms a ring-shaped structure. HAMAP MF_00318
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.3 Ref.2
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 HAMAP MF_00318 Vmax=2.792 µmol/min/mg enzyme

Ontologies

Keywords
Biological process	Glycolysis Virulence
Cellular component	Cytoplasm Secreted
Ligand	Magnesium Metal-binding
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: HAMAP pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell surface Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP phosphopyruvate hydratase activity Inferred from electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
lysS	Q97RS9	1	EBI-2207206,EBI-2207121

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 434

434

Enolase HAMAP MF_00318

PRO_0000133980

Regions

Region

55 – 63

9

Antigenic epitope HAMAP MF_00318

Region

370 – 373

4

Substrate binding By similarity

Motif

248 – 256

9

Plasminogen-binding HAMAP MF_00318

Sites

Active site

205

1

Proton donor By similarity

Active site

343

1

Proton acceptor By similarity

Metal binding

242

1

Magnesium By similarity

Metal binding

291

1

Magnesium By similarity

Metal binding

318

1

Magnesium By similarity

Binding site

155

1

Substrate By similarity

Binding site

164

1

Substrate By similarity

Binding site

291

1

Substrate By similarity

Binding site

318

1

Substrate By similarity

Binding site

343

1

Substrate (covalent); in inhibited form By similarity

Binding site

394

1

Substrate By similarity

Amino acid modifications

Modified residue

285

1

Phosphotyrosine By similarity

Experimental info

Mutagenesis

251

1

K → L: Great decrease in ability to bind plasminogen. Decrease in virulence; when associated with G-252 and L-254. Ref.4

Mutagenesis

252

1

E → G: Great decrease in ability to bind plasminogen. Decrease in virulence; when associated with L-251 and L-254. Ref.4

Mutagenesis

254

1

K → L: Great decrease in ability to bind plasminogen. Decrease in virulence; when associated with L-251 and G-252. Ref.4

Mutagenesis

433

1

K → 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

Mutagenesis

434

1

K → 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

Mutagenesis

434

1

K → 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 conflict

2

1

Missing AA sequence Ref.2

Sequence conflict

20

1

T → P AA sequence Ref.2

Sequence conflict

24

1

E → G AA sequence Ref.3

Secondary structure

1

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434

Helix Strand Turn

Details...

Beta strand

3 – 13

11

Beta strand

19 – 27

9

Beta strand

32 – 36

5

Helix

59 – 61

3

Helix

65 – 73

9

Helix

75 – 79

5

Helix

87 – 98

12

Turn

104 – 106

3

Helix

108 – 126

19

Helix

130 – 135

6

Beta strand

147 – 151

5

Helix

153 – 155

3

Beta strand

157 – 159

3

Beta strand

163 – 168

6

Helix

175 – 195

21

Helix

215 – 228

14

Turn

233 – 235

3

Beta strand

238 – 242

5

Helix

245 – 248

4

Helix

259 – 262

4

Helix

271 – 284

14

Beta strand

287 – 292

6

Helix

299 – 309

11

Turn

310 – 312

3

Beta strand

313 – 318

6

Turn

319 – 323

5

Helix

325 – 334

10

Beta strand

338 – 342

5

Helix

344 – 347

4

Helix

350 – 362

13

Beta strand

366 – 370

5

Helix

380 – 387

8

Beta strand

392 – 394

3

Beta strand

398 – 400

3

Helix

401 – 417

17

Helix

418 – 420

3

Helix

425 – 428

4

Sequences

	Sequence		Length	Mass (Da)
	Q97QS2-1 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: 0D64F8F04BBB99C4	FASTA	434	47,103
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE005672 Genomic DNA. Translation: AAK75238.1.

PIR

E95130.

RefSeq

NP_345598.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W6T	X-ray	2.10	A/B	1-434	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q97QS2. 15 interactions.

Genome annotation databases

GeneID

931642.

GenomeReviews

Gene locus SP_1128 in contig AE005672_GR.

KEGG

spn:SP_1128.

TIGR

SP_1128.

Phylogenomic databases

HOGENOM

Q97QS2.

OMA

Q97QS2. DIAVGTN.

Enzyme and pathway databases

BRENDA

4.2.1.11. 600.

Family and domain databases

HAMAP

MF_00318.
[Tree]

InterPro

IPR000941. Enolase.
[Graphical view]

PANTHER

PTHR11902. Enolase. 1 hit.

Pfam

PF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]

PIRSF

PIRSF001400. Enolase. 1 hit.

PRINTS

PR00148. ENOLASE.

ProDom

PD000902. Enolase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01060. eno. 1 hit.

PROSITE

PS00164. ENOLASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ENO_STRPN

Accession

Primary (citable) accession number: Q97QS2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 27, 2002
Last sequence update:	October 1, 2001
Last modified:	June 16, 2009
This is version 63 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)