ENO_STRPN
ID ENO_STRPN Reviewed; 434 AA.
AC Q97QS2;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Enolase {ECO:0000255|HAMAP-Rule:MF_00318};
DE EC=4.2.1.11 {ECO:0000255|HAMAP-Rule:MF_00318};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00318};
DE AltName: Full=2-phosphoglycerate dehydratase {ECO:0000255|HAMAP-Rule:MF_00318};
GN Name=eno {ECO:0000255|HAMAP-Rule:MF_00318}; OrderedLocusNames=SP_1128;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP PROTEIN SEQUENCE OF 1-20, SUBCELLULAR LOCATION, FUNCTION IN VIRULENCE,
RP BINDING TO PLASMINOGEN, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP LYS-433 AND LYS-434.
RC STRAIN=ATCC 11733 / Seroytpe 2;
RX PubMed=11442827; DOI=10.1046/j.1365-2958.2001.02448.x;
RA Bergmann S., Rohde M., Chhatwal G.S., Hammerschmidt S.;
RT "Alpha-enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding
RT protein displayed on the bacterial cell surface.";
RL Mol. Microbiol. 40:1273-1287(2001).
RN [3]
RP PROTEIN SEQUENCE OF 2-31, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, BINDING TO PLASMINOGEN, AND IMMUNOGENICITY.
RX PubMed=12435062; DOI=10.1099/0022-1317-51-10-837;
RA Whiting G.C., Evans J.T., Patel S., Gillespie S.H.;
RT "Purification of native alpha-enolase from Streptococcus pneumoniae that
RT binds plasminogen and is immunogenic.";
RL J. Med. Microbiol. 51:837-843(2002).
RN [4]
RP PLASMINOGEN-BINDING MOTIF, AND MUTAGENESIS OF LYS-251; GLU-252; LYS-254;
RP LYS-433 AND LYS-434.
RC STRAIN=ATCC 11733 / Seroytpe 2, and D39 / Serotype 2;
RX PubMed=12828639; DOI=10.1046/j.1365-2958.2003.03557.x;
RA Bergmann S., Wild D., Diekmann O., Frank R., Bracht D., Chhatwal G.S.,
RA Hammerschmidt S.;
RT "Identification of a novel plasmin(ogen)-binding motif in surface displayed
RT alpha-enolase of Streptococcus pneumoniae.";
RL Mol. Microbiol. 49:411-423(2003).
RN [5]
RP FUNCTION OF PLASMINOGEN-BINDING MOTIF ON DEGRADATION OF EXTRACELLULAR
RP MATRIX.
RC STRAIN=D39 / Serotype 2;
RX PubMed=16113819; DOI=10.1160/th05-05-0369;
RA Bergmann S., Rohde M., Preissner K.T., Hammerschmidt S.;
RT "The nine residue plasminogen-binding motif of the pneumococcal enolase is
RT the major cofactor of plasmin-mediated degradation of extracellular matrix,
RT dissolution of fibrin and transmigration.";
RL Thromb. Haemost. 94:304-311(2005).
RN [6]
RP EPITOPE MAPPING, AND ANTIGENICITY.
RC STRAIN=ATCC 11733 / Seroytpe 2;
RX PubMed=16622048; DOI=10.1099/mic.0.28747-0;
RA Kolberg J., Aase A., Bergmann S., Herstad T.K., Roedal G., Frank R.,
RA Rohde M., Hammerschmidt S.;
RT "Streptococcus pneumoniae enolase is important for plasminogen binding
RT despite low abundance of enolase protein on the bacterial cell surface.";
RL Microbiology 152:1307-1317(2006).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RC STRAIN=ATCC 11733 / Seroytpe 2;
RX PubMed=15476816; DOI=10.1016/j.jmb.2004.08.088;
RA Ehinger S., Schubert W.-D., Bergmann S., Hammerschmidt S., Heinz D.W.;
RT "Plasmin(ogen)-binding alpha-enolase from Streptococcus pneumoniae: crystal
RT structure and evaluation of plasmin(ogen)-binding sites.";
RL J. Mol. Biol. 343:997-1005(2004).
CC -!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate
CC into phosphoenolpyruvate. It is essential for the degradation of
CC carbohydrates via glycolysis. Binds plasminogen when expressed at the
CC bacterial cell surface, potentially allowing the bacterium to acquire
CC surface-associated proteolytic activity, which in turn contributes to
CC the degradation of the extracellular matrix and transmigration of the
CC bacteria. {ECO:0000255|HAMAP-Rule:MF_00318,
CC ECO:0000269|PubMed:11442827, ECO:0000269|PubMed:12435062,
CC ECO:0000269|PubMed:16113819}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00318, ECO:0000269|PubMed:12435062};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00318};
CC -!- ACTIVITY REGULATION: The covalent binding to the substrate causes
CC inactivation of the enzyme, and possibly serves as a signal for the
CC export of the protein. {ECO:0000255|HAMAP-Rule:MF_00318}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.5 mM for 2-phospho-D-glycerate {ECO:0000269|PubMed:11442827};
CC Vmax=2.792 umol/min/mg enzyme {ECO:0000269|PubMed:11442827};
CC Note=Catalytically active also when expressed on the bacterial cell
CC surface.;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
CC -!- SUBUNIT: Homooctamer. Forms a ring-shaped structure.
CC -!- INTERACTION:
CC Q97QS2; Q9S400: aroA; NbExp=2; IntAct=EBI-2207206, EBI-2207276;
CC Q97QS2; Q97PR0: asnS; NbExp=2; IntAct=EBI-2207206, EBI-2207302;
CC Q97QS2; P95830: dnaJ; NbExp=2; IntAct=EBI-2207206, EBI-2207079;
CC Q97QS2; Q97SE6: gatA; NbExp=2; IntAct=EBI-2207206, EBI-2207039;
CC Q97QS2; Q97SE7: gatB; NbExp=2; IntAct=EBI-2207206, EBI-2207023;
CC Q97QS2; Q97SE5: gatC; NbExp=2; IntAct=EBI-2207206, EBI-2207053;
CC Q97QS2; Q97NG1: gltX; NbExp=2; IntAct=EBI-2207206, EBI-2207733;
CC Q97QS2; Q97NV3: groES; NbExp=2; IntAct=EBI-2207206, EBI-2206949;
CC Q97QS2; Q97S73: grpE; NbExp=2; IntAct=EBI-2207206, EBI-2207065;
CC Q97QS2; Q97RS9: lysS; NbExp=3; IntAct=EBI-2207206, EBI-2207121;
CC Q97QS2; P65887: purA; NbExp=2; IntAct=EBI-2207206, EBI-2206955;
CC Q97QS2; P65946: pyrR; NbExp=2; IntAct=EBI-2207206, EBI-2207248;
CC Q97QS2; Q97SR4: uppS; NbExp=2; IntAct=EBI-2207206, EBI-2206983;
CC Q97QS2; Q97QP2: xerS; NbExp=2; IntAct=EBI-2207206, EBI-2207218;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted. Cell surface. Note=Fractions
CC of enolase are present in both the cytoplasm and on the cell surface.
CC The export of enolase possibly depends on the covalent binding to the
CC substrate; once secreted, it remains attached to the cell surface,
CC probably in complex with plasminogen.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
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DR EMBL; AE005672; AAK75238.1; -; Genomic_DNA.
DR PIR; E95130; E95130.
DR RefSeq; WP_000022813.1; NZ_AKVY01000001.1.
DR PDB; 1W6T; X-ray; 2.10 A; A/B=1-434.
DR PDBsum; 1W6T; -.
DR AlphaFoldDB; Q97QS2; -.
DR SMR; Q97QS2; -.
DR IntAct; Q97QS2; 14.
DR STRING; 170187.SP_1128; -.
DR MoonProt; Q97QS2; -.
DR EnsemblBacteria; AAK75238; AAK75238; SP_1128.
DR GeneID; 31536454; -.
DR GeneID; 66806230; -.
DR KEGG; spn:SP_1128; -.
DR eggNOG; COG0148; Bacteria.
DR OMA; EFMIIPV; -.
DR PhylomeDB; Q97QS2; -.
DR BioCyc; SPNE170187:G1FZB-1152-MON; -.
DR SABIO-RK; Q97QS2; -.
DR UniPathway; UPA00109; UER00187.
DR EvolutionaryTrace; Q97QS2; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:UniProt.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd03313; enolase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR HAMAP; MF_00318; Enolase; 1.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR020809; Enolase_CS.
DR InterPro; IPR020811; Enolase_N.
DR PANTHER; PTHR11902; PTHR11902; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PIRSF; PIRSF001400; Enolase; 1.
DR PRINTS; PR00148; ENOLASE.
DR SFLD; SFLDF00002; enolase; 1.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01060; eno; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase;
KW Magnesium; Metal-binding; Secreted; Virulence.
FT CHAIN 1..434
FT /note="Enolase"
FT /id="PRO_0000133980"
FT REGION 55..63
FT /note="Antigenic epitope"
FT MOTIF 248..256
FT /note="Plasminogen-binding"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 291
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 343
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 370..373
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT MUTAGEN 251
FT /note="K->L: Great decrease in ability to bind plasminogen.
FT Decrease in virulence; when associated with G-252 and L-
FT 254."
FT /evidence="ECO:0000269|PubMed:12828639"
FT MUTAGEN 252
FT /note="E->G: Great decrease in ability to bind plasminogen.
FT Decrease in virulence; when associated with L-251 and L-
FT 254."
FT /evidence="ECO:0000269|PubMed:12828639"
FT MUTAGEN 254
FT /note="K->L: Great decrease in ability to bind plasminogen.
FT Decrease in virulence; when associated with L-251 and G-
FT 252."
FT /evidence="ECO:0000269|PubMed:12828639"
FT MUTAGEN 433
FT /note="K->L: Decrease in ability to bind plasminogen under
FT denaturing conditions. No effect on ability to bind
FT plasminogen under non-denaturing conditions. Loss of
FT ability to form homooctamers. Decrease in virulence; when
FT associated with L-434."
FT /evidence="ECO:0000269|PubMed:11442827,
FT ECO:0000269|PubMed:12828639"
FT MUTAGEN 434
FT /note="K->L: Decrease in ability to bind plasminogen under
FT denaturing conditions. No effect on ability to bind
FT plasminogen under non-denaturing conditions."
FT /evidence="ECO:0000269|PubMed:11442827,
FT ECO:0000269|PubMed:12828639"
FT MUTAGEN 434
FT /note="K->L: Decrease in ability to bind plasminogen under
FT denaturing conditions. No effect on ability to bind
FT plasminogen under non-denaturing conditions. Loss of
FT ability to form homooctamers. Decrease in virulence; when
FT associated with L-433."
FT /evidence="ECO:0000269|PubMed:11442827,
FT ECO:0000269|PubMed:12828639"
FT CONFLICT 2
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="T -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="E -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:1W6T"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:1W6T"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:1W6T"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 108..126
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:1W6T"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1W6T"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1W6T"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 175..195
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 215..228
FT /evidence="ECO:0007829|PDB:1W6T"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:1W6T"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:1W6T"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 299..309
FT /evidence="ECO:0007829|PDB:1W6T"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:1W6T"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:1W6T"
FT TURN 319..323
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:1W6T"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 350..362
FT /evidence="ECO:0007829|PDB:1W6T"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 380..387
FT /evidence="ECO:0007829|PDB:1W6T"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:1W6T"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 401..417
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:1W6T"
FT HELIX 425..428
FT /evidence="ECO:0007829|PDB:1W6T"
SQ SEQUENCE 434 AA; 47103 MW; 0D64F8F04BBB99C4 CRC64;
MSIITDVYAR EVLDSRGNPT LEVEVYTESG AFGRGMVPSG ASTGEHEAVE LRDGDKSRYG
GLGTQKAVDN VNNIIAEAII GYDVRDQQAI DRAMIALDGT PNKGKLGANA ILGVSIAVAR
AAADYLEIPL YSYLGGFNTK VLPTPMMNII NGGSHSDAPI AFQEFMILPV GAPTFKEALR
YGAEIFHALK KILKSRGLET AVGDEGGFAP RFEGTEDGVE TILAAIEAAG YVPGKDVFIG
FDCASSEFYD KERKVYDYTK FEGEGAAVRT SAEQIDYLEE LVNKYPIITI EDGMDENDWD
GWKALTERLG KKVQLVGDDF FVTNTDYLAR GIQEGAANSI LIKVNQIGTL TETFEAIEMA
KEAGYTAVVS HRSGETEDST IADIAVATNA GQIKTGSLSR TDRIAKYNQL LRIEDQLGEV
AEYRGLKSFY NLKK
