ENO_STAAU
ID ENO_STAAU Reviewed; 434 AA.
AC O69174;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
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};
DE AltName: Full=Laminin-binding protein;
GN Name=eno {ECO:0000255|HAMAP-Rule:MF_00318};
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ISP3;
RA Choi G.H., Simpson A.J.;
RT "Identification of enolase as a laminin binding protein at the surface of
RT Staphylococcus aureus.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, FUNCTION IN VIRULENCE, AND
RP BINDING TO LAMININ.
RC STRAIN=ATCC 10832 / Wood 46;
RX PubMed=15158195; DOI=10.1016/j.micinf.2004.02.003;
RA Carneiro C.R.W., Postol E., Nomizo R., Reis L.F.L., Brentani R.R.;
RT "Identification of enolase as a laminin-binding protein on the surface of
RT Staphylococcus aureus.";
RL Microbes Infect. 6:604-608(2004).
CC -!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate
CC into phosphoenolpyruvate. It is essential for the degradation of
CC carbohydrates via glycolysis (By similarity). Binds laminin when
CC expressed on the bacterial cell surface; this probably induces
CC destruction of the extracellular matrix, favoring invasion and
CC dissemination. {ECO:0000255|HAMAP-Rule:MF_00318,
CC ECO:0000269|PubMed:15158195}.
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};
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 -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318,
CC ECO:0000269|PubMed:15158195}. Secreted {ECO:0000255|HAMAP-
CC Rule:MF_00318, ECO:0000269|PubMed:15158195}. Cell surface
CC {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15158195}.
CC Note=Fractions of enolase are present in both the cytoplasm and on the
CC cell surface. The export of enolase possibly depends on the covalent
CC binding to the substrate; once secreted, it remains attached to the
CC cell surface.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
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DR EMBL; AF065394; AAC17130.1; -; Genomic_DNA.
DR PIR; T47276; T47276.
DR PDB; 5BOE; X-ray; 1.60 A; A/B=1-434.
DR PDB; 5BOF; X-ray; 2.45 A; A/B=1-434.
DR PDBsum; 5BOE; -.
DR PDBsum; 5BOF; -.
DR AlphaFoldDB; O69174; -.
DR SMR; O69174; -.
DR BRENDA; 4.2.1.11; 3352.
DR UniPathway; UPA00109; UER00187.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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_0000133970"
FT ACT_SITE 207
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 157
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 244
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 STRAND 3..13
FT /evidence="ECO:0007829|PDB:5BOE"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:5BOE"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5BOE"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:5BOE"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 110..128
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:5BOE"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:5BOE"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:5BOE"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 177..197
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 217..230
FT /evidence="ECO:0007829|PDB:5BOE"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:5BOE"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:5BOE"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:5BOE"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 299..309
FT /evidence="ECO:0007829|PDB:5BOE"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:5BOE"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:5BOE"
FT TURN 319..323
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:5BOE"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 350..362
FT /evidence="ECO:0007829|PDB:5BOE"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 380..387
FT /evidence="ECO:0007829|PDB:5BOE"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:5BOE"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 401..417
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:5BOE"
FT HELIX 425..428
FT /evidence="ECO:0007829|PDB:5BOE"
SQ SEQUENCE 434 AA; 47117 MW; C4A19BA3675429B3 CRC64;
MPIITDVYAR EVLDSRGNPT VEVEVLTESG AFGRALVPSG ASTGEHEAVE LRDGDKSRYL
GKGVTKAVEN VNEIIAPEII EGEFSVLDQV SIDKMMIALD GTPNKGKLGA NAILGVSIAV
ARAAADLLGQ PLYKYLGGFN GKQLPVPMMN IVNGGSHSDA PIAFQEFMIL PVGATTFKES
LRWGTEIFHN LKSILSQRGL ETAVGDEGGF APKFEGTEDA VETIIQAIEA AGYKPGEEVF
LGFDCASSEF YENGVYDYSK FEGEHGAKRT AAEQVDYLEQ LVDKYPIITI EDGMDENDWD
GWKQLTERIG DRVQLVGDDL FVTNTEILAK GIENGIGNSI LIKVNQIGTL TETFDAIEMA
QKAGYTAVVS HRSGETEDTT IADIAVATNA GQIKTGSLSR TDRIAKYNQL LRIEDELFET
AKYDGIKSFY NLDK
