⊟Summary[edit | edit source]
- organism: Streptococcus pneumoniae SPN994038
- locus tag: SPN994038_RS05485 [old locus tag: SPN994038_10220 ]
- pan locus tag?: PNEUPAN002277000
- symbol: eno
- pan gene symbol?: eno
- synonym:
- product: phosphopyruvate hydratase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SPN994038_RS05485 [old locus tag: SPN994038_10220 ]
- symbol: eno
- product: phosphopyruvate hydratase
- replicon: chromosome
- strand: +
- coordinates: 1032703..1034007
- length: 1305
- essential: unknown other strains
⊟Accession numbers[edit | edit source]
- Location: NC_021026 (1032703..1034007) NCBI
- BioCyc:
- MicrobesOnline:
- PneumoBrowse for strain D39V: SPV_1012 PneumoBrowse
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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1261ATGTCAATTATTACTGATGTTTACGCTCGCGAAGTCCTAGACTCACGCGGTAACCCAACA
CTTGAAGTAGAAGTTTACACTGAATCAGGTGCTTTCGGACGTGGTATGGTTCCATCAGGA
GCTTCTACTGGTGAACACGAAGCAGTTGAACTTCGCGACGGTGACAAATCTCGTTACGGT
GGTCTTGGTACACAAAAAGCTGTTGACAACGTAAACAACATCATTGCTGAAGCTATCATT
GGCTACGATGTACGTGATCAACAAGCTATTGACCGTGCTATGATCGCACTTGACGGTACT
CCTAACAAAGGTAAATTGGGTGCGAATGCAATCCTCGGTGTGTCTATCGCTGTAGCTCGT
GCTGCTGCTGACTACCTTGAAATCCCACTTTACAGCTACCTTGGTGGATTCAACACTAAA
GTTCTTCCAACTCCAATGATGAACATCATCAACGGTGGTTCTCACTCTGACGCTCCAATC
GCTTTCCAAGAGTTCATGATCTTGCCAGTTGGTGCGCCAACATTTAAAGAAGCCCTTCGT
TACGGTGCTGAAATCTTCCACGCTCTTAAGAAAATCCTTAAATCACGTGGTTTGGAAACT
GCCGTAGGTGACGAAGGTGGATTCGCTCCTCGTTTCGAAGGAACTGAAGATGGTGTTGAA
ACTATCCTTGCTGCGATTGAAGCTGCTGGATATGTACCAGGTAAAGACGTATTTATCGGA
TTTGACTGTGCTTCATCAGAATTCTACGATAAAGAACGTAAAGTTTACGACTACACTAAA
TTTGAAGGTGAAGGTGCTGCTGTTCGTACATCTGCAGAACAAATCGACTACCTTGAAGAA
TTGGTTAACAAATACCCAATCATCACTATTGAAGATGGTATGGATGAAAACGACTGGGAT
GGTTGGAAAGCTCTTACTGAACGTCTTGGTAAGAAAGTACAACTTGTTGGTGACGACTTC
TTCGTAACAAACACTGACTACCTTGCACGTGGTATCCAAGAAGGTGCTGCTAACTCAATC
CTTATCAAAGTTAACCAAATCGGTACTCTTACTGAAACTTTTGAAGCTATCGAAATGGCT
AAAGAAGCTGGTTACACTGCTGTTGTATCACACCGTTCAGGTGAAACTGAAGATTCAACA
ATCGCTGATATCGCAGTTGCAACTAACGCAGGACAAATCAAGACTGGTTCACTTTCACGT
ACAGACCGTATCGCTAAATACAACCAATTGCTTCGTATCGAAGACCAACTTGGTGAAGTA
GCTGAATATCGTGGATTGAAATCATTCTACAACCTTAAAAAATAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SPN994038_RS05485 [old locus tag: SPN994038_10220 ]
- symbol: Eno
- description: phosphopyruvate hydratase
- length: 434
- theoretical pI: 4.42397
- theoretical MW: 47102.6
- GRAVY: -0.213825
⊟Function[edit | edit source]
- reaction: EC 4.2.1.11? ExPASyPhosphopyruvate hydratase 2-phospho-D-glycerate = phosphoenolpyruvate + H2O
- TIGRFAM: Energy metabolism Glycolysis/gluconeogenesis phosphopyruvate hydratase (TIGR01060; EC 4.2.1.11; HMM-score: 689.2)and 4 moreEnergy metabolism Fermentation methylaspartate ammonia-lyase (TIGR01502; EC 4.3.1.2; HMM-score: 24.3)Energy metabolism Amino acids and amines methylaspartate ammonia-lyase (TIGR01502; EC 4.3.1.2; HMM-score: 24.3)muconate and chloromuconate cycloisomerases (TIGR02534; EC 5.5.1.-; HMM-score: 22.2)Biosynthesis of cofactors, prosthetic groups, and carriers Menaquinone and ubiquinone o-succinylbenzoate synthase (TIGR01928; EC 4.2.1.113; HMM-score: 21.6)
- TheSEED: data available for D39, Hungary19A-6, TIGR4
- PFAM: Enolase_TIM (CL0256) Enolase_C; Enolase, C-terminal TIM barrel domain (PF00113; HMM-score: 435.1)and 3 moreEnolase_N (CL0227) Enolase_N; Enolase, N-terminal domain (PF03952; HMM-score: 204.6)Enolase_TIM (CL0256) MAAL_C; Methylaspartate ammonia-lyase C-terminus (PF07476; HMM-score: 32.5)MR_MLE_C; Enolase C-terminal domain-like (PF13378; HMM-score: 30.3)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 10
- Cytoplasmic Membrane Score: 0
- Cellwall Score: 0
- Extracellular Score: 0
- Internal Helices: 0
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.006799
- TAT(Tat/SPI): 0.001562
- LIPO(Sec/SPII): 0.001052
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
- GI:
- RefSeq: WP_000022813 NCBI
- UniProt:
⊟Protein sequence[edit | edit source]
- MSIITDVYAREVLDSRGNPTLEVEVYTESGAFGRGMVPSGASTGEHEAVELRDGDKSRYGGLGTQKAVDNVNNIIAEAIIGYDVRDQQAIDRAMIALDGTPNKGKLGANAILGVSIAVARAAADYLEIPLYSYLGGFNTKVLPTPMMNIINGGSHSDAPIAFQEFMILPVGAPTFKEALRYGAEIFHALKKILKSRGLETAVGDEGGFAPRFEGTEDGVETILAAIEAAGYVPGKDVFIGFDCASSEFYDKERKVYDYTKFEGEGAAVRTSAEQIDYLEELVNKYPIITIEDGMDENDWDGWKALTERLGKKVQLVGDDFFVTNTDYLARGIQEGAANSILIKVNQIGTLTETFEAIEMAKEAGYTAVVSHRSGETEDSTIADIAVATNAGQIKTGSLSRTDRIAKYNQLLRIEDQLGEVAEYRGLKSFYNLKK
⊟Experimental data[edit | edit source]
- protein localization:
- interaction partners:
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- data available for TIGR4
⊟Expression data[edit | edit source]
- PneumoExpress for strain D39V: SPV_1012 PneumoExpress
⊟Biological Material[edit | edit source]
⊟Mutants[edit | edit source]
⊟Expression vector[edit | edit source]
⊟lacZ fusion[edit | edit source]
⊟GFP fusion[edit | edit source]
⊟two-hybrid system[edit | edit source]
⊟FLAG-tag construct[edit | edit source]
⊟Antibody[edit | edit source]
⊟Other Information[edit | edit source]
You are kindly invited to share additional interesting facts.
⊟Literature[edit | edit source]
⊟References[edit | edit source]
⊟Relevant publications[edit | edit source]
S Bergmann, M Rohde, G S Chhatwal, S Hammerschmidt
alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface.
Mol Microbiol: 2001, 40(6);1273-87
[PubMed:11442827] [WorldCat.org] [DOI] (P p)Simone Bergmann, Daniela Wild, Oliver Diekmann, Ronald Frank, Dagmar Bracht, Gursharan S Chhatwal, Sven Hammerschmidt
Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae.
Mol Microbiol: 2003, 49(2);411-23
[PubMed:12828639] [WorldCat.org] [DOI] (P p)Stefanie Ehinger, Wolf-Dieter Schubert, Simone Bergmann, Sven Hammerschmidt, Dirk W Heinz
Plasmin(ogen)-binding alpha-enolase from Streptococcus pneumoniae: crystal structure and evaluation of plasmin(ogen)-binding sites.
J Mol Biol: 2004, 343(4);997-1005
[PubMed:15476816] [WorldCat.org] [DOI] (P p)Simone Bergmann, Manfred Rohde, Klaus T Preissner, Sven Hammerschmidt
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.
Thromb Haemost: 2005, 94(2);304-11
[PubMed:16113819] [WorldCat.org] [DOI] (P p)Jan Kolberg, Audun Aase, Simone Bergmann, Tove K Herstad, Gunnhild Rødal, Ronald Frank, Manfred Rohde, Sven Hammerschmidt
Streptococcus pneumoniae enolase is important for plasminogen binding despite low abundance of enolase protein on the bacterial cell surface.
Microbiology (Reading): 2006, 152(Pt 5);1307-1317
[PubMed:16622048] [WorldCat.org] [DOI] (P p)Yuka Mori, Masaya Yamaguchi, Yutaka Terao, Shigeyuki Hamada, Takashi Ooshima, Shigetada Kawabata
α-Enolase of Streptococcus pneumoniae induces formation of neutrophil extracellular traps.
J Biol Chem: 2012, 287(13);10472-10481
[PubMed:22262863] [WorldCat.org] [DOI] (I p)Vaibhav Agarwal, Sven Hammerschmidt, Sven Malm, Simone Bergmann, Kristian Riesbeck, Anna M Blom
Enolase of Streptococcus pneumoniae binds human complement inhibitor C4b-binding protein and contributes to complement evasion.
J Immunol: 2012, 189(7);3575-84
[PubMed:22925928] [WorldCat.org] [DOI] (I p)Simone Bergmann, Hanne Schoenen, Sven Hammerschmidt
The interaction between bacterial enolase and plasminogen promotes adherence of Streptococcus pneumoniae to epithelial and endothelial cells.
Int J Med Microbiol: 2013, 303(8);452-62
[PubMed:23906818] [WorldCat.org] [DOI] (I p)