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PangenomeTIGR4
serotype 4
D39
serotype 2
D39V
serotype 2
Hungary19A-6
serotype 19A
EF3030
serotype 19F
670-6B
serotype 6B
6A-10
serotype 6A
70585
serotype 5
A026
serotype 19F
A66
serotype 3
AP200
serotype 11A
ASP0581
serotype 12F
ATCC 49619
serotype 19F
ATCC 700669
serotype 23F
BVJ1JL
serotype 1
CGSP14
serotype 14
G54
serotype 19F
HU-OH
serotype 3
Hu15
serotype 19A
Hu17
serotype 19A
INV104
serotype 1
INV200
serotype 14
JJA
serotype 14
MDRSPN001
serotype 19F
NCTC7466
serotype 2
NU83127
serotype 4
OXC141
serotype 3
P1031
serotype 1
R6
serotype 2
SP49
serotype 19A
SPN032672
serotype 1
SPN034156
serotype 3
SPN034183
serotype 3
SPN994038
serotype 3
SPN994039
serotype 3
SPNA45
serotype 3
ST556
serotype 19F
TCH8431/19A
serotype 19A
Taiwan19F-14
serotype 19F
Xen35
serotype 4
gamPNI0373
serotype 1

NCBI: 10-MAR-2021

⊟Summary[edit | edit source]

  • organism: Streptococcus pneumoniae Hungary19A-6
  • locus tag: SPH_RS05925 [old locus tag: SPH_1222 ]
  • 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: SPH_RS05925 [old locus tag: SPH_1222 ]
  • symbol: eno
  • product: phosphopyruvate hydratase
  • replicon: chromosome
  • strand: +
  • coordinates: 1121624..1122928
  • length: 1305
  • essential: unknown other strains

⊟Accession numbers[edit | edit source]

  • Location: NC_010380 (1121624..1122928) NCBI
  • BioCyc: SPH_RS05925 BioCyc
  • MicrobesOnline: see SPH_1222
  • PneumoBrowse for strain D39V: SPV_1012 PneumoBrowse

⊟Phenotype[edit | edit source]

Share your knowledge and add information here. [edit]

⊟DNA sequence[edit | edit source]

  • 1
    61
    121
    181
    241
    301
    361
    421
    481
    541
    601
    661
    721
    781
    841
    901
    961
    1021
    1081
    1141
    1201
    1261
    ATGTCAATTATTACTGATGTTTACGCTCGCGAAGTCCTAGACTCACGCGGTAACCCAACA
    CTTGAAGTAGAAGTTTACACTGAATCAGGTGCTTTCGGACGTGGTATGGTTCCATCAGGA
    GCTTCTACTGGTGAACACGAAGCAGTTGAACTTCGCGACGGTGACAAATCTCGTTACGGT
    GGTCTTGGTACACAAAAAGCTGTTGACAACGTAAACAACATCATTGCTGAAGCTATCATT
    GGCTACGATGTACGTGATCAACAAGCTATTGACCGTGCTATGATCGCACTTGACGGTACT
    CCTAACAAAGGTAAATTGGGTGCGAATGCAATCCTCGGTGTGTCTATCGCTGTAGCTCGT
    GCTGCTGCTGACTACCTTGAAATCCCACTTTACAGCTACCTTGGTGGATTCAACACTAAA
    GTTCTTCCAACTCCAATGATGAACATCATCAACGGTGGTTCTCACTCTGACGCTCCAATC
    GCTTTCCAAGAGTTCATGATCTTGCCAGTTGGTGCGCCAACATTTAAAGAAGCCCTTCGT
    TACGGTGCTGAAATCTTCCACGCCCTTAAGAAAATCCTTAAATCACGTGGTTTGGAAACT
    GCCGTAGGTGACGAAGGTGGATTCGCTCCTCGTTTCGAAGGAACTGAAGATGGTGTTGAA
    ACTATCCTTGCTGCGATTGAAGCTGCTGGATATGTACCAGGTAAAGACGTATTTATTGGA
    TTTGACTGTGCTTCATCAGAATTCTACGATAAAGAACGTAAAGTTTACGACTACACTAAA
    TTTGAAGGTGAAGGTGCTGCTGTTCGTACATCTGCAGAACAAATCGACTACCTTGAAGAA
    TTGGTTAACAAATACCCAATCATCACTATTGAAGATGGTATGGATGAAAACGACTGGGAT
    GGTTGGAAAGCTCTTACTGAACGTCTTGGTAAGAAAGTACAACTTGTTGGTGACGACTTC
    TTCGTAACAAACACTGACTACCTTGCACGTGGTATCCAAGAAGGTGCTGCTAACTCAATC
    CTTATCAAAGTTAACCAAATCGGTACTCTTACTGAAACTTTTGAAGCTATCGAAATGGCT
    AAAGAAGCTGGTTACACTGCTGTTGTATCACACCGTTCAGGTGAAACTGAAGATTCAACA
    ATCGCTGATATTGCAGTTGCAACTAACGCAGGACAAATCAAGACTGGTTCACTTTCACGT
    ACAGACCGCATCGCTAAATACAACCAATTGCTTCGTATCGAAGACCAACTTGGTGAAGTA
    GCTGAATATCGTGGATTGAAATCATTCTACAACCTTAAAAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1305

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SPH_RS05925 [old locus tag: SPH_1222 ]
  • 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?  ExPASy
    Phosphopyruvate hydratase 2-phospho-D-glycerate = phosphoenolpyruvate + H2O
  • TIGRFAM:
    Metabolism Energy metabolism Glycolysis/gluconeogenesis phosphopyruvate hydratase (TIGR01060; EC 4.2.1.11; HMM-score: 689.2)
    and 4 more
    Metabolism Energy metabolism Fermentation methylaspartate ammonia-lyase (TIGR01502; EC 4.3.1.2; HMM-score: 24.3)
    Metabolism 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)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Menaquinone and ubiquinone o-succinylbenzoate synthase (TIGR01928; EC 4.2.1.113; HMM-score: 21.6)
  • TheSEED: see SPH_1222
  • PFAM:
    Enolase_TIM (CL0256) Enolase_C; Enolase, C-terminal TIM barrel domain (PF00113; HMM-score: 435.1)
    and 3 more
    Enolase_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]

⊟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]

⊟Expression data[edit | edit source]

⊟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)

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