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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

Genome View[edit | edit source]

Gene[edit | edit source]

General[edit | edit source]

  • type: CDS
  • locus tag: MDRSPN_00976 [new locus tag: MDRSPN_RS05095 ]
  • symbol: eno
  • product: enolase
  • replicon: chromosome
  • strand: +
  • coordinates: 983383..984687
  • length: 1305
  • essential: unknown other strains

Accession numbers[edit | edit source]

  • Location: AP018391 (983383..984687) 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]

  • 1
    61
    121
    181
    241
    301
    361
    421
    481
    541
    601
    661
    721
    781
    841
    901
    961
    1021
    1081
    1141
    1201
    1261
    ATGTCAATTATTACTGATGTTTACGCTCGCGAAGTCCTAGACTCACGCGGTAACCCAACA
    CTTGAGGTAGAAGTTTATACTGAATCAGGTGCTTTCGGACGTGGTATGGTTCCATCAGGA
    GCTTCTACTGGTGAACACGAAGCAGTTGAACTTCGCGACGGTGACAAATCTCGTTACGGT
    GGTCTTGGTACACAAAAAGCTGTTGACAACGTAAACAACATCATCGCTGAAGCTATCATC
    GGCTACGATGTACGTGACCAACAAGCTATCGACCGTGCTATGATCGCACTTGACGGTACT
    CCTAACAAAGGTAAATTGGGTGCAAACGCAATTCTTGGTGTGTCTATCGCTGTAGCTCGT
    GCTGCTGCTGACTACCTTGAAATCCCACTTTACAGCTACCTTGGTGGATTCAACACTAAA
    GTTCTTCCAACTCCAATGATGAACATCATCAACGGTGGTTCTCACTCTGACGCTCCAATC
    GCTTTCCAAGAATTCATGATCGTACCTGCTGGTGCACCAACATTCAAAGAAGCTCTTCGT
    TGGGGTGCTGAAATCTTCCACGCTCTTAAGAAAATTCTTAAATCACGTGGTTTGGAAACA
    GCCGTAGGTGACGAAGGTGGATTCGCTCCTCGTTTCGAAGGAACTGAAGACGGTGTTGAA
    ACTATCCTTGCTGCAATCGAAGCTGCTGGATATGTTCCTGGTAAAGACGTATTTATCGGA
    TTTGACTGTGCTTCATCAGAATTCTATGATGAAGAACGTAAAGTTTACGACTACACTAAA
    TTTGAAGGTGAAGGCGCTGCTGTACGTACTGCTGCAGAACAAATCGACTACCTTGAAGAA
    TTGGTAAACAAATACCCAATCATCACTATCGAAGATGGTATGGATGAAAACGACTGGGAC
    GGTTGGAAAGCTCTTACTGAACGTCTTGGTGGTAAAGTACAATTGGTTGGTGATGACTTC
    TTCGTAACAAACACTTCTTACCTTGAAAAAGGTATTGCAGAAGGTGCTGCTAACTCAATC
    CTTATCAAAGTTAACCAAATCGGTACTCTTACTGAAACATTCGACGCTATCGAAATGGCG
    AAAGAAGCTGGTTACACTGCAGTTGTATCACACCGTTCAGGTGAAACTGAAGATTCAACA
    ATCGCTGACATCGCAGTTGCAACTAACGCAGGACAAATCAAGACTGGTTCACTTTCACGT
    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: MDRSPN_00976 [new locus tag: MDRSPN_RS05095 ]
  • symbol: Eno
  • description: enolase
  • length: 434
  • theoretical pI: 4.34278
  • theoretical MW: 46928.3
  • GRAVY: -0.194931

Function[edit | edit source]

  • TIGRFAM:
    Metabolism Energy metabolism Glycolysis/gluconeogenesis phosphopyruvate hydratase (TIGR01060; EC 4.2.1.11; HMM-score: 687.8)
    and 4 more
    Metabolism Energy metabolism Fermentation methylaspartate ammonia-lyase (TIGR01502; EC 4.3.1.2; HMM-score: 22.9)
    Metabolism Energy metabolism Amino acids and amines methylaspartate ammonia-lyase (TIGR01502; EC 4.3.1.2; HMM-score: 22.9)
    muconate and chloromuconate cycloisomerases (TIGR02534; EC 5.5.1.-; HMM-score: 19.9)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Menaquinone and ubiquinone o-succinylbenzoate synthase (TIGR01928; EC 4.2.1.113; HMM-score: 18.6)
  • TheSEED: data available for D39, Hungary19A-6, TIGR4
  • PFAM:
    Enolase_TIM (CL0256) Enolase_C; Enolase, C-terminal TIM barrel domain (PF00113; HMM-score: 432.5)
    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: 31.5)
    MR_MLE_C; Enolase C-terminal domain-like (PF13378; HMM-score: 28.7)

Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • effectors:

Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.97
    • Cytoplasmic Membrane Score: 0
    • Cellwall Score: 0.01
    • Extracellular Score: 0.02
    • 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: BBA59179 NCBI
  • UniProt:

Protein sequence[edit | edit source]

  • MSIITDVYAREVLDSRGNPTLEVEVYTESGAFGRGMVPSGASTGEHEAVELRDGDKSRYGGLGTQKAVDNVNNIIAEAIIGYDVRDQQAIDRAMIALDGTPNKGKLGANAILGVSIAVARAAADYLEIPLYSYLGGFNTKVLPTPMMNIINGGSHSDAPIAFQEFMIVPAGAPTFKEALRWGAEIFHALKKILKSRGLETAVGDEGGFAPRFEGTEDGVETILAAIEAAGYVPGKDVFIGFDCASSEFYDEERKVYDYTKFEGEGAAVRTAAEQIDYLEELVNKYPIITIEDGMDENDWDGWKALTERLGGKVQLVGDDFFVTNTSYLEKGIAEGAANSILIKVNQIGTLTETFDAIEMAKEAGYTAVVSHRSGETEDSTIADIAVATNAGQIKTGSLSRTDRIAKYNQLLRIEDQLGEVAEYRGLKSFYNLKK

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)

NCBI: 05-OCT-2017

Summary[edit | edit source]

  • organism: Streptococcus pneumoniae MDRSPN001
  • locus tag: MDRSPN_00976 [new locus tag: MDRSPN_RS05095 ]
  • pan locus tag?: PNEUPAN002277000
  • symbol: eno
  • pan gene symbol?: eno
  • synonym:
  • product: enolase

Genome View[edit | edit source]

Gene[edit | edit source]

General[edit | edit source]

  • type: CDS
  • locus tag: MDRSPN_00976 [new locus tag: MDRSPN_RS05095 ]
  • symbol: eno
  • product: enolase
  • replicon: chromosome
  • strand: +
  • coordinates: 983383..984687
  • length: 1305
  • essential: unknown other strains

Accession numbers[edit | edit source]

  • Location: AP018391 (983383..984687) 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]

  • 1
    61
    121
    181
    241
    301
    361
    421
    481
    541
    601
    661
    721
    781
    841
    901
    961
    1021
    1081
    1141
    1201
    1261
    ATGTCAATTATTACTGATGTTTACGCTCGCGAAGTCCTAGACTCACGCGGTAACCCAACA
    CTTGAGGTAGAAGTTTATACTGAATCAGGTGCTTTCGGACGTGGTATGGTTCCATCAGGA
    GCTTCTACTGGTGAACACGAAGCAGTTGAACTTCGCGACGGTGACAAATCTCGTTACGGT
    GGTCTTGGTACACAAAAAGCTGTTGACAACGTAAACAACATCATCGCTGAAGCTATCATC
    GGCTACGATGTACGTGACCAACAAGCTATCGACCGTGCTATGATCGCACTTGACGGTACT
    CCTAACAAAGGTAAATTGGGTGCAAACGCAATTCTTGGTGTGTCTATCGCTGTAGCTCGT
    GCTGCTGCTGACTACCTTGAAATCCCACTTTACAGCTACCTTGGTGGATTCAACACTAAA
    GTTCTTCCAACTCCAATGATGAACATCATCAACGGTGGTTCTCACTCTGACGCTCCAATC
    GCTTTCCAAGAATTCATGATCGTACCTGCTGGTGCACCAACATTCAAAGAAGCTCTTCGT
    TGGGGTGCTGAAATCTTCCACGCTCTTAAGAAAATTCTTAAATCACGTGGTTTGGAAACA
    GCCGTAGGTGACGAAGGTGGATTCGCTCCTCGTTTCGAAGGAACTGAAGACGGTGTTGAA
    ACTATCCTTGCTGCAATCGAAGCTGCTGGATATGTTCCTGGTAAAGACGTATTTATCGGA
    TTTGACTGTGCTTCATCAGAATTCTATGATGAAGAACGTAAAGTTTACGACTACACTAAA
    TTTGAAGGTGAAGGCGCTGCTGTACGTACTGCTGCAGAACAAATCGACTACCTTGAAGAA
    TTGGTAAACAAATACCCAATCATCACTATCGAAGATGGTATGGATGAAAACGACTGGGAC
    GGTTGGAAAGCTCTTACTGAACGTCTTGGTGGTAAAGTACAATTGGTTGGTGATGACTTC
    TTCGTAACAAACACTTCTTACCTTGAAAAAGGTATTGCAGAAGGTGCTGCTAACTCAATC
    CTTATCAAAGTTAACCAAATCGGTACTCTTACTGAAACATTCGACGCTATCGAAATGGCG
    AAAGAAGCTGGTTACACTGCAGTTGTATCACACCGTTCAGGTGAAACTGAAGATTCAACA
    ATCGCTGACATCGCAGTTGCAACTAACGCAGGACAAATCAAGACTGGTTCACTTTCACGT
    ACAGACCGCATCGCTAAATACAACCAATTGCTTCGTATCGAAGACCAACTTGGTGAAGTA
    GCTGAATATCGTGGATTGAAATCATTCTACAACCTTAAAAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1305

This data comes from external databases and cannot be edited.

Protein[edit | edit source]

General[edit | edit source]

  • locus tag: MDRSPN_00976 [new locus tag: MDRSPN_RS05095 ]
  • symbol: Eno
  • description: enolase
  • length: 434
  • theoretical pI: 4.34278
  • theoretical MW: 46928.3
  • GRAVY: -0.194931

Function[edit | edit source]

  • TIGRFAM:
    Metabolism Energy metabolism Glycolysis/gluconeogenesis phosphopyruvate hydratase (TIGR01060; EC 4.2.1.11; HMM-score: 687.8)
    and 4 more
    Metabolism Energy metabolism Fermentation methylaspartate ammonia-lyase (TIGR01502; EC 4.3.1.2; HMM-score: 22.9)
    Metabolism Energy metabolism Amino acids and amines methylaspartate ammonia-lyase (TIGR01502; EC 4.3.1.2; HMM-score: 22.9)
    muconate and chloromuconate cycloisomerases (TIGR02534; EC 5.5.1.-; HMM-score: 19.9)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Menaquinone and ubiquinone o-succinylbenzoate synthase (TIGR01928; EC 4.2.1.113; HMM-score: 18.6)
  • TheSEED: data available for D39, Hungary19A-6, TIGR4
  • PFAM:
    Enolase_TIM (CL0256) Enolase_C; Enolase, C-terminal TIM barrel domain (PF00113; HMM-score: 432.5)
    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: 31.5)
    MR_MLE_C; Enolase C-terminal domain-like (PF13378; HMM-score: 28.7)

Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • effectors:

Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.97
    • Cytoplasmic Membrane Score: 0
    • Cellwall Score: 0.01
    • Extracellular Score: 0.02
    • 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: BBA59179 NCBI
  • UniProt:

Protein sequence[edit | edit source]

  • MSIITDVYAREVLDSRGNPTLEVEVYTESGAFGRGMVPSGASTGEHEAVELRDGDKSRYGGLGTQKAVDNVNNIIAEAIIGYDVRDQQAIDRAMIALDGTPNKGKLGANAILGVSIAVARAAADYLEIPLYSYLGGFNTKVLPTPMMNIINGGSHSDAPIAFQEFMIVPAGAPTFKEALRWGAEIFHALKKILKSRGLETAVGDEGGFAPRFEGTEDGVETILAAIEAAGYVPGKDVFIGFDCASSEFYDEERKVYDYTKFEGEGAAVRTAAEQIDYLEELVNKYPIITIEDGMDENDWDGWKALTERLGGKVQLVGDDFFVTNTSYLEKGIAEGAANSILIKVNQIGTLTETFDAIEMAKEAGYTAVVSHRSGETEDSTIADIAVATNAGQIKTGSLSRTDRIAKYNQLLRIEDQLGEVAEYRGLKSFYNLKK

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]

This data comes from external databases and cannot be edited.

This data comes from external databases and cannot be edited.

This data comes from external databases and cannot be edited.

This data comes from external databases and cannot be edited.

This data comes from external databases and cannot be edited.

This data comes from external databases and cannot be edited.

This data comes from external databases and cannot be edited.

Other Information[edit | edit source]

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)