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Conserved domains on  [gi|527038287|ref|WP_020884698|]
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MULTISPECIES: curli minor subunit CsgB [Enterobacter]

Protein Classification

curlin minor subunit CsgB( domain architecture ID 11484578)

curlin minor subunit CsgB is required for CsgA polymerization on the cell surface

Gene Symbol:  csgB
Gene Ontology:  GO:0098775
PubMed:  17636121|22684146|31932609

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
csgB PRK10101
curlin minor subunit CsgB; Provisional
 1-151 3.57e-84

curlin minor subunit CsgB; Provisional


:

Pssm-ID: 182242 [Multi-domain]  Cd Length: 151  Bit Score: 243.61  E-value: 3.57e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527038287   1 MKNTSLFMMFTLLGAPGFVIAADSDLANAEYNFTVNELSRSSLNQAAIIGQQGMLNDAQVRQDGSKLLSIVSQDGAGNRA 80
Cdd:PRK10101   1 MKNKLLFMMLTILGAPGIAAAAGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQVRQGGSKLLAVVSQEGSSNRA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527038287  81 RVDQSGTYNIAWIDQSGSANDAGITQDGYGNSAKIIQKGSGNRANITQYGTQKTAVVVQRQSQMAIRVIQR 151
Cdd:PRK10101  81 KIDQTGDYNLAYIDQTGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAVVVQRQSQMAIRVTQR 151
 
Name Accession Description Interval E-value
csgB PRK10101
curlin minor subunit CsgB; Provisional
 1-151 3.57e-84

curlin minor subunit CsgB; Provisional


Pssm-ID: 182242 [Multi-domain]  Cd Length: 151  Bit Score: 243.61  E-value: 3.57e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527038287   1 MKNTSLFMMFTLLGAPGFVIAADSDLANAEYNFTVNELSRSSLNQAAIIGQQGMLNDAQVRQDGSKLLSIVSQDGAGNRA 80
Cdd:PRK10101   1 MKNKLLFMMLTILGAPGIAAAAGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQVRQGGSKLLAVVSQEGSSNRA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527038287  81 RVDQSGTYNIAWIDQSGSANDAGITQDGYGNSAKIIQKGSGNRANITQYGTQKTAVVVQRQSQMAIRVIQR 151
Cdd:PRK10101  81 KIDQTGDYNLAYIDQTGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAVVVQRQSQMAIRVTQR 151
Curlin_rpt pfam07012
Curlin associated repeat; This family consists of several bacterial repeats of around 30 ...
 97-130 7.70e-07

Curlin associated repeat; This family consists of several bacterial repeats of around 30 residues in length. These repeats are often found in multiple copies in the curlin proteins CsgA and CsgB. Curli fibres are thin aggregative surface fibres, connected with adhesion, which bind laminin, fibronectin, plasminogen, human contact phase proteins, and major histocompatibility complex (MHC) class I molecules. Curli fibres are coded for by the csg gene cluster, which is comprised of two divergently transcribed operons. One operon encodes the csgB, csgA, and csgC genes, while the other encodes csgD, csgE, csgF, and csgG. The assembly of the fibres is unique and involves extracellular self-assembly of the curlin subunit (CsgA), dependent on a specific nucleator protein (CsgB). CsgD is a transcriptional activator essential for expression of the two curli fibre operons, and CsgG is an outer membrane lipoprotein involved in extracellular stabilization of CsgA and CsgB.


Pssm-ID: 429248 [Multi-domain]  Cd Length: 34  Bit Score: 43.22  E-value: 7.70e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 527038287   97 GSANDAGITQDGYGNSAKIIQKGSGNRANITQYG 130
Cdd:pfam07012   1 GDDNTADITQSGDNNSAYVGQSGSNNDATVTQTG 34
 
Name Accession Description Interval E-value
csgB PRK10101
curlin minor subunit CsgB; Provisional
 1-151 3.57e-84

curlin minor subunit CsgB; Provisional


Pssm-ID: 182242 [Multi-domain]  Cd Length: 151  Bit Score: 243.61  E-value: 3.57e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527038287   1 MKNTSLFMMFTLLGAPGFVIAADSDLANAEYNFTVNELSRSSLNQAAIIGQQGMLNDAQVRQDGSKLLSIVSQDGAGNRA 80
Cdd:PRK10101   1 MKNKLLFMMLTILGAPGIAAAAGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQVRQGGSKLLAVVSQEGSSNRA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527038287  81 RVDQSGTYNIAWIDQSGSANDAGITQDGYGNSAKIIQKGSGNRANITQYGTQKTAVVVQRQSQMAIRVIQR 151
Cdd:PRK10101  81 KIDQTGDYNLAYIDQTGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAVVVQRQSQMAIRVTQR 151
Curlin_rpt pfam07012
Curlin associated repeat; This family consists of several bacterial repeats of around 30 ...
 97-130 7.70e-07

Curlin associated repeat; This family consists of several bacterial repeats of around 30 residues in length. These repeats are often found in multiple copies in the curlin proteins CsgA and CsgB. Curli fibres are thin aggregative surface fibres, connected with adhesion, which bind laminin, fibronectin, plasminogen, human contact phase proteins, and major histocompatibility complex (MHC) class I molecules. Curli fibres are coded for by the csg gene cluster, which is comprised of two divergently transcribed operons. One operon encodes the csgB, csgA, and csgC genes, while the other encodes csgD, csgE, csgF, and csgG. The assembly of the fibres is unique and involves extracellular self-assembly of the curlin subunit (CsgA), dependent on a specific nucleator protein (CsgB). CsgD is a transcriptional activator essential for expression of the two curli fibre operons, and CsgG is an outer membrane lipoprotein involved in extracellular stabilization of CsgA and CsgB.


Pssm-ID: 429248 [Multi-domain]  Cd Length: 34  Bit Score: 43.22  E-value: 7.70e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 527038287   97 GSANDAGITQDGYGNSAKIIQKGSGNRANITQYG 130
Cdd:pfam07012   1 GDDNTADITQSGDNNSAYVGQSGSNNDATVTQTG 34
Curlin_rpt pfam07012
Curlin associated repeat; This family consists of several bacterial repeats of around 30 ...
 75-108 1.23e-04

Curlin associated repeat; This family consists of several bacterial repeats of around 30 residues in length. These repeats are often found in multiple copies in the curlin proteins CsgA and CsgB. Curli fibres are thin aggregative surface fibres, connected with adhesion, which bind laminin, fibronectin, plasminogen, human contact phase proteins, and major histocompatibility complex (MHC) class I molecules. Curli fibres are coded for by the csg gene cluster, which is comprised of two divergently transcribed operons. One operon encodes the csgB, csgA, and csgC genes, while the other encodes csgD, csgE, csgF, and csgG. The assembly of the fibres is unique and involves extracellular self-assembly of the curlin subunit (CsgA), dependent on a specific nucleator protein (CsgB). CsgD is a transcriptional activator essential for expression of the two curli fibre operons, and CsgG is an outer membrane lipoprotein involved in extracellular stabilization of CsgA and CsgB.


Pssm-ID: 429248 [Multi-domain]  Cd Length: 34  Bit Score: 37.44  E-value: 1.23e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 527038287   75 GAGNRARVDQSGTYNIAWIDQSGSANDAGITQDG 108
Cdd:pfam07012   1 GDDNTADITQSGDNNSAYVGQSGSNNDATVTQTG 34
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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