RegulonDB

Gene
Name:	csgA
Synonym(s):	ECK1028, EG11489, b1042
Genome position(nucleotides):	1104447 --> 1104902 Genome Browser
Strand:	forward
Sequence:	Get nucleotide sequence FastaFormat
GC content %:	51.1
External database links:

ASAP:	ABE-0003537
CGSC:	30620
ECHOBASE:	EB1452
ECOLIHUB:	csgA
OU-MICROARRAY:	b1042
STRING:	511145.b1042
COLOMBOS:	csgA

Gene

Name:

csgA

Synonym(s):

ECK1028, EG11489, b1042

Genome position(nucleotides):

1104447 --> 1104902 Genome Browser

Strand:

forward

Sequence:

Get nucleotide sequence FastaFormat

GC content %:

51.1

External database links:

ASAP:

CGSC:

ECHOBASE:

ECOLIHUB:

OU-MICROARRAY:

STRING:

COLOMBOS:

Product

Name:

curlin, major subunit

Synonym(s):

CsgA

Sequence:

Get amino acid sequence Fasta Format

Cellular location:

extracellular space,pilus

Molecular weight:

15.049

Isoelectric point:

4.889

Motif(s):

Type	Positions	Sequence
	54 -> 54	N
	111 -> 132	SEMTVKQFGGGNGAAVDQTASN
	1 -> 22	MKLLKVAAIAAIVFSGSALAGV
	21 -> 151	GVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY
	49 -> 49	Q

Classification:

Multifun Terms (GenProtEC)
		1 - metabolism --> 1.6 - biosynthesis of macromolecules (cellular constituents) --> 1.6.13 - fimbri, pili
		5 - cell processes --> 5.10 - defense/survival
Gene Ontology Terms (GO)
	cellular_component	GO:0009289 - pilus GO:0005576 - extracellular region
	molecular_function	GO:0005515 - protein binding GO:0042802 - identical protein binding
	biological_process	GO:0007155 - cell adhesion GO:0044010 - single-species biofilm formation

Note(s):

Note(s): ...[more].

Evidence:

[IDA] Inferred from direct assay

Reference(s):

[1] Arnqvist A., et al., 1992
[2] Balistreri A., et al., 2020
[3] Chapman MR., et al., 2002
[4] DeBenedictis EP., et al., 2016
[5] Hammer ND., et al., 2007
[6] Kan A., et al., 2019
[7] Klein RD., et al., 2018
[8] Li Y., et al., 2020
[9] Loferer H., et al., 1997
[10] Olsen A., et al., 1993
[11] Onur T., et al., 2018
[12] Perov S., et al., 2019
[13] Samoilova Z., et al., 2019
[14] Sugimoto S., et al., 2018
[15] Swasthi HM., et al., 2018
[16] Yan Z., et al., 2020
[17] Yuca E., et al., 2021

External database links:

DIP:

ECOCYC:

ECOLIWIKI:

INTERPRO:

PDB:

PDB:

PDB:

PDB:

PFAM:

PRIDE:

PRODB:

REFSEQ:

SMR:

UNIPROT:

Transcriptional Regulation
	Display Regulation
Activated by:	BolA, CsgD
Repressed by:	FliZ, CpxR, BtsR

Transcriptional Regulation

Display Regulation

Activated by:

BolA, CsgD

Repressed by:

FliZ, CpxR, BtsR

	Type	Name	Post Left	Post Right	Strand	Notes	Evidence (Confirmed, Strong, Weak)	References
	promoter	ymdAp5	1105225		forward	nd	[ICWHO]	[18]

Type

Name

Post Left

Post Right

Strand

Notes

Evidence (Confirmed, Strong, Weak)

References

promoter

ymdAp5

1105225

forward

[ICWHO]

[18]

Evidence
[ICWHO] Inferred computationally without human oversight

Evidence

[ICWHO] Inferred computationally without human oversight

Reference(s)
[1] Arnqvist A., Olsen A., Pfeifer J., Russell DG., Normark S., 1992, The Crl protein activates cryptic genes for curli formation and fibronectin binding in Escherichia coli HB101., Mol Microbiol 6(17):2443-52
[2] Balistreri A., Kahana E., Janakiraman S., Chapman MR., 2020, Tuning Functional Amyloid Formation Through Disulfide Engineering., Front Microbiol 11:944
[3] Chapman MR., Robinson LS., Pinkner JS., Roth R., Heuser J., Hammar M., Normark S., Hultgren SJ., 2002, Role of Escherichia coli curli operons in directing amyloid fiber formation., Science 295(5556):851-5
[4] DeBenedictis EP., Liu J., Keten S., 2016, Adhesion mechanisms of curli subunit CsgA to abiotic surfaces., Sci Adv 2(11):e1600998
[5] Hammer ND., Schmidt JC., Chapman MR., 2007, The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization., Proc Natl Acad Sci U S A 104(30):12494-9
[6] Kan A., Birnbaum DP., Praveschotinunt P., Joshi NS., 2019, Congo Red Fluorescence for Rapid In Situ Characterization of Synthetic Curli Systems., Appl Environ Microbiol 85(13)
[7] Klein RD., Shu Q., Cusumano ZT., Nagamatsu K., Gualberto NC., Lynch AJL., Wu C., Wang W., Jain N., Pinkner JS., Amarasinghe GK., Hultgren SJ., Frieden C., Chapman MR., 2018, Structure-Function Analysis of the Curli Accessory Protein CsgE Defines Surfaces Essential for Coordinating Amyloid Fiber Formation., MBio 9(4)
[8] Li Y., Li K., Wang X., Cui M., Ge P., Zhang J., Qiu F., Zhong C., 2020, Conformable self-assembling amyloid protein coatings with genetically programmable functionality., Sci Adv 6(21):eaba1425
[9] Loferer H., Hammar M., Normark S., 1997, Availability of the fibre subunit CsgA and the nucleator protein CsgB during assembly of fibronectin-binding curli is limited by the intracellular concentration of the novel lipoprotein CsgG., Mol Microbiol 26(1):11-23
[10] Olsen A., Arnqvist A., Hammar M., Sukupolvi S., Normark S., 1993, The RpoS sigma factor relieves H-NS-mediated transcriptional repression of csgA, the subunit gene of fibronectin-binding curli in Escherichia coli., Mol Microbiol 7(4):523-36
[11] Onur T., Yuca E., Olmez TT., Seker UOS., 2018, Self-assembly of bacterial amyloid protein nanomaterials on solid surfaces., J Colloid Interface Sci 520:145-154
[12] Perov S., Lidor O., Salinas N., Golan N., Tayeb-Fligelman E., Deshmukh M., Willbold D., Landau M., 2019, Structural Insights into Curli CsgA Cross-β Fibril Architecture Inspire Repurposing of Anti-amyloid Compounds as Anti-biofilm Agents., PLoS Pathog 15(8):e1007978
[13] Samoilova Z., Tyulenev A., Muzyka N., Smirnova G., Oktyabrsky O., 2019, Tannic and gallic acids alter redox-parameters of the medium and modulate biofilm formation., AIMS Microbiol 5(4):379-392
[14] Sugimoto S., Arita-Morioka KI., Terao A., Yamanaka K., Ogura T., Mizunoe Y., 2018, Multitasking of Hsp70 chaperone in the biogenesis of bacterial functional amyloids., Commun Biol 1:52
[15] Swasthi HM., Bhasne K., Mahapatra S., Mukhopadhyay S., 2018, Human Fibrinogen Inhibits Amyloid Assembly of Biofilm-Forming CsgA., Biochemistry 57(44):6270-6273
[16] Yan Z., Yin M., Chen J., Li X., 2020, Assembly and substrate recognition of curli biogenesis system., Nat Commun 11(1):241
[17] Yuca E., Åžahin Kehribar E., Åžeker UÃ–Åž., 2021, Interaction of microbial functional amyloids with solid surfaces., Colloids Surf B Biointerfaces 199:111547
[18] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78

Reference(s)

[1] Arnqvist A., Olsen A., Pfeifer J., Russell DG., Normark S., 1992, The Crl protein activates cryptic genes for curli formation and fibronectin binding in Escherichia coli HB101., Mol Microbiol 6(17):2443-52

[2] Balistreri A., Kahana E., Janakiraman S., Chapman MR., 2020, Tuning Functional Amyloid Formation Through Disulfide Engineering., Front Microbiol 11:944

[3] Chapman MR., Robinson LS., Pinkner JS., Roth R., Heuser J., Hammar M., Normark S., Hultgren SJ., 2002, Role of Escherichia coli curli operons in directing amyloid fiber formation., Science 295(5556):851-5

[4] DeBenedictis EP., Liu J., Keten S., 2016, Adhesion mechanisms of curli subunit CsgA to abiotic surfaces., Sci Adv 2(11):e1600998

[5] Hammer ND., Schmidt JC., Chapman MR., 2007, The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization., Proc Natl Acad Sci U S A 104(30):12494-9

[6] Kan A., Birnbaum DP., Praveschotinunt P., Joshi NS., 2019, Congo Red Fluorescence for Rapid In Situ Characterization of Synthetic Curli Systems., Appl Environ Microbiol 85(13)

[7] Klein RD., Shu Q., Cusumano ZT., Nagamatsu K., Gualberto NC., Lynch AJL., Wu C., Wang W., Jain N., Pinkner JS., Amarasinghe GK., Hultgren SJ., Frieden C., Chapman MR., 2018, Structure-Function Analysis of the Curli Accessory Protein CsgE Defines Surfaces Essential for Coordinating Amyloid Fiber Formation., MBio 9(4)

[8] Li Y., Li K., Wang X., Cui M., Ge P., Zhang J., Qiu F., Zhong C., 2020, Conformable self-assembling amyloid protein coatings with genetically programmable functionality., Sci Adv 6(21):eaba1425

[9] Loferer H., Hammar M., Normark S., 1997, Availability of the fibre subunit CsgA and the nucleator protein CsgB during assembly of fibronectin-binding curli is limited by the intracellular concentration of the novel lipoprotein CsgG., Mol Microbiol 26(1):11-23

[10] Olsen A., Arnqvist A., Hammar M., Sukupolvi S., Normark S., 1993, The RpoS sigma factor relieves H-NS-mediated transcriptional repression of csgA, the subunit gene of fibronectin-binding curli in Escherichia coli., Mol Microbiol 7(4):523-36

[11] Onur T., Yuca E., Olmez TT., Seker UOS., 2018, Self-assembly of bacterial amyloid protein nanomaterials on solid surfaces., J Colloid Interface Sci 520:145-154

[12] Perov S., Lidor O., Salinas N., Golan N., Tayeb-Fligelman E., Deshmukh M., Willbold D., Landau M., 2019, Structural Insights into Curli CsgA Cross-β Fibril Architecture Inspire Repurposing of Anti-amyloid Compounds as Anti-biofilm Agents., PLoS Pathog 15(8):e1007978

[13] Samoilova Z., Tyulenev A., Muzyka N., Smirnova G., Oktyabrsky O., 2019, Tannic and gallic acids alter redox-parameters of the medium and modulate biofilm formation., AIMS Microbiol 5(4):379-392

[14] Sugimoto S., Arita-Morioka KI., Terao A., Yamanaka K., Ogura T., Mizunoe Y., 2018, Multitasking of Hsp70 chaperone in the biogenesis of bacterial functional amyloids., Commun Biol 1:52

[15] Swasthi HM., Bhasne K., Mahapatra S., Mukhopadhyay S., 2018, Human Fibrinogen Inhibits Amyloid Assembly of Biofilm-Forming CsgA., Biochemistry 57(44):6270-6273

[16] Yan Z., Yin M., Chen J., Li X., 2020, Assembly and substrate recognition of curli biogenesis system., Nat Commun 11(1):241

[17] Yuca E., Åžahin Kehribar E., Åžeker UÃ–Åž., 2021, Interaction of microbial functional amyloids with solid surfaces., Colloids Surf B Biointerfaces 199:111547

[18] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78