RegulonDB

Gene
Name:	csgB
Synonym(s):	ECK1027, G6547, b1041
Genome position(nucleotides):	1103951 --> 1104406 Genome Browser
Strand:	forward
Sequence:	Get nucleotide sequence FastaFormat
GC content %:	41.89
External database links:

ASAP:	ABE-0003534
ECHOBASE:	EB2505
ECOLIHUB:	csgB
OU-MICROARRAY:	b1041
STRING:	511145.b1041
COLOMBOS:	csgB

Gene

Name:

csgB

Synonym(s):

ECK1027, G6547, b1041

Genome position(nucleotides):

1103951 --> 1104406 Genome Browser

Strand:

forward

Sequence:

Get nucleotide sequence FastaFormat

GC content %:

41.89

External database links:

ASAP:

ECHOBASE:

ECOLIHUB:

OU-MICROARRAY:

STRING:

COLOMBOS:

Product

Name:

curlin, minor subunit

Synonym(s):

CsgB

Sequence:

Get amino acid sequence Fasta Format

Cellular location:

pilus,outer membrane

Molecular weight:

15.882

Isoelectric point:

10.043

Motif(s):

Type	Positions	Sequence
	97 -> 130	GSANDASISQGAYGNTAMIIQKGSGNKANITQYG
	1 -> 21	MKNKLLFMMLTILGAPGIAAA
	75 -> 106	GSSNRAKIDQTGDYNLAYIDQAGSANDASISQ
	22 -> 151	AGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTGDYNLAYIDQAGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAIVVQRQSQMAIRVTQR
	53 -> 86	GTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTG

Classification:

Multifun Terms (GenProtEC)
		1 - metabolism --> 1.6 - biosynthesis of macromolecules (cellular constituents) --> 1.6.11 - glycoprotein
		6 - cell structure --> 6.5 - pilus
Gene Ontology Terms (GO)
	cellular_component	GO:0009279 - cell outer membrane GO:0009289 - pilus
	molecular_function	GO:0005515 - protein binding GO:0042802 - identical protein binding
	biological_process	GO:0098775 - curli assembly GO:0007155 - cell adhesion GO:0044010 - single-species biofilm formation GO:1990000 - amyloid fibril formation

Note(s):

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

Evidence:

[APPHINH] Assay of protein purified to homogeneity from its native host
[IMP] Inferred from mutant phenotype

Reference(s):

[1] Hammar M., et al., 1995
[2] Hammer ND., et al., 2007
[3] Mao X., et al., 2019
[4] Onur T., et al., 2018
[5] Serra DO., et al., 2013
[6] Shewmaker F., et al., 2009
[7] Shu Q., et al., 2012
[8] Sugimoto S., et al., 2018
[9] Yuca E., et al., 2021

External database links:

DIP:

ECOCYC:

ECOLIWIKI:

INTERPRO:

PFAM:

PRIDE:

REFSEQ:

UNIPROT:

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

Transcriptional Regulation

Display Regulation

Activated by:

CsgD

Repressed by:

FliZ, CpxR, BtsR

Reference(s)
[1] Hammar M., Arnqvist A., Bian Z., Olsen A., Normark S., 1995, Expression of two csg operons is required for production of fibronectin- and congo red-binding curli polymers in Escherichia coli K-12., Mol Microbiol 18(4):661-70
[2] 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
[3] Mao X., Li K., Liu M., Wang X., Zhao T., An B., Cui M., Li Y., Pu J., Li J., Wang L., Lu TK., Fan C., Zhong C., 2019, Directing curli polymerization with DNA origami nucleators., Nat Commun 10(1):1395
[4] 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
[5] Serra DO., Richter AM., Hengge R., 2013, Cellulose as an architectural element in spatially structured Escherichia coli biofilms., J Bacteriol 195(24):5540-54
[6] Shewmaker F., McGlinchey RP., Thurber KR., McPhie P., Dyda F., Tycko R., Wickner RB., 2009, The Functional Curli Amyloid Is Not Based on In-register Parallel {beta}-Sheet Structure., J Biol Chem 284(37):25065-76
[7] Shu Q., Crick SL., Pinkner JS., Ford B., Hultgren SJ., Frieden C., 2012, The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism., Proc Natl Acad Sci U S A 109(17):6502-7
[8] 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
[9] Yuca E., Åžahin Kehribar E., Åžeker UÃ–Åž., 2021, Interaction of microbial functional amyloids with solid surfaces., Colloids Surf B Biointerfaces 199:111547

Reference(s)

[1] Hammar M., Arnqvist A., Bian Z., Olsen A., Normark S., 1995, Expression of two csg operons is required for production of fibronectin- and congo red-binding curli polymers in Escherichia coli K-12., Mol Microbiol 18(4):661-70

[2] 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

[3] Mao X., Li K., Liu M., Wang X., Zhao T., An B., Cui M., Li Y., Pu J., Li J., Wang L., Lu TK., Fan C., Zhong C., 2019, Directing curli polymerization with DNA origami nucleators., Nat Commun 10(1):1395

[4] 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

[5] Serra DO., Richter AM., Hengge R., 2013, Cellulose as an architectural element in spatially structured Escherichia coli biofilms., J Bacteriol 195(24):5540-54

[6] Shewmaker F., McGlinchey RP., Thurber KR., McPhie P., Dyda F., Tycko R., Wickner RB., 2009, The Functional Curli Amyloid Is Not Based on In-register Parallel {beta}-Sheet Structure., J Biol Chem 284(37):25065-76

[7] Shu Q., Crick SL., Pinkner JS., Ford B., Hultgren SJ., Frieden C., 2012, The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism., Proc Natl Acad Sci U S A 109(17):6502-7

[8] 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

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