RegulonDB RegulonDB 11.0: Gene Form
   

csgB gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

csgD csgB csgA BtsR Cra CpxR CsgD CsgD CsgD CsgD RcdA CpxR Cra Cra CpxR CpxR CpxR CRP CsgD IHF CpxR CpxR MlrA CsgD CpxR CpxR CpxR BasR MqsA CpxR CpxR CpxR CpxR RstA CpxR OmpR IHF CRP BtsR CpxR CpxR CsgD CsgD BtsR Cra ppGpp anti-terminator anti-anti-terminator csgAp csgAp csgBp2 csgBp2 csgBp csgBp csgDp3 csgDp3 csgDp1 csgDp1 csgDp2 csgDp2 csgDp csgDp

Gene      
Name: csgB    Texpresso search in the literature
Synonym(s): ECK1027, G6547, b1041
Genome position(nucleotides): 1103951 --> 1104406
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


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 Comment
1 -> 21 MKNKLLFMMLTILGAPGIAAA
22 -> 151 AGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTGDYNLAYIDQAGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAIVVQRQSQMAIRVTQR UniProt: Minor curlin subunit.
53 -> 86 GTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTG
75 -> 106 GSSNRAKIDQTGDYNLAYIDQAGSANDASISQ
97 -> 130 GSANDASISQGAYGNTAMIIQKGSGNKANITQYG

 

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:  
ALPHAFOLD:
P0ABK7
DIP:
DIP-46504N
ECOCYC:
G6547-MONOMER
ECOLIWIKI:
b1041
INTERPRO:
IPR009742
PFAM:
PF07012
PRIDE:
P0ABK7
REFSEQ:
NP_415559
UNIPROT:
P0ABK7


Operon      
Name: csgBAC         
Operon arrangement:
Transcription unit        Promoter
csgBAC
csgBAC
csgA
csgC


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


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References


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., Şahin Kehribar E., Şeker UÖŞ., 2021, Interaction of microbial functional amyloids with solid surfaces., Colloids Surf B Biointerfaces 199:111547


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