RegulonDB RegulonDB 11.1: Gene Form
   

fimC gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

fimD fimC fimI terminator anti-terminator TSS_5140 TSS_5140 TSS_5139 TSS_5139 TSS_5138 TSS_5138 TSS_5137 TSS_5137

Gene      
Name: fimC    Texpresso search in the literature
Synonym(s): ECK4307, EG10310, b4316, pilB
Genome position(nucleotides): 4544304 --> 4545029
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 44.49
External database links:  
ASAP:
 ABE-0014149
CGSC:
 18352
ECHOBASE:
 EB0306
ECOLIHUB:
 fimC
OU-MICROARRAY:
 b4316
STRING:
 511145.b4316
COLOMBOS: fimC


Product      
Name: type 1 fimbriae periplasmic chaperone
Synonym(s): FimC, PilB
Sequence: Get amino acid sequence Fasta Format
Cellular location: periplasmic space
Molecular weight: 26.689
Isoelectric point: 9.809
Motif(s):
 
Type Positions Sequence Comment
1 -> 36 MSNKNVNVRKSQEITFCLLAGILMFMAMMVAGRAEA
29 -> 29 M UniProt: In strain: Clinical isolate 149 and O2:K1:H+ / MT78..
37 -> 241 GVALGATRVIYPAGQKQEQLAVTNNDENSTYLIQSWVENADGVKDGRFIVTPPLFAMKGKKENTLRILDATNNQLPQDRESLFWMNVKAIPSMDKSKLTENTLQLAIISRIKLYYRPAKLALPPDQAAEKLRFRRSANSLTLINPTPYYLTVTELNAGTRVLENALVPPMGESTVKLPSDAGSNITYRTINDYGALTPKMTGVME UniProt: Chaperone protein FimC.
54 -> 54 E UniProt: In strain: Clinical isolate 149 and O2:K1:H+ / MT78..
81 -> 81 D UniProt: In Ref. 1; CAA35967..

 
Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.4 - chaperoning, repair (refolding)
  6 - cell structure --> 6.5 - pilus
Gene Ontology Terms (GO)  
cellular_component GO:0030288 - outer membrane-bounded periplasmic space
GO:0042597 - periplasmic space
molecular_function GO:0005515 - protein binding
GO:0044183 - protein folding chaperone
biological_process GO:0071555 - cell wall organization
GO:0061077 - chaperone-mediated protein folding
Note(s): Note(s): ...[more].
Evidence: [EXP-IDA-PURIFIED-PROTEIN] Assay of protein purified to homogeneity
Reference(s): [1] Barnhart MM., et al., 2000
[2] Choudhury D., et al., 1999
[3] Hermanns U., et al., 2000
[4] Pellecchia M., et al., 1999
External database links:  
ALPHAFOLD:
 P31697
DIP:
 DIP-9611N
ECOCYC:
 EG10310-MONOMER
ECOLIWIKI:
 b4316
INTERPRO:
 IPR013783
INTERPRO:
 IPR008962
INTERPRO:
 IPR016147
INTERPRO:
 IPR016148
INTERPRO:
 IPR018046
INTERPRO:
 IPR036316
INTERPRO:
 IPR001829
MINT:
 P31697
MODBASE:
 P31697
PDB:
 6SWH
PDB:
 6E15
PDB:
 6E14
PDB:
 4J3O
PDB:
 4DWH
PDB:
 3SQB
PDB:
 3RFZ
PDB:
 3JWN
PDB:
 3BWU
PDB:
 1ZE3
PDB:
 1QUN
PDB:
 1KLF
PDB:
 1KIU
PDB:
 1BF8
PFAM:
 PF00345
PFAM:
 PF02753
PRIDE:
 P31697
PRINTS:
 PR00969
PRODB:
 PRO_000022618
PROSITE:
 PS00635
REFSEQ:
 NP_418736
SMR:
 P31697
UNIPROT:
 P31697


Operon      
Name: fimAICDFGH         
Operon arrangement:
Transcription unit        Promoter
fimAICDFGH


Transcriptional Regulation      
Display Regulation             
Activated by: H-NS, IHF, Lrp, QseB


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
  promoter TSS_5137 4544668 forward nd [RS-EPT-CBR] [5]
  promoter TSS_5138 4544808 forward nd [RS-EPT-CBR] [5]
  promoter TSS_5139 4545062 forward nd [RS-EPT-CBR] [5]
  promoter TSS_5140 4545183 forward nd [RS-EPT-CBR] [5]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates


Reference(s)    

 [1] Barnhart MM., Pinkner JS., Soto GE., Sauer FG., Langermann S., Waksman G., Frieden C., Hultgren SJ., 2000, PapD-like chaperones provide the missing information for folding of pilin proteins., Proc Natl Acad Sci U S A 97(14):7709-14

 [2] Choudhury D., Thompson A., Stojanoff V., Langermann S., Pinkner J., Hultgren SJ., Knight SD., 1999, X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli., Science 285(5430):1061-6

 [3] Hermanns U., Sebbel P., Eggli V., Glockshuber R., 2000, Characterization of FimC, a periplasmic assembly factor for biogenesis of type 1 pili in Escherichia coli., Biochemistry 39(38):11564-70

 [4] Pellecchia M., Sebbel P., Hermanns U., Wuthrich K., Glockshuber R., 1999, Pilus chaperone FimC-adhesin FimH interactions mapped by TROSY-NMR., Nat Struct Biol 6(4):336-9

 [5] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

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