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Protein

Chaperone protein FaeE

Gene

faeE

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Mediates assembly of pili by forming soluble multimeric complexes with pili subunits as an intermediate step in the assembly process. This protein is involved in K88 pili assembly. Protects pilin protein from proteolytic degradation by DegP and from premature polymerization.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Fimbrium biogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Chaperone protein FaeE
Gene namesi
Name:faeE
Encoded oniPlasmid pFM2050 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434Sequence analysisAdd
BLAST
Chaini35 – 258224Chaperone protein FaeEPRO_0000009270Add
BLAST

Proteomic databases

PRIDEiP25401.

Structurei

Secondary structure

1
258
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 394Combined sources
Beta strandi41 – 466Combined sources
Beta strandi52 – 587Combined sources
Beta strandi61 – 633Combined sources
Beta strandi65 – 7511Combined sources
Beta strandi82 – 9211Combined sources
Beta strandi97 – 1048Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi115 – 12410Combined sources
Beta strandi129 – 1324Combined sources
Beta strandi135 – 14612Combined sources
Helixi148 – 1503Combined sources
Helixi157 – 1604Combined sources
Beta strandi162 – 1654Combined sources
Beta strandi171 – 1744Combined sources
Beta strandi177 – 1793Combined sources
Beta strandi183 – 1886Combined sources
Beta strandi191 – 1933Combined sources
Helixi198 – 2047Combined sources
Beta strandi212 – 2143Combined sources
Beta strandi219 – 2257Combined sources
Beta strandi231 – 2377Combined sources
Turni243 – 2453Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3F65X-ray2.29A/B/C/D/E/F/G/H35-258[»]
3F6IX-ray2.79A/B35-258[»]
3F6LX-ray2.80A/B35-258[»]
3GEWX-ray2.00B/C35-258[»]
3GFUX-ray1.99A/C35-258[»]
ProteinModelPortaliP25401.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25401.

Family & Domainsi

Sequence similaritiesi

Belongs to the periplasmic pilus chaperone family.Curated

Keywords - Domaini

Immunoglobulin domain, Signal

Family and domain databases

Gene3Di2.60.40.360. 1 hit.
InterProiIPR008962. PapD-like.
IPR001829. Pili_assmbl_chaperone_bac.
IPR016148. Pili_assmbl_chaperone_C.
IPR018046. Pili_assmbl_chaperone_CS.
IPR016147. Pili_assmbl_chaperone_N.
[Graphical view]
PfamiPF00345. PapD_N. 1 hit.
[Graphical view]
PRINTSiPR00969. CHAPERONPILI.
SUPFAMiSSF49354. SSF49354. 1 hit.
SSF49584. SSF49584. 1 hit.
PROSITEiPS00635. PILI_CHAPERONE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25401-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKRNAVTTF FTNRVTKALG MTLALMMTCQ SAMASLAVDQ TRYIFRGDKD
60 70 80 90 100
ALTITVTNND KERTFGGQAW VDNIVEKDTR PTFVVTPSFF KVKPNGQQTL
110 120 130 140 150
RIIMASDHLP KDKESVYWLN LQDIPPALEG SGIAVALRTK LKLFYRPKAL
160 170 180 190 200
LEGRKGAEEG ISLQSRPDGR TMLVNTTPYI FAIGSLLDGN GKKIATDNGT
210 220 230 240 250
TQKLLMFMPG DEVQVKGNVV KVDSLNDYGE LQTWTINKKK PAAPEAAKAE

KADTAEQK
Length:258
Mass (Da):28,478
Last modified:May 1, 1992 - v1
Checksum:iFF80904B3DE5420B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56003 Genomic DNA. Translation: CAA39478.1.
Z11699 Genomic DNA. Translation: CAA77756.1.
PIRiS15227.
RefSeqiWP_000044493.1. NZ_LVOL01000086.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56003 Genomic DNA. Translation: CAA39478.1.
Z11699 Genomic DNA. Translation: CAA77756.1.
PIRiS15227.
RefSeqiWP_000044493.1. NZ_LVOL01000086.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3F65X-ray2.29A/B/C/D/E/F/G/H35-258[»]
3F6IX-ray2.79A/B35-258[»]
3F6LX-ray2.80A/B35-258[»]
3GEWX-ray2.00B/C35-258[»]
3GFUX-ray1.99A/C35-258[»]
ProteinModelPortaliP25401.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP25401.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP25401.

Family and domain databases

Gene3Di2.60.40.360. 1 hit.
InterProiIPR008962. PapD-like.
IPR001829. Pili_assmbl_chaperone_bac.
IPR016148. Pili_assmbl_chaperone_C.
IPR018046. Pili_assmbl_chaperone_CS.
IPR016147. Pili_assmbl_chaperone_N.
[Graphical view]
PfamiPF00345. PapD_N. 1 hit.
[Graphical view]
PRINTSiPR00969. CHAPERONPILI.
SUPFAMiSSF49354. SSF49354. 1 hit.
SSF49584. SSF49584. 1 hit.
PROSITEiPS00635. PILI_CHAPERONE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Structure and function of periplasmic chaperone-like proteins involved in the biosynthesis of K88 and K99 fimbriae in enterotoxigenic Escherichia coli."
    Bakker D., Vader C.E.M., Roosendaal B., Mooi F.R., Oudega B., de Graaf F.K.
    Mol. Microbiol. 5:875-886(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Identification of minor fimbrial subunits involved in biosynthesis of K88 fimbriae."
    Bakker D., Willemsen P.T.J., Willems R.H., Huisman T.T., Mooi F.R., Oudega B., Stegehuis F., de Graaf F.K.
    J. Bacteriol. 174:6350-6358(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-258.

Entry informationi

Entry nameiFAEE_ECOLX
AccessioniPrimary (citable) accession number: P25401
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: July 6, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.