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Protein

Chaperone protein PapD

Gene

papD

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds and caps interactive surfaces on P pilus subunits to prevent them from participating in non-productive interactions. Facilitates the import of P pilus subunits into the periplasm, probably also facilitates their folding (PubMed:9351822). Chaperone-subunit complexes are then targeted to the PapC outer membrane usher where the chaperone must uncap from the subunits. Coexpression of this chaperone with individual, otherwise toxic, P pilus subunits (tested with PapA, PapE and PapG) suppresses their growth inhibitory phenotype (PubMed:9351822).1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Fimbrium biogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Chaperone protein PapD
Gene namesi
Name:papD
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi29 – 291R → A or G: Loss of chaperone activity, no interaction with PapG, no longer suppresses PapA P pilus subunit toxicity. 1 Publication
Mutagenesisi133 – 1331K → A: Loss of chaperone activity, no interaction with PapG. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Chaini22 – 239218Chaperone protein PapDPRO_0000009285Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi228 ↔ 233

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Interacts with substrates PapG and PapK.2 Publications

Protein-protein interaction databases

DIPiDIP-6196N.
IntActiP15319. 2 interactions.
MINTiMINT-101928.
STRINGi199310.c5185.

Structurei

Secondary structure

1
239
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 264Combined sources
Beta strandi28 – 336Combined sources
Beta strandi36 – 4510Combined sources
Beta strandi48 – 503Combined sources
Beta strandi52 – 598Combined sources
Beta strandi68 – 747Combined sources
Beta strandi76 – 805Combined sources
Beta strandi85 – 928Combined sources
Helixi94 – 985Combined sources
Beta strandi101 – 1033Combined sources
Beta strandi105 – 11410Combined sources
Beta strandi123 – 13715Combined sources
Helixi139 – 1413Combined sources
Helixi150 – 1523Combined sources
Beta strandi154 – 1585Combined sources
Beta strandi161 – 1666Combined sources
Beta strandi168 – 1703Combined sources
Beta strandi172 – 1809Combined sources
Helixi181 – 1866Combined sources
Beta strandi192 – 1943Combined sources
Beta strandi198 – 2036Combined sources
Beta strandi211 – 2155Combined sources
Beta strandi223 – 2297Combined sources
Beta strandi232 – 2354Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N0LX-ray2.30A/C22-239[»]
1PDKX-ray2.40A22-239[»]
1QPPX-ray2.60A/B22-239[»]
1QPXX-ray2.40A/B22-239[»]
2J2ZX-ray2.30A22-239[»]
2J7LX-ray2.60A22-239[»]
2UY6X-ray2.50A22-239[»]
2UY7X-ray2.60A/C/E/G22-239[»]
2W07X-ray2.20A22-239[»]
2WMPX-ray2.30A22-239[»]
2XG4X-ray2.40A22-239[»]
2XG5X-ray2.00A22-239[»]
3DPAX-ray2.50A22-239[»]
3ME0X-ray2.03A22-239[»]
ProteinModelPortaliP15319.
SMRiP15319. Positions 22-237.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15319.

Family & Domainsi

Sequence similaritiesi

Belongs to the periplasmic pilus chaperone family.Curated

Keywords - Domaini

Immunoglobulin domain, Signal

Phylogenomic databases

eggNOGiENOG4106P2F. Bacteria.
COG3121. LUCA.

Family and domain databases

Gene3Di2.60.40.1070. 1 hit.
2.60.40.360. 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]
PfamiPF02753. PapD_C. 1 hit.
PF00345. 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.

P15319-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRKKILMAA IPLFVISGAD AAVSLDRTRA VFDGSEKSMT LDISNDNKQL
60 70 80 90 100
PYLAQAWIEN ENQEKIITGP VIATPPVQRL EPGAKSMVRL STTPDISKLP
110 120 130 140 150
QDRESLFYFN LREIPPRSEK ANVLQIALQT KIKLFYRPAA IKTRPNEVWQ
160 170 180 190 200
DQLILNKVSG GYRIENPTPY YVTVIGLGGS EKQAEEGEFE TVMLSPRSEQ
210 220 230
TVKSANYNTP YLSYINDYGG RPVLSFICNG SRCSVKKEK
Length:239
Mass (Da):26,803
Last modified:November 1, 1995 - v2
Checksum:iD8AAEA2B346D7268
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811E → D no nucleotide entry (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61239 Genomic DNA. Translation: CAA43565.1.
PIRiA33491.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61239 Genomic DNA. Translation: CAA43565.1.
PIRiA33491.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N0LX-ray2.30A/C22-239[»]
1PDKX-ray2.40A22-239[»]
1QPPX-ray2.60A/B22-239[»]
1QPXX-ray2.40A/B22-239[»]
2J2ZX-ray2.30A22-239[»]
2J7LX-ray2.60A22-239[»]
2UY6X-ray2.50A22-239[»]
2UY7X-ray2.60A/C/E/G22-239[»]
2W07X-ray2.20A22-239[»]
2WMPX-ray2.30A22-239[»]
2XG4X-ray2.40A22-239[»]
2XG5X-ray2.00A22-239[»]
3DPAX-ray2.50A22-239[»]
3ME0X-ray2.03A22-239[»]
ProteinModelPortaliP15319.
SMRiP15319. Positions 22-237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6196N.
IntActiP15319. 2 interactions.
MINTiMINT-101928.
STRINGi199310.c5185.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4106P2F. Bacteria.
COG3121. LUCA.

Miscellaneous databases

EvolutionaryTraceiP15319.

Family and domain databases

Gene3Di2.60.40.1070. 1 hit.
2.60.40.360. 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]
PfamiPF02753. PapD_C. 1 hit.
PF00345. 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. "Horizontal gene transfer of the Escherichia coli pap and prs pili operons as a mechanism for the development of tissue-specific adhesive properties."
    Marklund B.-I., Tennent J.M., Garcia E., Hamers A., Baga M., Lindberg F., Gaastra W., Normark S.
    Mol. Microbiol. 6:2225-2242(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 700336 / J96.
  2. Lindberg F.
    Thesis (1987), University of Umea, Sweden
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems."
    Jones C.H., Danese P.N., Pinkner J.S., Silhavy T.J., Hultgren S.J.
    EMBO J. 16:6394-6406(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-29 AND LYS-133.
  4. "Pilus biogenesis via the chaperone/usher pathway: an integration of structure and function."
    Hung D.L., Hultgren S.J.
    J. Struct. Biol. 124:201-220(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  5. "Crystal structure of chaperone protein PapD reveals an immunoglobulin fold."
    Holmgren A., Braenden C.-I.
    Nature 342:248-251(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-239.
  6. "Structural basis of chaperone function and pilus biogenesis."
    Sauer F.G., Fuetterer K., Pinkner J.S., Dodson K.W., Hultgren S.J., Waksman G.
    Science 285:1058-1061(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 22-239 IN THE PAPD-PAPK COMPLEX, SUBUNIT.

Entry informationi

Entry nameiPAPD_ECOLX
AccessioniPrimary (citable) accession number: P15319
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

PapD donates its G1 beta strand to complete the Ig fold of PapK (donor strand complementation).1 Publication

Keywords - Technical termi

3D-structure

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.