Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi29R → A or G: Loss of chaperone activity, no interaction with PapG, no longer suppresses PapA P pilus subunit toxicity. 1 Publication1
Mutagenesisi133K → A: Loss of chaperone activity, no interaction with PapG. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Add BLAST21
ChainiPRO_000000928522 – 239Chaperone protein PapDAdd BLAST218

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 interactors.
MINTiMINT-101928.
STRINGi199310.c5185.

Structurei

Secondary structure

1239
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 26Combined sources4
Beta strandi28 – 33Combined sources6
Beta strandi36 – 45Combined sources10
Beta strandi48 – 50Combined sources3
Beta strandi52 – 59Combined sources8
Beta strandi68 – 74Combined sources7
Beta strandi76 – 80Combined sources5
Beta strandi85 – 92Combined sources8
Helixi94 – 98Combined sources5
Beta strandi101 – 103Combined sources3
Beta strandi105 – 114Combined sources10
Beta strandi123 – 137Combined sources15
Helixi139 – 141Combined sources3
Helixi150 – 152Combined sources3
Beta strandi154 – 158Combined sources5
Beta strandi161 – 166Combined sources6
Beta strandi168 – 170Combined sources3
Beta strandi172 – 180Combined sources9
Helixi181 – 186Combined sources6
Beta strandi192 – 194Combined sources3
Beta strandi198 – 203Combined sources6
Beta strandi211 – 215Combined sources5
Beta strandi223 – 229Combined sources7
Beta strandi232 – 235Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5K93X-ray2.70A/B22-237[»]
ProteinModelPortaliP15319.
SMRiP15319.
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)DescriptionActionsGraphical viewLength
Sequence conflicti81E → D no nucleotide entry (Ref. 2) Curated1

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
PDB 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[»]
5K93X-ray2.70A/B22-237[»]
ProteinModelPortaliP15319.
SMRiP15319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6196N.
IntActiP15319. 2 interactors.
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...

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: November 2, 2016
This is version 113 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.