Reviewed, UniProtKB/Swiss-Prot P15319 (PAPD_ECOLX)

Names and origin

Protein names

Recommended name:
    Chaperone protein papD

Gene names

Name:

papD

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	239 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Binds and caps interactive surfaces on pilus subunits to prevent them from participating in non-productive interactions. Facilitates the import of subunits into the periplasm. May facilitate subunit folding. Chaperone-subunit complexes are then targeted to the papC outer membrane usher where the chaperone must uncap from the subunits.
Subcellular location	Periplasm.
Miscellaneous	PapD donates its G1 beta strand to complete the Ig fold of papK (donor strand complementation).
Sequence similarities	Belongs to the periplasmic pilus chaperone family. Contains 1 Ig-like (immunoglobulin-like) domain.

Ontologies

Keywords
Biological process	Fimbrium biogenesis
Cellular component	Periplasm
Domain	Immunoglobulin domain Signal
Molecular function	Chaperone
PTM	Disulfide bond
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cellular cell wall organization Inferred from electronic annotation. Source: InterPro
Cellular component	outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Chain

22 – 239

218

Chaperone protein papD

PRO_0000009285

Amino acid modifications

Disulfide bond

228 ↔ 233

Experimental info

Sequence conflict

81

1

E → D Ref.2

Secondary structure

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239

Helix Strand Turn

Details...

Beta strand

26 – 33

8

Beta strand

36 – 45

10

Beta strand

52 – 60

9

Beta strand

65 – 74

10

Beta strand

76 – 80

5

Beta strand

85 – 92

8

Helix

94 – 98

5

Beta strand

101 – 103

3

Beta strand

105 – 114

10

Beta strand

119 – 137

19

Helix

139 – 141

3

Helix

149 – 152

4

Beta strand

154 – 158

5

Beta strand

161 – 166

6

Beta strand

168 – 170

3

Beta strand

172 – 180

9

Helix

181 – 186

6

Beta strand

192 – 194

3

Beta strand

198 – 203

6

Beta strand

211 – 215

5

Beta strand

223 – 229

7

Beta strand

232 – 235

4

Sequences

	Sequence		Length	Mass (Da)
	P15319-1 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: D8AAEA2B346D7268	FASTA	239	26,803
	10 20 30 40 50 60 MIRKKILMAA IPLFVISGAD AAVSLDRTRA VFDGSEKSMT LDISNDNKQL PYLAQAWIEN 70 80 90 100 110 120 ENQEKIITGP VIATPPVQRL EPGAKSMVRL STTPDISKLP QDRESLFYFN LREIPPRSEK 130 140 150 160 170 180 ANVLQIALQT KIKLFYRPAA IKTRPNEVWQ DQLILNKVSG GYRIENPTPY YVTVIGLGGS 190 200 210 220 230 EKQAEEGEFE TVMLSPRSEQ TVKSANYNTP YLSYINDYGG RPVLSFICNG SRCSVKKEK

References

[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: 1357526] [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]	"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: 10049807] [Abstract] Cited for: REVIEW.
[4]	"Crystal structure of chaperone protein PapD reveals an immunoglobulin fold." Holmgren A., Braenden C.-I. Nature 342:248-251(1989) [PubMed: 2478891] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[5]	"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: 10446050] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE PAPD-PAPK COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X61239 Genomic DNA. Translation: CAA43565.1.

PIR

A33491.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N0L	X-ray	2.30	A/C	22-239	[»]
1PDK	X-ray	2.40	A	22-239	[»]
1QPP	X-ray	2.60	A/B	22-239	[»]
1QPX	X-ray	2.40	A/B	22-239	[»]
2J2Z	X-ray	2.30	A	22-239	[»]
2J7L	X-ray	2.60	A	22-239	[»]
2UY6	X-ray	2.50	A	22-239	[»]
2UY7	X-ray	2.60	A/C/E/G	22-239	[»]
2W07	X-ray	2.20	A	22-239	[»]
3DPA	X-ray	2.50	A	22-239	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6196N.

Family and domain databases

InterPro

IPR008962. PapD-like.
IPR001829. Pili_assmbl_chaperone_bac.
IPR016148. Pili_assmbl_chaperone_C_bac.
IPR018046. Pili_assmbl_chaperone_CS.
IPR016147. Pili_assmbl_chaperone_N_bac.
[Graphical view]

Gene3D

G3DSA:2.60.40.360. MSP. 1 hit.
G3DSA:2.60.40.1070. Pili_chaperone. 1 hit.

Pfam

PF02753. Pili_assembly_C. 1 hit.
PF00345. Pili_assembly_N. 1 hit.
[Graphical view]

PRINTS

PR00969. CHAPERONPILI.

PROSITE

PS00635. PILI_CHAPERONE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PAPD_ECOLX

Accession

Primary (citable) accession number: P15319

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	November 1, 1995
Last modified:	January 19, 2010
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)