PAPD_ECOLX
ID PAPD_ECOLX Reviewed; 239 AA.
AC P15319;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Chaperone protein PapD;
DE Flags: Precursor;
GN Name=papD;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700336 / J96 / UPEC;
RX PubMed=1357526; DOI=10.1111/j.1365-2958.1992.tb01399.x;
RA Marklund B.-I., Tennent J.M., Garcia E., Hamers A., Baga M., Lindberg F.,
RA Gaastra W., Normark S.;
RT "Horizontal gene transfer of the Escherichia coli pap and prs pili operons
RT as a mechanism for the development of tissue-specific adhesive
RT properties.";
RL Mol. Microbiol. 6:2225-2242(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lindberg F.;
RL Thesis (1987), University of Umea, Sweden.
RN [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-29 AND
RP LYS-133.
RX PubMed=9351822; DOI=10.1093/emboj/16.21.6394;
RA Jones C.H., Danese P.N., Pinkner J.S., Silhavy T.J., Hultgren S.J.;
RT "The chaperone-assisted membrane release and folding pathway is sensed by
RT two signal transduction systems.";
RL EMBO J. 16:6394-6406(1997).
RN [4]
RP REVIEW.
RX PubMed=10049807; DOI=10.1006/jsbi.1998.4049;
RA Hung D.L., Hultgren S.J.;
RT "Pilus biogenesis via the chaperone/usher pathway: an integration of
RT structure and function.";
RL J. Struct. Biol. 124:201-220(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-239.
RX PubMed=2478891; DOI=10.1038/342248a0;
RA Holmgren A., Braenden C.-I.;
RT "Crystal structure of chaperone protein PapD reveals an immunoglobulin
RT fold.";
RL Nature 342:248-251(1989).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 22-239 IN THE PAPD-PAPK COMPLEX,
RP AND SUBUNIT.
RX PubMed=10446050; DOI=10.1126/science.285.5430.1058;
RA Sauer F.G., Fuetterer K., Pinkner J.S., Dodson K.W., Hultgren S.J.,
RA Waksman G.;
RT "Structural basis of chaperone function and pilus biogenesis.";
RL Science 285:1058-1061(1999).
CC -!- FUNCTION: Binds and caps interactive surfaces on P pilus subunits to
CC prevent them from participating in non-productive interactions.
CC Facilitates the import of P pilus subunits into the periplasm, probably
CC also facilitates their folding (PubMed:9351822). Chaperone-subunit
CC complexes are then targeted to the PapC outer membrane usher where the
CC chaperone must uncap from the subunits. Coexpression of this chaperone
CC with individual, otherwise toxic, P pilus subunits (tested with PapA,
CC PapE and PapG) suppresses their growth inhibitory phenotype
CC (PubMed:9351822). {ECO:0000269|PubMed:9351822}.
CC -!- SUBUNIT: Interacts with substrates PapG and PapK.
CC {ECO:0000269|PubMed:10446050, ECO:0000269|PubMed:9351822}.
CC -!- INTERACTION:
CC P15319; P08407: papE; NbExp=2; IntAct=EBI-1034993, EBI-1034986;
CC P15319; P08408: papF; NbExp=5; IntAct=EBI-1034993, EBI-15725486;
CC P15319; P13720: papGI; NbExp=2; IntAct=EBI-1034993, EBI-15725472;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:9351822}.
CC -!- MISCELLANEOUS: PapD donates its G1 beta strand to complete the Ig fold
CC of PapK (donor strand complementation). {ECO:0000269|PubMed:2478891}.
CC -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC {ECO:0000305}.
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DR EMBL; X61239; CAA43565.1; -; Genomic_DNA.
DR PIR; A33491; A33491.
DR RefSeq; WP_001363619.1; NZ_VJVB01000041.1.
DR PDB; 1N0L; X-ray; 2.30 A; A/C=22-239.
DR PDB; 1PDK; X-ray; 2.40 A; A=22-239.
DR PDB; 1QPP; X-ray; 2.60 A; A/B=22-239.
DR PDB; 1QPX; X-ray; 2.40 A; A/B=22-239.
DR PDB; 2J2Z; X-ray; 2.30 A; A=22-239.
DR PDB; 2J7L; X-ray; 2.60 A; A=22-239.
DR PDB; 2UY6; X-ray; 2.50 A; A=22-239.
DR PDB; 2UY7; X-ray; 2.60 A; A/C/E/G=22-239.
DR PDB; 2W07; X-ray; 2.20 A; A=22-239.
DR PDB; 2WMP; X-ray; 2.30 A; A=22-239.
DR PDB; 2XG4; X-ray; 2.40 A; A=22-239.
DR PDB; 2XG5; X-ray; 2.00 A; A=22-239.
DR PDB; 3DPA; X-ray; 2.50 A; A=22-239.
DR PDB; 3ME0; X-ray; 2.03 A; A=22-239.
DR PDB; 5K93; X-ray; 2.70 A; A/B=22-237.
DR PDB; 6CD2; X-ray; 3.70 A; A=22-236.
DR PDB; 7LHG; EM; 3.80 A; D=1-239.
DR PDB; 7LHH; EM; 7.20 A; D=22-239.
DR PDB; 7LHI; EM; 7.60 A; D=22-239.
DR PDBsum; 1N0L; -.
DR PDBsum; 1PDK; -.
DR PDBsum; 1QPP; -.
DR PDBsum; 1QPX; -.
DR PDBsum; 2J2Z; -.
DR PDBsum; 2J7L; -.
DR PDBsum; 2UY6; -.
DR PDBsum; 2UY7; -.
DR PDBsum; 2W07; -.
DR PDBsum; 2WMP; -.
DR PDBsum; 2XG4; -.
DR PDBsum; 2XG5; -.
DR PDBsum; 3DPA; -.
DR PDBsum; 3ME0; -.
DR PDBsum; 5K93; -.
DR PDBsum; 6CD2; -.
DR PDBsum; 7LHG; -.
DR PDBsum; 7LHH; -.
DR PDBsum; 7LHI; -.
DR AlphaFoldDB; P15319; -.
DR SMR; P15319; -.
DR DIP; DIP-6196N; -.
DR IntAct; P15319; 7.
DR MINT; P15319; -.
DR BindingDB; P15319; -.
DR ChEMBL; CHEMBL3309037; -.
DR OMA; DSEFNAV; -.
DR EvolutionaryTrace; P15319; -.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008962; PapD-like_sf.
DR InterPro; IPR036316; Pili_assmbl_chap_C_dom_sf.
DR InterPro; IPR001829; Pili_assmbl_chaperone_bac.
DR InterPro; IPR016148; Pili_assmbl_chaperone_C.
DR InterPro; IPR018046; Pili_assmbl_chaperone_CS.
DR InterPro; IPR016147; Pili_assmbl_chaperone_N.
DR Pfam; PF02753; PapD_C; 1.
DR Pfam; PF00345; PapD_N; 1.
DR PRINTS; PR00969; CHAPERONPILI.
DR SUPFAM; SSF49354; SSF49354; 1.
DR SUPFAM; SSF49584; SSF49584; 1.
DR PROSITE; PS00635; PILI_CHAPERONE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Disulfide bond; Fimbrium biogenesis;
KW Immunoglobulin domain; Periplasm; Signal.
FT SIGNAL 1..21
FT CHAIN 22..239
FT /note="Chaperone protein PapD"
FT /id="PRO_0000009285"
FT DISULFID 228..233
FT MUTAGEN 29
FT /note="R->A,G: Loss of chaperone activity, no interaction
FT with PapG, no longer suppresses PapA P pilus subunit
FT toxicity."
FT /evidence="ECO:0000269|PubMed:9351822"
FT MUTAGEN 133
FT /note="K->A: Loss of chaperone activity, no interaction
FT with PapG."
FT /evidence="ECO:0000269|PubMed:9351822"
FT CONFLICT 81
FT /note="E -> D (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:2XG5"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 123..137
FT /evidence="ECO:0007829|PDB:2XG5"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:2XG5"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:2XG5"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:2XG5"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:2XG5"
SQ SEQUENCE 239 AA; 26803 MW; D8AAEA2B346D7268 CRC64;
MIRKKILMAA IPLFVISGAD AAVSLDRTRA VFDGSEKSMT LDISNDNKQL PYLAQAWIEN
ENQEKIITGP VIATPPVQRL EPGAKSMVRL STTPDISKLP QDRESLFYFN LREIPPRSEK
ANVLQIALQT KIKLFYRPAA IKTRPNEVWQ DQLILNKVSG GYRIENPTPY YVTVIGLGGS
EKQAEEGEFE TVMLSPRSEQ TVKSANYNTP YLSYINDYGG RPVLSFICNG SRCSVKKEK
