PAPK_ECOLX
ID PAPK_ECOLX Reviewed; 178 AA.
AC P62532; P42190;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Fimbrial adapter PapK;
DE Flags: Precursor;
GN Name=papK;
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 FUNCTION.
RX PubMed=8096174; DOI=10.1002/j.1460-2075.1993.tb05724.x;
RA Jacob-Dubuisson F., Heuser J., Dodson K., Normark S., Hultgren S.;
RT "Initiation of assembly and association of the structural elements of a
RT bacterial pilus depend on two specialized tip proteins.";
RL EMBO J. 12:837-847(1993).
RN [3]
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE PAPD-PAPK COMPLEX.
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: Adapter that links the pilus rod to the base of the tip
CC fibrillum. Regulates the length of the tip fibrillum and joins it to
CC the pilus rod. Pili are polar filaments radiating from the surface of
CC the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300
CC per cell, and enable bacteria to colonize the epithelium of specific
CC host organs. {ECO:0000269|PubMed:8096174}.
CC -!- SUBCELLULAR LOCATION: Secreted. Fimbrium.
CC -!- MISCELLANEOUS: Strains of E.coli that cause infection of the human
CC urinary tract produce pap-pili which are hair-like appendages
CC consisting of about 1000 helically arranged subunits of the protein
CC PapA. These pili mediate binding to digalactoside-containing
CC glycolipids present on the epithelial cells which line the urinary
CC tract.
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DR EMBL; X61239; CAA43567.1; -; Genomic_DNA.
DR PIR; S25221; S16400.
DR RefSeq; WP_000597713.1; NZ_WWEL01000003.1.
DR PDB; 1PDK; X-ray; 2.40 A; B=22-178.
DR PDB; 7LHG; EM; 3.80 A; K=1-178.
DR PDB; 7LHH; EM; 7.20 A; K=1-178.
DR PDB; 7LHI; EM; 7.60 A; K=1-178.
DR PDBsum; 1PDK; -.
DR PDBsum; 7LHG; -.
DR PDBsum; 7LHH; -.
DR PDBsum; 7LHI; -.
DR AlphaFoldDB; P62532; -.
DR SMR; P62532; -.
DR DIP; DIP-60778N; -.
DR IntAct; P62532; 3.
DR EvolutionaryTrace; P62532; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR Gene3D; 2.60.40.1090; -; 1.
DR InterPro; IPR000259; Adhesion_dom_fimbrial.
DR InterPro; IPR036937; Adhesion_dom_fimbrial_sf.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR Pfam; PF00419; Fimbrial; 1.
DR SUPFAM; SSF49401; SSF49401; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fimbrium; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..178
FT /note="Fimbrial adapter PapK"
FT /id="PRO_0000022008"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1PDK"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:1PDK"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:1PDK"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1PDK"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:1PDK"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:1PDK"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1PDK"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:1PDK"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:1PDK"
FT STRAND 141..152
FT /evidence="ECO:0007829|PDB:1PDK"
FT HELIX 154..158
FT /evidence="ECO:0007829|PDB:1PDK"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:1PDK"
SQ SEQUENCE 178 AA; 18872 MW; DABF3054B87CA8CB CRC64;
MIKSTGALLL FAALSAGQAI ASDVAFRGNL LDRPCHVSGD SLNKHVVFKT RASRDFWYPP
GRSPTESFVI RLENCHATAV GKIVTLTFKG TEEAALPGHL KVTGVNAGRL GIALLDTDGS
SLLKPGTSHN KGQGEKVTGN SLELPFGAYV VATPEALRTK SVVPGDYEAT ATFELTYR
