ID   PAPA_ECOLX              Reviewed;         185 AA.
AC   P04127;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1986, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Pap fimbrial major pilin protein;
DE            Short=Pap pili;
DE   Flags: Precursor;
GN   Name=papA;
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=6140260; DOI=10.1128/jb.157.1.330-333.1984;
RA   Baga M., Normark S., Hardy J., O'Hanley P., Lark D., Olsson O.,
RA   Schoolnik G., Falkow S.;
RT   "Nucleotide sequence of the papA gene encoding the Pap pilus subunit of
RT   human uropathogenic Escherichia coli.";
RL   J. Bacteriol. 157:330-333(1984).
RN   [2]
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   [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 (2.5 ANGSTROMS) OF 23-185 IN COMPLEX WITH PAPD, AND
RP   DISULFIDE BOND.
RX   PubMed=17511517; DOI=10.1371/journal.ppat.0030073;
RA   Verger D., Bullitt E., Hultgren S.J., Waksman G.;
RT   "Crystal structure of the P pilus rod subunit PapA.";
RL   PLoS Pathog. 3:674-682(2007).
CC   -!- FUNCTION: Polymerizes to form the thick (6.8 nm in diameter) rod of the
CC       pilus (also called fimbria). The rod is a right-handed helical cylinder
CC       with 3.28 PapA subunits per turn. Pili are polar filaments radiating
CC       from the surface of the bacterium to a length of 0.5-1.5 micrometers
CC       and numbering 100-300 per cell, and enable bacteria to colonize the
CC       epithelium of specific host organs.
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.
CC   -!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
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DR   EMBL; X03391; CAA27126.1; -; Genomic_DNA.
DR   EMBL; X61239; CAA43562.1; -; Genomic_DNA.
DR   PIR; A23221; YQECPP.
DR   PDB; 2UY6; X-ray; 2.50 A; B/C=23-185.
DR   PDB; 2UY7; X-ray; 2.60 A; B/D/F/H=23-185.
DR   PDB; 5FLU; EM; 3.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M=23-185.
DR   PDBsum; 2UY6; -.
DR   PDBsum; 2UY7; -.
DR   PDBsum; 5FLU; -.
DR   AlphaFoldDB; P04127; -.
DR   SMR; P04127; -.
DR   DIP; DIP-44594N; -.
DR   IntAct; P04127; 4.
DR   MINT; P04127; -.
DR   EvolutionaryTrace; P04127; -.
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; Disulfide bond; Fimbrium; Secreted; Signal.
FT   SIGNAL          1..22
FT   CHAIN           23..185
FT                   /note="Pap fimbrial major pilin protein"
FT                   /id="PRO_0000009197"
FT   DISULFID        44..83
FT                   /evidence="ECO:0000269|PubMed:17511517"
FT   STRAND          33..40
FT                   /evidence="ECO:0007829|PDB:2UY6"
FT   STRAND          45..47
FT                   /evidence="ECO:0007829|PDB:2UY6"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:2UY6"
FT   HELIX           62..67
FT                   /evidence="ECO:0007829|PDB:2UY6"
FT   STRAND          74..83
FT                   /evidence="ECO:0007829|PDB:2UY6"
FT   STRAND          98..104
FT                   /evidence="ECO:0007829|PDB:2UY6"
FT   STRAND          111..116
FT                   /evidence="ECO:0007829|PDB:2UY6"
FT   STRAND          118..121
FT                   /evidence="ECO:0007829|PDB:2UY6"
FT   STRAND          123..128
FT                   /evidence="ECO:0007829|PDB:2UY6"
FT   STRAND          130..133
FT                   /evidence="ECO:0007829|PDB:2UY6"
FT   STRAND          137..140
FT                   /evidence="ECO:0007829|PDB:2UY6"
FT   STRAND          152..161
FT                   /evidence="ECO:0007829|PDB:2UY6"
FT   STRAND          175..184
FT                   /evidence="ECO:0007829|PDB:2UY6"
SQ   SEQUENCE   185 AA;  18686 MW;  93DB4FFDA211C671 CRC64;
     MIKSVIAGAV AMAVVSFGVN NAAPTIPQGQ GKVTFNGTVV DAPCSISQKS ADQSIDFGQL
     SKSFLEAGGV SKPMDLDIEL VNCDITAFKG GNGAKKGTVK LAFTGPIVNG HSDELDTNGG
     TGTAIVVQGA GKNVVFDGSE GDANTLKDGE NVLHYTAVVK KSSAVGAAVT EGAFSAVANF
     NLTYQ