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PAPH_ECOLX
ID   PAPH_ECOLX              Reviewed;         195 AA.
AC   P07111;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=PAP fimbrial minor pilin protein;
DE   Flags: Precursor;
GN   Name=papH;
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=2882856; DOI=10.1016/0092-8674(87)90565-4;
RA   Baga M., Norgren M., Normark S.;
RT   "Biogenesis of E. coli Pap pili: papH, a minor pilin subunit involved in
RT   cell anchoring and length modulation.";
RL   Cell 49:241-251(1987).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-195.
RC   STRAIN=ATCC 700336 / J96 / UPEC;
RX   PubMed=2897064; DOI=10.1111/j.1365-2958.1987.tb00509.x;
RA   Norgren M., Baga M., Tennent J.M., Normark S.;
RT   "Nucleotide sequence, regulation and functional analysis of the papC gene
RT   required for cell surface localization of Pap pili of uropathogenic
RT   Escherichia coli.";
RL   Mol. Microbiol. 1:169-178(1987).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-195, AND DISULFIDE BOND.
RX   PubMed=17082819; DOI=10.1038/sj.embor.7400833;
RA   Verger D., Miller E., Remaut H., Waksman G., Hultgren S.;
RT   "Molecular mechanism of P pilus termination in uropathogenic Escherichia
RT   coli.";
RL   EMBO Rep. 7:1228-1232(2006).
CC   -!- FUNCTION: Fimbriae (also called pili), polar filaments radiating from
CC       the surface of the bacterium to a length of 0.5-1.5 micrometers and
CC       numbering 100-300 per cell, enable bacteria to colonize the epithelium
CC       of specific host organs.
CC   -!- FUNCTION: PapH seems to anchor the pilus to the bacterial cell. In
CC       addition the stoichiometric relationship between PapH and PapA
CC       determines the pilus length.
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; Y00529; CAA68587.1; -; Genomic_DNA.
DR   EMBL; M16202; AAA24286.1; -; Genomic_DNA.
DR   EMBL; X61239; CAA43563.1; -; Genomic_DNA.
DR   PIR; A27021; YQECPH.
DR   RefSeq; WP_001239368.1; NZ_VOHF01000048.1.
DR   PDB; 2J2Z; X-ray; 2.30 A; B=23-195.
DR   PDB; 2XG4; X-ray; 2.40 A; B=23-195.
DR   PDB; 2XG5; X-ray; 2.00 A; B=23-195.
DR   PDBsum; 2J2Z; -.
DR   PDBsum; 2XG4; -.
DR   PDBsum; 2XG5; -.
DR   AlphaFoldDB; P07111; -.
DR   SMR; P07111; -.
DR   DIP; DIP-44596N; -.
DR   IntAct; P07111; 3.
DR   MINT; P07111; -.
DR   EvolutionaryTrace; P07111; -.
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; IPR036937; Adhesion_dom_fimbrial_sf.
DR   InterPro; IPR008966; Adhesion_dom_sf.
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..195
FT                   /note="PAP fimbrial minor pilin protein"
FT                   /id="PRO_0000009198"
FT   DISULFID        58..97
FT                   /evidence="ECO:0000269|PubMed:17082819"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:2XG5"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:2XG5"
FT   HELIX           76..80
FT                   /evidence="ECO:0007829|PDB:2XG5"
FT   STRAND          88..97
FT                   /evidence="ECO:0007829|PDB:2XG5"
FT   TURN            106..110
FT                   /evidence="ECO:0007829|PDB:2XG5"
FT   STRAND          111..118
FT                   /evidence="ECO:0007829|PDB:2XG5"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:2J2Z"
FT   STRAND          134..142
FT                   /evidence="ECO:0007829|PDB:2XG5"
FT   STRAND          165..174
FT                   /evidence="ECO:0007829|PDB:2XG5"
FT   STRAND          187..194
FT                   /evidence="ECO:0007829|PDB:2XG5"
SQ   SEQUENCE   195 AA;  21835 MW;  D2120FC5DA063169 CRC64;
     MRLRFSVPLF FFGCVFVHGV FAGPFPPPGM SLPEYWGEEH VWWDGRAAFH GEVVRPACTL
     AMEDAWQIID MGETPVRDLQ NGFSGPERKF SLRLRNCEFN SQGGNLFSDS RIRVTFDGVR
     GETPDKFNLS GQAKGINLQI ADVRGNIARA GKVMPAIPLT GNEEALDYTL RIVRNGKKLE
     AGNYFAVLGF RVDYE
 
 
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