PRSH_ECOLX
ID PRSH_ECOLX Reviewed; 195 AA.
AC P42185;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=PRS fimbrial minor pilin protein;
DE Flags: Precursor;
GN Name=prsH;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1442;
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).
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: Seems to anchor the pilus to the bacterial cell. In addition
CC the stoichiometric relationship between PrsH and PrsA determines the
CC pilus length.
CC -!- SUBCELLULAR LOCATION: Secreted. Fimbrium.
CC -!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X62157; CAA44082.1; -; Genomic_DNA.
DR PIR; S25205; S25205.
DR RefSeq; WP_021528975.1; NZ_UCUV01000013.1.
DR AlphaFoldDB; P42185; -.
DR SMR; P42185; -.
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 3: Inferred from homology;
KW Disulfide bond; Fimbrium; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..195
FT /note="PRS fimbrial minor pilin protein"
FT /id="PRO_0000009199"
FT DISULFID 58..97
FT /evidence="ECO:0000305"
SQ SEQUENCE 195 AA; 21837 MW; A5065E8F93D5861B CRC64;
MRLRFSVPLF FFGCVFVHGV FAGPFPPPGM SLPEYWGEEH VWWDGRATFH GEVVRPACTL
AMEDAWQIID MGETPVRDLQ NGFSGPERKF SLRLRNCEFN SQGGNLFSDS RIRVTFDGVR
GETPDKFNLS GQAKGINLQI ADARGNIARA GKVMPAIPLT GNEEALDYTL RIVRNGKKLE
AGNYFAVLGF RVDYE