PRSD_ECOLX
ID PRSD_ECOLX Reviewed; 115 AA.
AC P42183;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Chaperone protein PrsD;
DE Flags: Fragment;
GN Name=prsD;
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: Mediates assembly of pili by forming soluble multimeric
CC complexes with pili subunits as an intermediate step in the assembly
CC process.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC {ECO:0000305}.
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DR EMBL; X62158; CAA44084.1; -; Genomic_DNA.
DR PIR; S25207; S25207.
DR AlphaFoldDB; P42183; -.
DR SMR; P42183; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR036316; Pili_assmbl_chap_C_dom_sf.
DR InterPro; IPR016148; Pili_assmbl_chaperone_C.
DR Pfam; PF02753; PapD_C; 1.
DR SUPFAM; SSF49584; SSF49584; 1.
PE 3: Inferred from homology;
KW Chaperone; Fimbrium biogenesis; Immunoglobulin domain; Periplasm.
FT CHAIN <1..115
FT /note="Chaperone protein PrsD"
FT /id="PRO_0000208270"
FT NON_TER 1
SQ SEQUENCE 115 AA; 13080 MW; 38EF5F5A33B05B6D CRC64;
LQIALQTKIK LFYRPAAIKT RPNEVWQDQL ILNKVSGGYR IENPTPYYVT VIGLGGSEKQ
AEEGEFETVM LSPRSEQTVN RNYNTPYLSY INDYGGRPVL SFICNGSRCS VKKEK