ID   PMFD_PROMH              Reviewed;         254 AA.
AC   P53520; B4F038;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Chaperone protein PmfD;
DE   Flags: Precursor;
GN   Name=pmfD; OrderedLocusNames=PMI1879;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7959033; DOI=10.1016/0378-1119(94)90866-4;
RA   Massad G., Mobley H.L.T.;
RT   "Genetic organization and complete sequence of the Proteus mirabilis pmf
RT   fimbrial operon.";
RL   Gene 150:101-104(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
CC   -!- FUNCTION: Involved in the biogenesis of the PMF fimbria.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC       {ECO:0000305}.
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DR   EMBL; Z35428; CAA84591.1; -; Genomic_DNA.
DR   EMBL; AM942759; CAR43898.1; -; Genomic_DNA.
DR   RefSeq; WP_004243877.1; NC_010554.1.
DR   AlphaFoldDB; P53520; -.
DR   SMR; P53520; -.
DR   STRING; 529507.PMI1879; -.
DR   PRIDE; P53520; -.
DR   EnsemblBacteria; CAR43898; CAR43898; PMI1879.
DR   GeneID; 6802209; -.
DR   KEGG; pmr:PMI1879; -.
DR   eggNOG; COG3121; Bacteria.
DR   HOGENOM; CLU_070768_5_1_6; -.
DR   OMA; DYGGHPE; -.
DR   Proteomes; UP000008319; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008962; PapD-like_sf.
DR   InterPro; IPR036316; Pili_assmbl_chap_C_dom_sf.
DR   InterPro; IPR001829; Pili_assmbl_chaperone_bac.
DR   InterPro; IPR016148; Pili_assmbl_chaperone_C.
DR   InterPro; IPR018046; Pili_assmbl_chaperone_CS.
DR   InterPro; IPR016147; Pili_assmbl_chaperone_N.
DR   Pfam; PF02753; PapD_C; 1.
DR   Pfam; PF00345; PapD_N; 1.
DR   PRINTS; PR00969; CHAPERONPILI.
DR   SUPFAM; SSF49354; SSF49354; 1.
DR   SUPFAM; SSF49584; SSF49584; 1.
DR   PROSITE; PS00635; PILI_CHAPERONE; 1.
PE   3: Inferred from homology;
KW   Chaperone; Fimbrium biogenesis; Immunoglobulin domain; Periplasm;
KW   Reference proteome; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..254
FT                   /note="Chaperone protein PmfD"
FT                   /id="PRO_0000009286"
SQ   SEQUENCE   254 AA;  28209 MW;  B1A5684115F83216 CRC64;
     MNSFSTLKTL FCGSLLALSL VNTTQAGVSL DRTRIVLTGN ENSASVNLKN TSPDIPFLAQ
     SWVENENGQK ISSPLVALPP LQRLDGAQKG VVRITKTAEV GLLPQDRESL FYLNVREIPP
     APKQANVLQM AMQSRIKLFY RPSAIVPEKP GMVWQDQLVF KKQGNKFIVN NPTPYYITII
     SLSNKLNGED SDKLTTFPGL MVAPKASLDI PVKTSNVNQF YMMYVNDYGG HPELKFVCQQ
     DSCKVAPKDQ QPKY