ID   PMFA_PROMH              Reviewed;         184 AA.
AC   Q04681; B4F036;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Major fimbrial subunit;
DE   Flags: Precursor;
GN   Name=pmfA; OrderedLocusNames=PMI1877;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-42.
RX   PubMed=8094384; DOI=10.1128/iai.61.3.884-891.1993;
RA   Bahrani F.K., Cook S., Hull R.A., Massad G., Mobley H.L.T.;
RT   "Proteus mirabilis fimbriae: N-terminal amino acid sequence of a major
RT   fimbrial subunit and nucleotide sequences of the genes from two strains.";
RL   Infect. Immun. 61:884-891(1993).
RN   [2]
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   [3]
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: Major structural component of PMF fimbriae.
CC   -!- SUBCELLULAR LOCATION: Fimbrium.
CC   -!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
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DR   EMBL; Z19553; CAA79612.1; -; Genomic_DNA.
DR   EMBL; Z35428; CAA84589.1; -; Genomic_DNA.
DR   EMBL; AM942759; CAR43895.1; -; Genomic_DNA.
DR   PIR; B49239; B49239.
DR   RefSeq; WP_004243875.1; NC_010554.1.
DR   AlphaFoldDB; Q04681; -.
DR   SMR; Q04681; -.
DR   STRING; 529507.PMI1877; -.
DR   DNASU; 6802017; -.
DR   EnsemblBacteria; CAR43895; CAR43895; PMI1877.
DR   GeneID; 6802017; -.
DR   KEGG; pmr:PMI1877; -.
DR   eggNOG; COG3539; Bacteria.
DR   HOGENOM; CLU_088965_3_4_6; -.
DR   OMA; TIPFVAY; -.
DR   Proteomes; UP000008319; Chromosome.
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   Direct protein sequencing; Disulfide bond; Fimbrium; Reference proteome;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:8094384"
FT   CHAIN           23..184
FT                   /note="Major fimbrial subunit"
FT                   /id="PRO_0000009232"
FT   DISULFID        49..88
FT                   /evidence="ECO:0000250"
FT   VARIANT         73
FT                   /note="L -> Q (in strain: HU1069)"
SQ   SEQUENCE   184 AA;  18922 MW;  C26B8B9B46F4663B CRC64;
     MKLSKIALAA ALVFGINSVA TAENETPAPK VSSTKGEIQL KGEIVNSACG LAASSSPVIV
     DFSEIPTSAL ANLQKAGNIK KDIELQDCDT TVAKTATVSY TPSVVNAVNK DLASFVSGNA
     SGAGIGLMDA GSKAVKWNTA TTPVQLINGV SKIPFVAYVQ AESADAKVTP GEFQAVINFQ
     VDYQ