ID   MRKD_KLEPN              Reviewed;         321 AA.
AC   P21648;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Fimbria adhesin protein;
DE   Flags: Precursor;
GN   Name=mrkD;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IA565;
RX   PubMed=1670938; DOI=10.1128/jb.173.2.916-920.1991;
RA   Allen B.L., Gerlach G.-F., Clegg S.;
RT   "Nucleotide sequence and functions of mrk determinants necessary for
RT   expression of type 3 fimbriae in Klebsiella pneumoniae.";
RL   J. Bacteriol. 173:916-920(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2563996; DOI=10.1128/jb.171.3.1262-1270.1989;
RA   Gerlach G.-F., Clegg S., Allen B.L.;
RT   "Identification and characterization of the genes encoding the type 3 and
RT   type 1 fimbrial adhesins of Klebsiella pneumoniae.";
RL   J. Bacteriol. 171:1262-1270(1989).
CC   -!- SUBCELLULAR LOCATION: Fimbrium.
CC   -!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
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DR   EMBL; M55912; AAA25096.1; -; Genomic_DNA.
DR   EMBL; M24536; AAA25098.1; -; Genomic_DNA.
DR   PIR; B32801; B32801.
DR   PDB; 3U4K; X-ray; 3.00 A; A=21-181.
DR   PDBsum; 3U4K; -.
DR   AlphaFoldDB; P21648; -.
DR   SMR; P21648; -.
DR   PRIDE; P21648; -.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Fimbrium; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           19..321
FT                   /note="Fimbria adhesin protein"
FT                   /id="PRO_0000009230"
FT   CONFLICT        113
FT                   /note="Y -> V (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   STRAND          22..26
FT                   /evidence="ECO:0007829|PDB:3U4K"
FT   STRAND          29..32
FT                   /evidence="ECO:0007829|PDB:3U4K"
FT   STRAND          36..39
FT                   /evidence="ECO:0007829|PDB:3U4K"
FT   STRAND          48..57
FT                   /evidence="ECO:0007829|PDB:3U4K"
FT   STRAND          63..79
FT                   /evidence="ECO:0007829|PDB:3U4K"
FT   HELIX           88..90
FT                   /evidence="ECO:0007829|PDB:3U4K"
FT   STRAND          99..109
FT                   /evidence="ECO:0007829|PDB:3U4K"
FT   STRAND          111..125
FT                   /evidence="ECO:0007829|PDB:3U4K"
FT   STRAND          129..137
FT                   /evidence="ECO:0007829|PDB:3U4K"
FT   STRAND          139..141
FT                   /evidence="ECO:0007829|PDB:3U4K"
FT   STRAND          149..159
FT                   /evidence="ECO:0007829|PDB:3U4K"
FT   STRAND          161..166
FT                   /evidence="ECO:0007829|PDB:3U4K"
FT   STRAND          168..174
FT                   /evidence="ECO:0007829|PDB:3U4K"
SQ   SEQUENCE   321 AA;  33970 MW;  5D1EB44F4335AB72 CRC64;
     MKKLTLFIGL MALGTTSAWA SCWQSNSAYE INMAMGRVVV SPDLPVGSVI ATKTWTMPDN
     NTIYVTCDRN TTLKSDAKVV AAGLVQGANK VYSTAIPGIG LRFSRKGAIS MIYPDSYTTT
     GSSFRLVGST FTLDIIKTST TTGSGTLASG PYTEYGPGFT ILKTSLNADA ITIVSPSCTI
     LGGKNMNVDI GTIKRADLKG VGTWAGGTPF DIKLECSGGV SVSGYANINT SFSGTLATNT
     SANQGVLLNE KTGNSAAKGV GVQVIKDNTP LEFNKKHNIG TLQSQETRYI TLPLHARFYQ
     YAPTTSTGEV ESHLVFNLTY D