ID   MRKB_KLEPN              Reviewed;         233 AA.
AC   P21646;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Chaperone protein MrkB;
DE   Flags: Precursor;
GN   Name=mrkB;
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).
CC   -!- FUNCTION: Mediates assembly of pili by forming soluble multimeric
CC       complexes with pili subunits as an intermediate step in the assembly
CC       process. This protein is involved in type 3 pili assembly.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC       {ECO:0000305}.
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DR   EMBL; M55912; AAA25094.1; -; Genomic_DNA.
DR   PIR; C39142; C39142.
DR   AlphaFoldDB; P21646; -.
DR   SMR; P21646; -.
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; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..233
FT                   /note="Chaperone protein MrkB"
FT                   /id="PRO_0000009282"
SQ   SEQUENCE   233 AA;  25144 MW;  F71EAA9E0AF2317C CRC64;
     MKRIALFFCF IFSFAAHANN IIVNGTRFIY PGNEKEITVQ LSNTADRPAL ATAWLDNGNA
     DATPDTITTP FIITPPISRV DAKSGQTLRI KLGSNAGLAK DKETLWWLNL LEIPPVEASQ
     KNEGQNILQL AIRSRFKFIY RPAGLGNRDA AAEKLALSAN GSSLSVSNPT PFYITVSRIS
     RNGGKALNSK TVMFAPQSSQ TIALSSAVSK GETLTVNNIN DYGADVAVKV TVK