Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]

MULTISPECIES: molecular chaperone [Klebsiella].


LOCUS       WP_002892383             231 aa            linear   BCT 01-JAN-2025
ACCESSION   WP_002892383
VERSION     WP_002892383.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Hung,D.L., Knight,S.D., Woods,R.M., Pinkner,J.S. and Hultgren,S.J.
  TITLE     Molecular basis of two subfamilies of immunoglobulin-like
            chaperones
  JOURNAL   EMBO J 15 (15), 3792-3805 (1996)
   PUBMED   8670884
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Hultgren,S.J., Normark,S. and Abraham,S.N.
  TITLE     Chaperone-assisted assembly and molecular architecture of adhesive
            pili
  JOURNAL   Annu Rev Microbiol 45, 383-415 (1991)
   PUBMED   1683764
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11459711
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..231
                     /product="molecular chaperone"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_process="GO:0043711 - pilus organization [Evidence
                     IEA]"
                     /GO_process="GO:0061077 - chaperone-mediated protein
                     folding [Evidence IEA]"
                     /calculated_mol_wt=25232
     Region          1..230
                     /region_name="FimC"
                     /note="P pilus assembly protein, chaperone PapD
                     [Extracellular structures]; COG3121"
                     /db_xref="CDD:442355"
ORIGIN      
        1 mrrmvlalll ssylpsadas mvidgtriif sgdkkeiavr atnmgetpsl tqvwvddgrv
       61 qnqpekdaap fivlppivri epgkgqswrl vfngsrlpqd reslfwfnll dippepkngk
      121 tdnylqlair sriklfyrpa gvaaekiaae kalswalapt gnglrvsnas aryitidsit
      181 lngkkhaagm vapfssleia pkgvalrtlp akfsfttind ygavvnhnyp q