ID   SKP_BLOFL               Reviewed;         168 AA.
AC   Q7VRD7;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Chaperone protein Skp;
DE   Flags: Precursor;
GN   Name=skp; OrderedLocusNames=Bfl280;
OS   Blochmannia floridanus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=203907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA   Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA   Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA   van Ham R.C.H.J., Gross R., Moya A.;
RT   "The genome sequence of Blochmannia floridanus: comparative analysis of
RT   reduced genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
CC   -!- FUNCTION: Molecular chaperone that interacts specifically with outer
CC       membrane proteins, thus maintaining the solubility of early folding
CC       intermediates during passage through the periplasm. {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Skp family. {ECO:0000305}.
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DR   EMBL; BX248583; CAD83351.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7VRD7; -.
DR   SMR; Q7VRD7; -.
DR   STRING; 203907.Bfl280; -.
DR   PRIDE; Q7VRD7; -.
DR   EnsemblBacteria; CAD83351; CAD83351; Bfl280.
DR   KEGG; bfl:Bfl280; -.
DR   eggNOG; COG2825; Bacteria.
DR   HOGENOM; CLU_101388_2_0_6; -.
DR   OMA; EKEQYDM; -.
DR   Proteomes; UP000002192; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   Gene3D; 3.30.910.20; -; 1.
DR   InterPro; IPR005632; Chaperone_Skp.
DR   InterPro; IPR024930; Skp_dom_sf.
DR   PANTHER; PTHR35089; PTHR35089; 1.
DR   Pfam; PF03938; OmpH; 1.
DR   PIRSF; PIRSF002094; OMP26_Skp; 1.
DR   SMART; SM00935; OmpH; 1.
DR   SUPFAM; SSF111384; SSF111384; 1.
PE   3: Inferred from homology;
KW   Chaperone; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..168
FT                   /note="Chaperone protein Skp"
FT                   /id="PRO_0000227886"
FT   REGION          102..113
FT                   /note="Lipopolysaccharide binding"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   168 AA;  19664 MW;  37BC6B37A5AAAB43 CRC64;
     MKNRVYMLGI IIWLAQINYV NAANKIVVMN VANIFQQSAQ RTEIIKQLEY EFKDRAAELE
     MMEHDLQTKM QTLQRDGATM TASDRNTLEK SLIAQRELFS NKAKLFQQEN HARQTEERDK
     ILDMIYKIVK NIAKKENYDI VIDTNAVVYF SSHIKDITDS VSNQMRVK