ID   SKP_BLOPB               Reviewed;         166 AA.
AC   Q493C3;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Chaperone protein Skp;
DE   Flags: Precursor;
GN   Name=skp; OrderedLocusNames=BPEN_288;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPEN;
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ40919.1; -; Genomic_DNA.
DR   RefSeq; WP_011282826.1; NC_007292.1.
DR   AlphaFoldDB; Q493C3; -.
DR   SMR; Q493C3; -.
DR   STRING; 291272.BPEN_288; -.
DR   EnsemblBacteria; AAZ40919; AAZ40919; BPEN_288.
DR   KEGG; bpn:BPEN_288; -.
DR   eggNOG; COG2825; Bacteria.
DR   HOGENOM; CLU_101388_2_0_6; -.
DR   OMA; EKEQYDM; -.
DR   BioCyc; CBLO291272:BPEN_RS01415-MON; -.
DR   Proteomes; UP000007794; 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; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..166
FT                   /note="Chaperone protein Skp"
FT                   /id="PRO_0000227887"
FT   REGION          102..113
FT                   /note="Lipopolysaccharide binding"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   166 AA;  19505 MW;  CC15B1025A06051D CRC64;
     MKKWTYILSM VIWITQISPV DAEDKIAIVN ISNIFQQSSQ RAKIIKQLEY EFKDRATELE
     KMEHDLQMKI QTLQRDGATM KTIERSELEK SLINQREIFS NKAKEFQQEN HSRQTEERDK
     ILNMIQNVVT NVAKKENYDI VIDTNAVLYH SIRVTDITNS VMKQVG