ID   SKP_YERPS               Reviewed;         165 AA.
AC   P31520; Q667J8;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Chaperone protein Skp;
DE   AltName: Full=Cationic 19 kDa outer membrane protein;
DE   Flags: Precursor;
GN   Name=skp; Synonyms=ompH; OrderedLocusNames=YPTB2994;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-158.
RC   STRAIN=78;
RX   PubMed=1756172; DOI=10.1016/0167-4781(91)90226-c;
RA   Vuorio R., Hirvas L., Raybourne R.B., Yu D.T.Y., Vaara M.;
RT   "The nucleotide and deduced amino acid sequence of the cationic 19 kDa
RT   outer membrane protein OmpH of Yersinia pseudotuberculosis.";
RL   Biochim. Biophys. Acta 1129:124-126(1991).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH22232.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX936398; CAH22232.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M73247; AAA27657.1; -; Genomic_DNA.
DR   PIR; S19728; S19728.
DR   RefSeq; WP_002212140.1; NZ_CP009712.1.
DR   AlphaFoldDB; P31520; -.
DR   SMR; P31520; -.
DR   EnsemblBacteria; CAH22232; CAH22232; YPTB2994.
DR   GeneID; 66844577; -.
DR   KEGG; ypo:BZ17_3627; -.
DR   KEGG; yps:YPTB2994; -.
DR   PATRIC; fig|273123.14.peg.3808; -.
DR   OMA; EKEQYDM; -.
DR   Proteomes; UP000001011; 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..165
FT                   /note="Chaperone protein Skp"
FT                   /id="PRO_0000020182"
FT   REGION          102..113
FT                   /note="Lipopolysaccharide binding"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   165 AA;  18279 MW;  982D3BEF3A66FB6C CRC64;
     MKKWLCAASL GLALAASASV QAADKIAIVN VSSIFQQLPA REAVAKQLEN EFKGRATELQ
     GMERDLQTKM QKLQRDGSTM KASDRTKLEN EVMKQRETFS TKAQAFEQDN RRRQAEERNK
     ILSRIQDAVK SVATKGGYDV VIDANAVAYA DSSKDITADV LKQVK