ID   SKP_YEREN               Reviewed;         164 AA.
AC   P31519;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Chaperone protein Skp;
DE   AltName: Full=Cationic 19 kDa outer membrane protein;
DE   Flags: Precursor;
GN   Name=skp; Synonyms=ompH;
OS   Yersinia enterocolitica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1991717; DOI=10.1128/jb.173.3.1223-1229.1991;
RA   Hirvas L., Koski P., Vaara M.;
RT   "The ompH gene of Yersinia enterocolitica: cloning, sequencing, expression,
RT   and comparison with known enterobacterial ompH sequences.";
RL   J. Bacteriol. 173:1223-1229(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}.
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DR   EMBL; M34854; AAA27658.1; -; mRNA.
DR   AlphaFoldDB; P31519; -.
DR   SMR; P31519; -.
DR   STRING; 1443113.LC20_01204; -.
DR   eggNOG; COG2825; Bacteria.
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   2: Evidence at transcript level;
KW   Chaperone; Periplasm; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..164
FT                   /note="Chaperone protein Skp"
FT                   /id="PRO_0000020180"
FT   REGION          101..112
FT                   /note="Lipopolysaccharide binding"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   164 AA;  18225 MW;  70F6C0E5B3C85B7B CRC64;
     MKKWLCAASL GLALAASASV QAAKIAIVNV SRIFQQLPES ETVAKQLENE FKGRATELQG
     MESDLQTKMQ KLQRDGSTMK ASDRTKLEND VMKQRETFST KAQAFEQDNR RRQMEERNKI
     LSRIQDAVKS VASKGGYDVV IDANAVAYAD PSKDITADVL KQVK