ID   SKP_VIBCH               Reviewed;         169 AA.
AC   Q9KPW1;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Chaperone protein Skp;
DE   Flags: Precursor;
GN   Name=skp; Synonyms=ompH; OrderedLocusNames=VC_2251;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003852; AAF95395.1; -; Genomic_DNA.
DR   PIR; A82099; A82099.
DR   RefSeq; NP_231882.1; NC_002505.1.
DR   RefSeq; WP_000794125.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KPW1; -.
DR   SMR; Q9KPW1; -.
DR   STRING; 243277.VC_2251; -.
DR   EnsemblBacteria; AAF95395; AAF95395; VC_2251.
DR   GeneID; 57740874; -.
DR   KEGG; vch:VC_2251; -.
DR   PATRIC; fig|243277.26.peg.2147; -.
DR   eggNOG; COG2825; Bacteria.
DR   HOGENOM; CLU_101388_2_1_6; -.
DR   OMA; EKEQYDM; -.
DR   BioCyc; VCHO:VC2251-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR   GO; GO:0032978; P:protein insertion into membrane from inner side; IBA:GO_Central.
DR   GO; GO:0022417; P:protein maturation by protein folding; IBA:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..169
FT                   /note="Chaperone protein Skp"
FT                   /id="PRO_0000020179"
SQ   SEQUENCE   169 AA;  18952 MW;  9C878AB7CE217CC7 CRC64;
     MKNMIKAASL GLIILSSSMM ANAAEAAQKI GYINTAQVFQ ALPQREVVLQ KMQEEFKDKA
     AELQAIQADA KTKIEKLKRD GQLMGQDEVE KLRIEIGQLD SKYKIKAQAL EQASARREAE
     EKQKLFKVIQ DAVKKVAEKE GYDIVLDTSS MQYGKPEHNL SEKVIKAIK