ID   SKP_SHIFL               Reviewed;         161 AA.
AC   P0AEV0; P11457;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Chaperone protein Skp;
DE   Flags: Precursor;
GN   Name=skp; Synonyms=hlpA; OrderedLocusNames=SF0168, S0171;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(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; AE005674; AAN41830.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP15711.1; -; Genomic_DNA.
DR   RefSeq; NP_706123.1; NC_004337.2.
DR   RefSeq; WP_000758956.1; NZ_WPGN01000007.1.
DR   AlphaFoldDB; P0AEV0; -.
DR   BMRB; P0AEV0; -.
DR   SMR; P0AEV0; -.
DR   STRING; 198214.SF0168; -.
DR   PRIDE; P0AEV0; -.
DR   EnsemblBacteria; AAN41830; AAN41830; SF0168.
DR   EnsemblBacteria; AAP15711; AAP15711; S0171.
DR   GeneID; 1024435; -.
DR   GeneID; 67416254; -.
DR   KEGG; sfl:SF0168; -.
DR   KEGG; sfx:S0171; -.
DR   PATRIC; fig|198214.7.peg.190; -.
DR   HOGENOM; CLU_101388_2_0_6; -.
DR   OMA; EKEQYDM; -.
DR   OrthoDB; 1854604at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..161
FT                   /note="Chaperone protein Skp"
FT                   /id="PRO_0000045055"
FT   REGION          97..108
FT                   /note="Lipopolysaccharide binding"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   161 AA;  17688 MW;  2A966BBD83F3E675 CRC64;
     MKKWLLAAGL GLALATSAQA ADKIAIVNMG SLFQQVAQKT GVSNTLENEF KGRASELQRM
     ETDLQAKMKK LQSMKAGSDR TKLEKDVMAQ RQTFAQKAQA FEQDRARRSN EERGKLVTRI
     QTAVKSVANS QDIDLVVDAN AVAYNSSDVK DITADVLKQV K