ID   SKP_PECAS               Reviewed;         165 AA.
AC   Q6D8D4;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Chaperone protein Skp;
DE   Flags: Precursor;
GN   Name=skp; OrderedLocusNames=ECA1040;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG73951.1; -; Genomic_DNA.
DR   RefSeq; WP_011092638.1; NC_004547.2.
DR   AlphaFoldDB; Q6D8D4; -.
DR   SMR; Q6D8D4; -.
DR   STRING; 218491.ECA1040; -.
DR   EnsemblBacteria; CAG73951; CAG73951; ECA1040.
DR   GeneID; 57207869; -.
DR   KEGG; eca:ECA1040; -.
DR   PATRIC; fig|218491.5.peg.1048; -.
DR   eggNOG; COG2825; Bacteria.
DR   HOGENOM; CLU_101388_2_0_6; -.
DR   OMA; EKEQYDM; -.
DR   OrthoDB; 1854604at2; -.
DR   Proteomes; UP000007966; 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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..165
FT                   /note="Chaperone protein Skp"
FT                   /id="PRO_0000227888"
FT   REGION          70..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..113
FT                   /note="Lipopolysaccharide binding"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   165 AA;  18307 MW;  F28E7CE2CA096568 CRC64;
     MKKWLCAAGL GLVLAASASV QAADKIAVVN VSSIFQQLPQ RESVGKQLEN EFKGRASELQ
     SMENDLQGKM QKLQRDGSTM KASDRSKMEK DVMAQREQFS TKAQAFEQDN RRRQTEERNK
     ILSRIQDAVK AVATKEGYDV VIDANAVAYV ANAKDITADV LKQVK