SKP_ECO57
ID SKP_ECO57 Reviewed; 161 AA.
AC P0AEU9; P11457;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Chaperone protein Skp;
DE Flags: Precursor;
GN Name=skp; Synonyms=hlpA; OrderedLocusNames=Z0190, ECs0180;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG54480.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB33603.1; -; Genomic_DNA.
DR PIR; D85502; D85502.
DR PIR; D90651; D90651.
DR RefSeq; NP_308207.1; NC_002695.1.
DR RefSeq; WP_000758956.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AEU9; -.
DR BMRB; P0AEU9; -.
DR SMR; P0AEU9; -.
DR IntAct; P0AEU9; 1.
DR STRING; 155864.EDL933_0183; -.
DR EnsemblBacteria; AAG54480; AAG54480; Z0190.
DR EnsemblBacteria; BAB33603; BAB33603; ECs_0180.
DR GeneID; 67416254; -.
DR GeneID; 913889; -.
DR KEGG; ece:Z0190; -.
DR KEGG; ecs:ECs_0180; -.
DR PATRIC; fig|386585.9.peg.283; -.
DR eggNOG; COG2825; Bacteria.
DR HOGENOM; CLU_101388_2_0_6; -.
DR OMA; EKEQYDM; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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_0000045053"
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