(data stored in ACNUC7421 zone)

SWISSPROT: 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   08-MAY-2019, entry version 83.
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Molecular chaperone that interacts specifically with
CC       outer membrane proteins, thus maintaining the solubility of early
CC       folding intermediates during passage through the periplasm.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Skp family. {ECO:0000305}.
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_SDVX01000001.1.
DR   SMR; P0AEU9; -.
DR   IntAct; P0AEU9; 1.
DR   STRING; 155864.EDL933_0183; -.
DR   PRIDE; P0AEU9; -.
DR   EnsemblBacteria; AAG54480; AAG54480; Z0190.
DR   EnsemblBacteria; BAB33603; BAB33603; BAB33603.
DR   GeneID; 913889; -.
DR   KEGG; ece:Z0190; -.
DR   KEGG; ecs:ECs0180; -.
DR   PATRIC; fig|386585.9.peg.283; -.
DR   eggNOG; ENOG4108RFI; Bacteria.
DR   eggNOG; COG2825; LUCA.
DR   HOGENOM; HOG000261755; -.
DR   KO; K06142; -.
DR   BioCyc; ECOO157:HLPA-MONOMER; -.
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.
PE   3: Inferred from homology;
DR   PRODOM; P0AEU9.
DR   SWISS-2DPAGE; P0AEU9.
KW   Chaperone; Complete proteome; Periplasm; Reference proteome; Signal.
FT   SIGNAL        1     20       {ECO:0000250}.
FT   CHAIN        21    161       Chaperone protein Skp.
FT                                /FTId=PRO_0000045053.
FT   REGION       97    108       Lipopolysaccharide binding.
FT                                {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
//

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