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SKP_PHOLU
ID   SKP_PHOLU               Reviewed;         165 AA.
AC   Q9S340;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Chaperone protein Skp;
DE   Flags: Precursor;
GN   Name=skp; Synonyms=ompH;
OS   Photorhabdus luminescens (Xenorhabdus luminescens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=29488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Hm;
RA   Chatonnet-Marton P.I., Givaudan A., Lanois A., Boemare N.E.;
RT   "Photorhabdus luminescens genomic region homologous to 4.0 minute
RT   Escherichia coli region promotes pleiotropic phenotypes.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
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; AJ236920; CAB51930.1; -; Genomic_DNA.
DR   RefSeq; WP_049583806.1; NZ_MYFJ01000042.1.
DR   AlphaFoldDB; Q9S340; -.
DR   SMR; Q9S340; -.
DR   STRING; 29488.KS18_15800; -.
DR   GeneID; 45656649; -.
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; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..165
FT                   /note="Chaperone protein Skp"
FT                   /id="PRO_0000227890"
FT   REGION          102..113
FT                   /note="Lipopolysaccharide binding"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   165 AA;  18402 MW;  91BC88EB65FAD767 CRC64;
     MKKLLCAASF GIALAFSAGA QAADKIAVVN VGEIFQQLPA REAVAKQLEN EFKNRASELQ
     RMETDLQSKI QKLQRDGSTM KSSERTNLEK EVMAKREEFG KKAQAFEQDH RRREMEERNK
     ILSRIQDAIK VVAGKEGYDI VIDANAVAYS VSGKNITASV LKQVK
 
 
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