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ECOLI:SKP

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) skp (synonyms: hlpA, ompH)
Protein Name(s) Chaperone protein Skp

DNA-binding 17 kDa protein Histone-like protein HLP-1 Seventeen kilodalton protein

External Links
UniProt P0AEU7
EMBL M21118
X75465
U70214
U00096
AP009048
X54797
PIR JT0304
RefSeq NP_414720.1
YP_488480.1
PDB 1SG2
1U2M
PDBsum 1SG2
1U2M
ProteinModelPortal P0AEU7
SMR P0AEU7
DIP DIP-36210N
IntAct P0AEU7
MINT MINT-1229504
STRING 511145.b0178
PaxDb P0AEU7
PRIDE P0AEU7
EnsemblBacteria AAC73289
BAA77853
GeneID 12934433
944861
KEGG ecj:Y75_p0174
eco:b0178
PATRIC 32115467
EchoBASE EB0450
EcoGene EG10455
eggNOG COG2825
HOGENOM HOG000261755
KO K06142
OMA KWLYAAG
OrthoDB EOG6F297R
PhylomeDB P0AEU7
BioCyc EcoCyc:EG10455-MONOMER
ECOL316407:JW0173-MONOMER
EvolutionaryTrace P0AEU7
PRO PR:P0AEU7
Proteomes UP000000318
UP000000625
Genevestigator P0AEU7
GO GO:0005829
GO:0030288
GO:0001530
GO:0051082
GO:0051085
GO:0043165
GO:0065002
GO:0006457
GO:0032978
GO:0022417
GO:0050821
InterPro IPR005632
IPR024930
Pfam PF03938
PIRSF PIRSF002094
SMART SM00935
SUPFAM SSF111384

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0022417

protein maturation by protein folding

PMID:9914480[1]

ECO:0000314

P

Fig. 4C shows the maturation on PhoE in Skp serum. Table 1 shows amount of PhoE folded based on incdreasing concentraions of Skp.

complete
CACAO 2085

involved_in

GO:0022417

protein maturation by protein folding

PMID:9914480[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0061077

chaperone-mediated protein folding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10455
PANTHER:PTN002170712

P

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10455
PANTHER:PTN002170712

F

Seeded From UniProt

complete

involved_in

GO:0050821

protein stabilization

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10455
PANTHER:PTN002170712

P

Seeded From UniProt

complete

involved_in

GO:0032978

protein insertion into membrane from inner side

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10455
PANTHER:PTN002170712

P

Seeded From UniProt

complete

part_of

GO:0030288

outer membrane-bounded periplasmic space

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10455
PANTHER:PTN002170712

C

Seeded From UniProt

complete

involved_in

GO:0022417

protein maturation by protein folding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10455
PANTHER:PTN002170712

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:24077225[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0AEU7

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:19181847[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0AEU7

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16858726[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0AEU7

F

Seeded From UniProt

complete

part_of

GO:0030288

outer membrane-bounded periplasmic space

PMID:10455120[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

PMID:10455120[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0061077

chaperone-mediated protein folding

PMID:12509434[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:9914480[1]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P02943
UniProtKB:P0A910

F

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:9914480[1]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P02932

F

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:17928002[8]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A910
UniProtKB:P0A940
UniProtKB:P76045

F

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:12509434[7]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A910

F

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:11278858[9]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P02932

F

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:10455120[6]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A910

F

Seeded From UniProt

complete

involved_in

GO:0050821

protein stabilization

PMID:23796519[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0050821

protein stabilization

PMID:15304217[11]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0050821

protein stabilization

PMID:12509434[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043165

Gram-negative-bacterium-type cell outer membrane assembly

PMID:17908933[12]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A940

P

Seeded From UniProt

complete

involved_in

GO:0043165

Gram-negative-bacterium-type cell outer membrane assembly

PMID:17908933[12]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P0ABZ6

P

Seeded From UniProt

complete

involved_in

GO:0043165

Gram-negative-bacterium-type cell outer membrane assembly

PMID:12509434[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0032978

protein insertion into membrane from inner side

PMID:23796519[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0032978

protein insertion into membrane from inner side

PMID:12509434[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0030288

outer membrane-bounded periplasmic space

PMID:8730870[13]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0030288

outer membrane-bounded periplasmic space

PMID:1838129[14]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0001530

lipopolysaccharide binding

PMID:17928002[8]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A910

F

Seeded From UniProt

complete

enables

GO:0001530

lipopolysaccharide binding

PMID:15304217[11]

ECO:0000245

automatically integrated combinatorial evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005632

F

Seeded From UniProt

complete

part_of

GO:0042597

periplasmic space

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0574
UniProtKB-SubCell:SL-0200

C

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 1.2 1.3 De Cock, H et al. (1999) Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein. Eur. J. Biochem. 259 96-103 PubMed GONUTS page
  2. ↑ 2.0 2.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 3.3 3.4 3.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. ↑ Burmann, BM et al. (2013) Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp. Nat. Struct. Mol. Biol. 20 1265-72 PubMed GONUTS page
  5. ↑ Walton, TA et al. (2009) The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains. Proc. Natl. Acad. Sci. U.S.A. 106 1772-7 PubMed GONUTS page
  6. ↑ 6.0 6.1 6.2 Schäfer, U et al. (1999) Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J. Biol. Chem. 274 24567-74 PubMed GONUTS page
  7. ↑ 7.0 7.1 7.2 7.3 7.4 Bulieris, PV et al. (2003) Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide. J. Biol. Chem. 278 9092-9 PubMed GONUTS page
  8. ↑ 8.0 8.1 Qu, J et al. (2007) The trimeric periplasmic chaperone Skp of Escherichia coli forms 1:1 complexes with outer membrane proteins via hydrophobic and electrostatic interactions. J. Mol. Biol. 374 91-105 PubMed GONUTS page
  9. ↑ Harms, N et al. (2001) The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane. J. Biol. Chem. 276 18804-11 PubMed GONUTS page
  10. ↑ 10.0 10.1 McMorran, LM et al. (2013) Dissecting the effects of periplasmic chaperones on the in vitro folding of the outer membrane protein PagP. J. Mol. Biol. 425 3178-91 PubMed GONUTS page
  11. ↑ 11.0 11.1 Walton, TA & Sousa, MC (2004) Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation. Mol. Cell 15 367-74 PubMed GONUTS page
  12. ↑ 12.0 12.1 Sklar, JG et al. (2007) Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli. Genes Dev. 21 2473-84 PubMed GONUTS page
  13. ↑ Chen, R & Henning, U (1996) A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Mol. Microbiol. 19 1287-94 PubMed GONUTS page
  14. ↑ Thome, BM & Müller, M (1991) Skp is a periplasmic Escherichia coli protein requiring SecA and SecY for export. Mol. Microbiol. 5 2815-21 PubMed GONUTS page
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