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Protein

Chaperone protein Skp

Gene

skp

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. Required for the efficient release of OmpA from the inner membrane, the maintenance of its solubility in the periplasm, and, in association with lipopolysaccharide (LPS), for the efficient folding and insertion of OmpA into the outer membrane.5 Publications

GO - Molecular functioni

  • lipopolysaccharide binding Source: EcoCyc
  • unfolded protein binding Source: EcoCyc

GO - Biological processi

  • chaperone mediated protein folding requiring cofactor Source: EcoCyc
  • Gram-negative-bacterium-type cell outer membrane assembly Source: EcoCyc
  • intracellular protein transmembrane transport Source: EcoCyc
  • protein folding Source: EcoCyc
  • protein insertion into membrane from inner side Source: EcoCyc
  • protein maturation by protein folding Source: CACAO
  • protein stabilization Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

BioCyciEcoCyc:EG10455-MONOMER.
ECOL316407:JW0173-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chaperone protein Skp
Alternative name(s):
DNA-binding 17 kDa protein
Histone-like protein HLP-1
Seventeen kilodalton protein
Gene namesi
Name:skp
Synonyms:hlpA, ompH
Ordered Locus Names:b0178, JW0173
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10455. skp.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • outer membrane-bounded periplasmic space Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20202 PublicationsAdd
BLAST
Chaini21 – 161141Chaperone protein SkpPRO_0000020176Add
BLAST

Proteomic databases

EPDiP0AEU7.
PaxDbiP0AEU7.
PRIDEiP0AEU7.

Interactioni

Subunit structurei

Homotrimer. Interacts with OmpA. Interacts with PhoE during its translocation across the inner membrane, but, in contrast to OmpA, release of PhoE from the inner membrane is not dependent on skp. Interacts also with LamB, OmpC and OmpF.3 Publications

GO - Molecular functioni

  • unfolded protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4263427. 186 interactions.
DIPiDIP-36210N.
IntActiP0AEU7. 28 interactions.
MINTiMINT-1229504.
STRINGi511145.b0178.

Structurei

Secondary structure

1
161
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 274Combined sources
Helixi29 – 4012Combined sources
Turni41 – 466Combined sources
Helixi48 – 6518Combined sources
Helixi78 – 9013Combined sources
Helixi92 – 10413Combined sources
Helixi106 – 13025Combined sources
Beta strandi134 – 1385Combined sources
Helixi139 – 1413Combined sources
Beta strandi142 – 1454Combined sources
Beta strandi149 – 1513Combined sources
Helixi153 – 1597Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SG2X-ray2.35A/B/C20-161[»]
1U2MX-ray2.30A/B/C21-161[»]
ProteinModelPortaliP0AEU7.
SMRiP0AEU7. Positions 21-161.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AEU7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 10812Lipopolysaccharide bindingSequence analysisAdd
BLAST

Domaini

Composed of a compact central beta-barrel domain with long alpha-helical extensions that form a three-pronged structure around an internal cavity. Substrate proteins may be bound in this cavity.

Sequence similaritiesi

Belongs to the Skp family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108RFI. Bacteria.
COG2825. LUCA.
HOGENOMiHOG000261755.
KOiK06142.
OMAiQAFDQDN.
OrthoDBiEOG6F297R.
PhylomeDBiP0AEU7.

Family and domain databases

InterProiIPR005632. Chaperone_Skp.
IPR024930. Skp_domain.
[Graphical view]
PfamiPF03938. OmpH. 1 hit.
[Graphical view]
PIRSFiPIRSF002094. OMP26_Skp. 1 hit.
SMARTiSM00935. OmpH. 1 hit.
[Graphical view]
SUPFAMiSSF111384. SSF111384. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AEU7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKWLLAAGL GLALATSAQA ADKIAIVNMG SLFQQVAQKT GVSNTLENEF
60 70 80 90 100
KGRASELQRM ETDLQAKMKK LQSMKAGSDR TKLEKDVMAQ RQTFAQKAQA
110 120 130 140 150
FEQDRARRSN EERGKLVTRI QTAVKSVANS QDIDLVVDAN AVAYNSSDVK
160
DITADVLKQV K
Length:161
Mass (Da):17,688
Last modified:December 20, 2005 - v1
Checksum:i2A966BBD83F3E675
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151A → L in CAA53207 (PubMed:1991717).Curated
Sequence conflicti149 – 1491V → E in CAA53207 (PubMed:1991717).Curated
Sequence conflicti153 – 1531T → I in CAA53207 (PubMed:1991717).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21118 Genomic DNA. Translation: AAA24630.1.
X75465 Genomic DNA. Translation: CAA53207.1.
U70214 Genomic DNA. Translation: AAB08607.1.
U00096 Genomic DNA. Translation: AAC73289.1.
AP009048 Genomic DNA. Translation: BAA77853.1.
X54797 Genomic DNA. Translation: CAA38567.1.
PIRiJT0304. DNEC17.
RefSeqiNP_414720.1. NC_000913.3.
WP_000758956.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73289; AAC73289; b0178.
BAA77853; BAA77853; BAA77853.
GeneIDi944861.
KEGGiecj:JW0173.
eco:b0178.
PATRICi32115467. VBIEscCol129921_0185.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21118 Genomic DNA. Translation: AAA24630.1.
X75465 Genomic DNA. Translation: CAA53207.1.
U70214 Genomic DNA. Translation: AAB08607.1.
U00096 Genomic DNA. Translation: AAC73289.1.
AP009048 Genomic DNA. Translation: BAA77853.1.
X54797 Genomic DNA. Translation: CAA38567.1.
PIRiJT0304. DNEC17.
RefSeqiNP_414720.1. NC_000913.3.
WP_000758956.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SG2X-ray2.35A/B/C20-161[»]
1U2MX-ray2.30A/B/C21-161[»]
ProteinModelPortaliP0AEU7.
SMRiP0AEU7. Positions 21-161.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263427. 186 interactions.
DIPiDIP-36210N.
IntActiP0AEU7. 28 interactions.
MINTiMINT-1229504.
STRINGi511145.b0178.

Proteomic databases

EPDiP0AEU7.
PaxDbiP0AEU7.
PRIDEiP0AEU7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73289; AAC73289; b0178.
BAA77853; BAA77853; BAA77853.
GeneIDi944861.
KEGGiecj:JW0173.
eco:b0178.
PATRICi32115467. VBIEscCol129921_0185.

Organism-specific databases

EchoBASEiEB0450.
EcoGeneiEG10455. skp.

Phylogenomic databases

eggNOGiENOG4108RFI. Bacteria.
COG2825. LUCA.
HOGENOMiHOG000261755.
KOiK06142.
OMAiQAFDQDN.
OrthoDBiEOG6F297R.
PhylomeDBiP0AEU7.

Enzyme and pathway databases

BioCyciEcoCyc:EG10455-MONOMER.
ECOL316407:JW0173-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AEU7.
PROiP0AEU7.

Family and domain databases

InterProiIPR005632. Chaperone_Skp.
IPR024930. Skp_domain.
[Graphical view]
PfamiPF03938. OmpH. 1 hit.
[Graphical view]
PIRSFiPIRSF002094. OMP26_Skp. 1 hit.
SMARTiSM00935. OmpH. 1 hit.
[Graphical view]
SUPFAMiSSF111384. SSF111384. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of the gene for the DNA-binding 17K protein of Escherichia coli."
    Holck A., Kleppe K.
    Gene 67:117-124(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-40.
  2. "The ompH gene of Yersinia enterocolitica: cloning, sequencing, expression, and comparison with known enterobacterial ompH sequences."
    Hirvas L., Koski P., Vaara M.
    J. Bacteriol. 173:1223-1229(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
    Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Cloning and nucleotide sequence of the firA gene and the firA200(Ts) allele from Escherichia coli."
    Dicker I.B., Seetharam S.R.
    J. Bacteriol. 173:334-344(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 72-161.
    Strain: K12 / MG1655 / ATCC 47076.
  8. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-32.
    Strain: K12 / EMG2.
  9. "Bacterial 'histone-like protein I' (HLP-I) is an outer membrane constituent?"
    Hirvas L., Coleman J., Koski P., Vaara M.
    FEBS Lett. 262:123-126(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISCUSSION OF SUBCELLULAR LOCATION.
    Strain: K12 / JM109 / ATCC 53323.
  10. "Skp is a periplasmic Escherichia coli protein requiring SecA and SecY for export."
    Thome B.M., Mueller M.
    Mol. Microbiol. 5:2815-2821(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins."
    Chen R., Henning U.
    Mol. Microbiol. 19:1287-1294(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  12. "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."
    de Cock H., Schaefer U., Potgeter M., Demel R., Mueller M., Tommassen J.
    Eur. J. Biochem. 259:96-103(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  13. "Skp, a molecular chaperone of Gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins."
    Schaefer U., Beck K., Mueller M.
    J. Biol. Chem. 274:24567-24574(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  14. "The early interaction of the outer membrane protein phoE with the periplasmic chaperone Skp occurs at the cytoplasmic membrane."
    Harms N., Koningstein G., Dontje W., Mueller M., Oudega B., Luirink J., de Cock H.
    J. Biol. Chem. 276:18804-18811(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  15. "Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide."
    Bulieris P.V., Behrens S., Holst O., Kleinschmidt J.H.
    J. Biol. Chem. 278:9092-9099(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "The periplasmic E. coli chaperone Skp is a trimer in solution: biophysical and preliminary crystallographic characterization."
    Schlapschy M., Dommel M.K., Hadian K., Fogarasi M., Korndoerfer I.P., Skerra A.
    Biol. Chem. 385:137-143(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, PRELIMINARY X-RAY CRYSTALLOGRAPHY.
    Strain: K12.
  17. "Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation."
    Walton T.A., Sousa M.C.
    Mol. Cell 15:367-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-161, SUBUNIT.
    Strain: K12.
  18. "Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture."
    Korndoerfer I.P., Dommel M.K., Skerra A.
    Nat. Struct. Mol. Biol. 11:1015-1020(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 21-161, SUBUNIT.

Entry informationi

Entry nameiSKP_ECOLI
AccessioniPrimary (citable) accession number: P0AEU7
Secondary accession number(s): P11457
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: April 13, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Does not require ATP for its activity.

Caution

Was originally thought to bind DNA. It was probably an artifact due to the cationic nature of skp.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.