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Chaperone protein Skp (DNA-binding 17 kDa protein) (Histone-like protein HLP-1) (Seventeen kilodalton protein)

 SKP_ECOLI               Reviewed;         161 AA.
P0AEU7; P11457;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 1.
28-MAR-2018, entry version 106.
RecName: Full=Chaperone protein Skp;
AltName: Full=DNA-binding 17 kDa protein;
AltName: Full=Histone-like protein HLP-1;
AltName: Full=Seventeen kilodalton protein;
Flags: Precursor;
Name=skp; Synonyms=hlpA, ompH; OrderedLocusNames=b0178, JW0173;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 21-40.
PubMed=2843433; DOI=10.1016/0378-1119(88)90014-5;
Holck A., Kleppe K.;
"Cloning and sequencing of the gene for the DNA-binding 17K protein of
Escherichia coli.";
Gene 67:117-124(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1991717; DOI=10.1128/jb.173.3.1223-1229.1991;
Hirvas L., Koski P., Vaara M.;
"The ompH gene of Yersinia enterocolitica: cloning, sequencing,
expression, and comparison with known enterobacterial ompH
sequences.";
J. Bacteriol. 173:1223-1229(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
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.;
"Systematic sequencing of the Escherichia coli genome: analysis of the
4.0 - 6.0 min (189,987 - 281,416bp) region.";
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
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.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 72-161.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=1987124; DOI=10.1128/jb.173.1.334-344.1991;
Dicker I.B., Seetharam S.R.;
"Cloning and nucleotide sequence of the firA gene and the firA200(Ts)
allele from Escherichia coli.";
J. Bacteriol. 173:334-344(1991).
[8]
PROTEIN SEQUENCE OF 21-32.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[9]
DISCUSSION OF SUBCELLULAR LOCATION.
STRAIN=K12 / JM109 / ATCC 53323;
PubMed=2318304; DOI=10.1016/0014-5793(90)80169-J;
Hirvas L., Coleman J., Koski P., Vaara M.;
"Bacterial 'histone-like protein I' (HLP-I) is an outer membrane
constituent?";
FEBS Lett. 262:123-126(1990).
[10]
SUBCELLULAR LOCATION.
PubMed=1838129; DOI=10.1111/j.1365-2958.1991.tb01990.x;
Thome B.M., Mueller M.;
"Skp is a periplasmic Escherichia coli protein requiring SecA and SecY
for export.";
Mol. Microbiol. 5:2815-2821(1991).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=8730870; DOI=10.1111/j.1365-2958.1996.tb02473.x;
Chen R., Henning U.;
"A periplasmic protein (Skp) of Escherichia coli selectively binds a
class of outer membrane proteins.";
Mol. Microbiol. 19:1287-1294(1996).
[12]
FUNCTION.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=9914480; DOI=10.1046/j.1432-1327.1999.00010.x;
de Cock H., Schaefer U., Potgeter M., Demel R., Mueller M.,
Tommassen J.;
"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(1999).
[13]
FUNCTION.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=10455120; DOI=10.1074/jbc.274.35.24567;
Schaefer U., Beck K., Mueller M.;
"Skp, a molecular chaperone of Gram-negative bacteria, is required for
the formation of soluble periplasmic intermediates of outer membrane
proteins.";
J. Biol. Chem. 274:24567-24574(1999).
[14]
FUNCTION.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=11278858; DOI=10.1074/jbc.M011194200;
Harms N., Koningstein G., Dontje W., Mueller M., Oudega B.,
Luirink J., de Cock H.;
"The early interaction of the outer membrane protein phoE with the
periplasmic chaperone Skp occurs at the cytoplasmic membrane.";
J. Biol. Chem. 276:18804-18811(2001).
[15]
FUNCTION.
PubMed=12509434; DOI=10.1074/jbc.M211177200;
Bulieris P.V., Behrens S., Holst O., Kleinschmidt J.H.;
"Folding and insertion of the outer membrane protein OmpA is assisted
by the chaperone Skp and by lipopolysaccharide.";
J. Biol. Chem. 278:9092-9099(2003).
[16]
SUBUNIT, AND PRELIMINARY X-RAY CRYSTALLOGRAPHY.
STRAIN=K12;
PubMed=15101556; DOI=10.1515/BC.2004.032;
Schlapschy M., Dommel M.K., Hadian K., Fogarasi M., Korndoerfer I.P.,
Skerra A.;
"The periplasmic E. coli chaperone Skp is a trimer in solution:
biophysical and preliminary crystallographic characterization.";
Biol. Chem. 385:137-143(2004).
[17]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-161, AND SUBUNIT.
STRAIN=K12;
PubMed=15304217; DOI=10.1016/j.molcel.2004.07.023;
Walton T.A., Sousa M.C.;
"Crystal structure of Skp, a prefoldin-like chaperone that protects
soluble and membrane proteins from aggregation.";
Mol. Cell 15:367-374(2004).
[18]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 21-161, AND SUBUNIT.
PubMed=15361861; DOI=10.1038/nsmb828;
Korndoerfer I.P., Dommel M.K., Skerra A.;
"Structure of the periplasmic chaperone Skp suggests functional
similarity with cytosolic chaperones despite differing architecture.";
Nat. Struct. Mol. Biol. 11:1015-1020(2004).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:10455120, ECO:0000269|PubMed:11278858,
ECO:0000269|PubMed:12509434, ECO:0000269|PubMed:8730870,
ECO:0000269|PubMed:9914480}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:15101556, ECO:0000269|PubMed:15304217,
ECO:0000269|PubMed:15361861}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-548242, EBI-548242;
P0A910:ompA; NbExp=6; IntAct=EBI-548242, EBI-371347;
P0A917:ompX; NbExp=2; IntAct=EBI-548242, EBI-552413;
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:1838129,
ECO:0000269|PubMed:8730870}.
-!- DOMAIN: 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.
-!- MISCELLANEOUS: Does not require ATP for its activity.
-!- SIMILARITY: Belongs to the Skp family. {ECO:0000305}.
-!- CAUTION: Was originally thought to bind DNA. It was probably an
artifact due to the cationic nature of skp. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M21118; AAA24630.1; -; Genomic_DNA.
EMBL; X75465; CAA53207.1; -; Genomic_DNA.
EMBL; U70214; AAB08607.1; -; Genomic_DNA.
EMBL; U00096; AAC73289.1; -; Genomic_DNA.
EMBL; AP009048; BAA77853.1; -; Genomic_DNA.
EMBL; X54797; CAA38567.1; -; Genomic_DNA.
PIR; JT0304; DNEC17.
RefSeq; NP_414720.1; NC_000913.3.
RefSeq; WP_000758956.1; NZ_LN832404.1.
PDB; 1SG2; X-ray; 2.35 A; A/B/C=20-161.
PDB; 1U2M; X-ray; 2.30 A; A/B/C=21-161.
PDBsum; 1SG2; -.
PDBsum; 1U2M; -.
ProteinModelPortal; P0AEU7; -.
SMR; P0AEU7; -.
BioGrid; 4263427; 241.
DIP; DIP-36210N; -.
IntAct; P0AEU7; 30.
STRING; 316385.ECDH10B_0158; -.
EPD; P0AEU7; -.
PaxDb; P0AEU7; -.
PRIDE; P0AEU7; -.
EnsemblBacteria; AAC73289; AAC73289; b0178.
EnsemblBacteria; BAA77853; BAA77853; BAA77853.
GeneID; 944861; -.
KEGG; ecj:JW0173; -.
KEGG; eco:b0178; -.
PATRIC; fig|1411691.4.peg.2101; -.
EchoBASE; EB0450; -.
EcoGene; EG10455; skp.
eggNOG; ENOG4108RFI; Bacteria.
eggNOG; COG2825; LUCA.
HOGENOM; HOG000261755; -.
KO; K06142; -.
OMA; YINPKHD; -.
PhylomeDB; P0AEU7; -.
BioCyc; EcoCyc:EG10455-MONOMER; -.
BioCyc; MetaCyc:EG10455-MONOMER; -.
EvolutionaryTrace; P0AEU7; -.
PRO; PR:P0AEU7; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; HDA:UniProtKB.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoliWiki.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0001530; F:lipopolysaccharide binding; IPI:EcoCyc.
GO; GO:0051082; F:unfolded protein binding; IPI:EcoCyc.
GO; GO:0061077; P:chaperone-mediated protein folding; IDA:EcoCyc.
GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IDA:EcoCyc.
GO; GO:0006457; P:protein folding; IMP:EcoliWiki.
GO; GO:0032978; P:protein insertion into membrane from inner side; IDA:EcoCyc.
GO; GO:0022417; P:protein maturation by protein folding; IDA:CACAO.
GO; GO:0050821; P:protein stabilization; IDA:EcoCyc.
Gene3D; 3.30.910.20; -; 1.
InterPro; IPR005632; Chaperone_Skp.
InterPro; IPR024930; Skp_dom_sf.
PANTHER; PTHR35089; PTHR35089; 1.
Pfam; PF03938; OmpH; 1.
PIRSF; PIRSF002094; OMP26_Skp; 1.
SMART; SM00935; OmpH; 1.
1: Evidence at protein level;
3D-structure; Chaperone; Complete proteome; Direct protein sequencing;
Periplasm; Reference proteome; Signal.
SIGNAL 1 20 {ECO:0000269|PubMed:2843433,
ECO:0000269|PubMed:9298646}.
CHAIN 21 161 Chaperone protein Skp.
/FTId=PRO_0000020176.
REGION 97 108 Lipopolysaccharide binding.
{ECO:0000255}.
CONFLICT 15 15 A -> L (in Ref. 2; CAA53207).
{ECO:0000305}.
CONFLICT 149 149 V -> E (in Ref. 2; CAA53207).
{ECO:0000305}.
CONFLICT 153 153 T -> I (in Ref. 2; CAA53207).
{ECO:0000305}.
STRAND 24 27 {ECO:0000244|PDB:1U2M}.
HELIX 29 40 {ECO:0000244|PDB:1U2M}.
TURN 41 46 {ECO:0000244|PDB:1U2M}.
HELIX 48 65 {ECO:0000244|PDB:1U2M}.
HELIX 78 90 {ECO:0000244|PDB:1U2M}.
HELIX 92 104 {ECO:0000244|PDB:1U2M}.
HELIX 106 130 {ECO:0000244|PDB:1U2M}.
STRAND 134 138 {ECO:0000244|PDB:1U2M}.
HELIX 139 141 {ECO:0000244|PDB:1U2M}.
STRAND 142 145 {ECO:0000244|PDB:1U2M}.
STRAND 149 151 {ECO:0000244|PDB:1SG2}.
HELIX 153 159 {ECO:0000244|PDB:1U2M}.
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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