SKP_ECOLI
ID SKP_ECOLI Reviewed; 161 AA.
AC P0AEU7; P11457;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Chaperone protein Skp;
DE AltName: Full=DNA-binding 17 kDa protein;
DE AltName: Full=Histone-like protein HLP-1;
DE AltName: Full=Seventeen kilodalton protein;
DE Flags: Precursor;
GN Name=skp; Synonyms=hlpA, ompH; OrderedLocusNames=b0178, JW0173;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 21-40.
RX PubMed=2843433; DOI=10.1016/0378-1119(88)90014-5;
RA Holck A., Kleppe K.;
RT "Cloning and sequencing of the gene for the DNA-binding 17K protein of
RT Escherichia coli.";
RL Gene 67:117-124(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1991717; DOI=10.1128/jb.173.3.1223-1229.1991;
RA Hirvas L., Koski P., Vaara M.;
RT "The ompH gene of Yersinia enterocolitica: cloning, sequencing, expression,
RT and comparison with known enterobacterial ompH sequences.";
RL J. Bacteriol. 173:1223-1229(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 72-161.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1987124; DOI=10.1128/jb.173.1.334-344.1991;
RA Dicker I.B., Seetharam S.R.;
RT "Cloning and nucleotide sequence of the firA gene and the firA200(Ts)
RT allele from Escherichia coli.";
RL J. Bacteriol. 173:334-344(1991).
RN [8]
RP PROTEIN SEQUENCE OF 21-32.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [9]
RP DISCUSSION OF SUBCELLULAR LOCATION.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=2318304; DOI=10.1016/0014-5793(90)80169-j;
RA Hirvas L., Coleman J., Koski P., Vaara M.;
RT "Bacterial 'histone-like protein I' (HLP-I) is an outer membrane
RT constituent?";
RL FEBS Lett. 262:123-126(1990).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=1838129; DOI=10.1111/j.1365-2958.1991.tb01990.x;
RA Thome B.M., Mueller M.;
RT "Skp is a periplasmic Escherichia coli protein requiring SecA and SecY for
RT export.";
RL Mol. Microbiol. 5:2815-2821(1991).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8730870; DOI=10.1111/j.1365-2958.1996.tb02473.x;
RA Chen R., Henning U.;
RT "A periplasmic protein (Skp) of Escherichia coli selectively binds a class
RT of outer membrane proteins.";
RL Mol. Microbiol. 19:1287-1294(1996).
RN [12]
RP FUNCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=9914480; DOI=10.1046/j.1432-1327.1999.00010.x;
RA de Cock H., Schaefer U., Potgeter M., Demel R., Mueller M., Tommassen J.;
RT "Affinity of the periplasmic chaperone Skp of Escherichia coli for
RT phospholipids, lipopolysaccharides and non-native outer membrane proteins.
RT Role of Skp in the biogenesis of outer membrane protein.";
RL Eur. J. Biochem. 259:96-103(1999).
RN [13]
RP FUNCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=10455120; DOI=10.1074/jbc.274.35.24567;
RA Schaefer U., Beck K., Mueller M.;
RT "Skp, a molecular chaperone of Gram-negative bacteria, is required for the
RT formation of soluble periplasmic intermediates of outer membrane
RT proteins.";
RL J. Biol. Chem. 274:24567-24574(1999).
RN [14]
RP FUNCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11278858; DOI=10.1074/jbc.m011194200;
RA Harms N., Koningstein G., Dontje W., Mueller M., Oudega B., Luirink J.,
RA de Cock H.;
RT "The early interaction of the outer membrane protein phoE with the
RT periplasmic chaperone Skp occurs at the cytoplasmic membrane.";
RL J. Biol. Chem. 276:18804-18811(2001).
RN [15]
RP FUNCTION.
RX PubMed=12509434; DOI=10.1074/jbc.m211177200;
RA Bulieris P.V., Behrens S., Holst O., Kleinschmidt J.H.;
RT "Folding and insertion of the outer membrane protein OmpA is assisted by
RT the chaperone Skp and by lipopolysaccharide.";
RL J. Biol. Chem. 278:9092-9099(2003).
RN [16]
RP SUBUNIT, AND PRELIMINARY X-RAY CRYSTALLOGRAPHY.
RC STRAIN=K12;
RX PubMed=15101556; DOI=10.1515/bc.2004.032;
RA Schlapschy M., Dommel M.K., Hadian K., Fogarasi M., Korndoerfer I.P.,
RA Skerra A.;
RT "The periplasmic E. coli chaperone Skp is a trimer in solution: biophysical
RT and preliminary crystallographic characterization.";
RL Biol. Chem. 385:137-143(2004).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-161, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=15304217; DOI=10.1016/j.molcel.2004.07.023;
RA Walton T.A., Sousa M.C.;
RT "Crystal structure of Skp, a prefoldin-like chaperone that protects soluble
RT and membrane proteins from aggregation.";
RL Mol. Cell 15:367-374(2004).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 21-161, AND SUBUNIT.
RX PubMed=15361861; DOI=10.1038/nsmb828;
RA Korndoerfer I.P., Dommel M.K., Skerra A.;
RT "Structure of the periplasmic chaperone Skp suggests functional similarity
RT with cytosolic chaperones despite differing architecture.";
RL Nat. Struct. Mol. Biol. 11:1015-1020(2004).
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. Required for the
CC efficient release of OmpA from the inner membrane, the maintenance of
CC its solubility in the periplasm, and, in association with
CC lipopolysaccharide (LPS), for the efficient folding and insertion of
CC OmpA into the outer membrane. {ECO:0000269|PubMed:10455120,
CC ECO:0000269|PubMed:11278858, ECO:0000269|PubMed:12509434,
CC ECO:0000269|PubMed:8730870, ECO:0000269|PubMed:9914480}.
CC -!- SUBUNIT: Homotrimer. Interacts with OmpA. Interacts with PhoE during
CC its translocation across the inner membrane, but, in contrast to OmpA,
CC release of PhoE from the inner membrane is not dependent on skp.
CC Interacts also with LamB, OmpC and OmpF. {ECO:0000269|PubMed:15101556,
CC ECO:0000269|PubMed:15304217, ECO:0000269|PubMed:15361861}.
CC -!- INTERACTION:
CC P0AEU7; P0A910: ompA; NbExp=6; IntAct=EBI-548242, EBI-371347;
CC P0AEU7; P0A917: ompX; NbExp=2; IntAct=EBI-548242, EBI-552413;
CC P0AEU7; P0AEU7: skp; NbExp=3; IntAct=EBI-548242, EBI-548242;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:1838129,
CC ECO:0000269|PubMed:8730870}.
CC -!- DOMAIN: Composed of a compact central beta-barrel domain with long
CC alpha-helical extensions that form a three-pronged structure around an
CC internal cavity. Substrate proteins may be bound in this cavity.
CC -!- MISCELLANEOUS: Does not require ATP for its activity.
CC -!- SIMILARITY: Belongs to the Skp family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to bind DNA. It was probably an
CC artifact due to the cationic nature of skp. {ECO:0000305}.
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DR EMBL; M21118; AAA24630.1; -; Genomic_DNA.
DR EMBL; X75465; CAA53207.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08607.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73289.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77853.1; -; Genomic_DNA.
DR EMBL; X54797; CAA38567.1; -; Genomic_DNA.
DR PIR; JT0304; DNEC17.
DR RefSeq; NP_414720.1; NC_000913.3.
DR RefSeq; WP_000758956.1; NZ_STEB01000032.1.
DR PDB; 1SG2; X-ray; 2.35 A; A/B/C=20-161.
DR PDB; 1U2M; X-ray; 2.30 A; A/B/C=21-161.
DR PDBsum; 1SG2; -.
DR PDBsum; 1U2M; -.
DR AlphaFoldDB; P0AEU7; -.
DR BMRB; P0AEU7; -.
DR SASBDB; P0AEU7; -.
DR SMR; P0AEU7; -.
DR BioGRID; 4263427; 241.
DR DIP; DIP-36210N; -.
DR IntAct; P0AEU7; 31.
DR STRING; 511145.b0178; -.
DR jPOST; P0AEU7; -.
DR PaxDb; P0AEU7; -.
DR PRIDE; P0AEU7; -.
DR EnsemblBacteria; AAC73289; AAC73289; b0178.
DR EnsemblBacteria; BAA77853; BAA77853; BAA77853.
DR GeneID; 67416254; -.
DR GeneID; 944861; -.
DR KEGG; ecj:JW0173; -.
DR KEGG; eco:b0178; -.
DR PATRIC; fig|1411691.4.peg.2101; -.
DR EchoBASE; EB0450; -.
DR eggNOG; COG2825; Bacteria.
DR HOGENOM; CLU_101388_2_0_6; -.
DR OMA; EKEQYDM; -.
DR PhylomeDB; P0AEU7; -.
DR BioCyc; EcoCyc:EG10455-MON; -.
DR BioCyc; MetaCyc:EG10455-MON; -.
DR EvolutionaryTrace; P0AEU7; -.
DR PRO; PR:P0AEU7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoliWiki.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:EcoCyc.
DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IDA:EcoCyc.
DR GO; GO:0006457; P:protein folding; IMP:EcoliWiki.
DR GO; GO:0032978; P:protein insertion into membrane from inner side; IDA:EcoCyc.
DR GO; GO:0022417; P:protein maturation by protein folding; IDA:CACAO.
DR GO; GO:0050821; P:protein stabilization; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Direct protein sequencing; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:2843433,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 21..161
FT /note="Chaperone protein Skp"
FT /id="PRO_0000020176"
FT REGION 97..108
FT /note="Lipopolysaccharide binding"
FT /evidence="ECO:0000255"
FT CONFLICT 15
FT /note="A -> L (in Ref. 2; CAA53207)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="V -> E (in Ref. 2; CAA53207)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="T -> I (in Ref. 2; CAA53207)"
FT /evidence="ECO:0000305"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:1U2M"
FT HELIX 29..40
FT /evidence="ECO:0007829|PDB:1U2M"
FT TURN 41..46
FT /evidence="ECO:0007829|PDB:1U2M"
FT HELIX 48..65
FT /evidence="ECO:0007829|PDB:1U2M"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:1U2M"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:1U2M"
FT HELIX 106..130
FT /evidence="ECO:0007829|PDB:1U2M"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:1U2M"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1U2M"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1U2M"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1SG2"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:1U2M"
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
