CNOX_ECOLI
ID CNOX_ECOLI Reviewed; 284 AA.
AC P77395; Q2MBT5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Chaperedoxin {ECO:0000303|PubMed:29754824};
DE AltName: Full=Heat shock protein CnoX {ECO:0000303|PubMed:29754824};
DE AltName: Full=Trxsc {ECO:0000303|PubMed:16563353};
GN Name=cnoX {ECO:0000303|PubMed:29754824}; Synonyms=ybbN;
GN OrderedLocusNames=b0492, JW5067;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
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 [4]
RP FUNCTION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16563353; DOI=10.1016/j.bbrc.2006.03.028;
RA Caldas T., Malki A., Kern R., Abdallah J., Richarme G.;
RT "The Escherichia coli thioredoxin homolog YbbN/Trxsc is a chaperone and a
RT weak protein oxidoreductase.";
RL Biochem. Biophys. Res. Commun. 343:780-786(2006).
RN [5]
RP FUNCTION, INTERACTION WITH DNAK AND GROEL, AND DISRUPTION PHENOTYPE.
RX PubMed=18657513; DOI=10.1016/j.bbrc.2008.07.080;
RA Kthiri F., Le H.T., Tagourti J., Kern R., Malki A., Caldas T., Abdallah J.,
RA Landoulsi A., Richarme G.;
RT "The thioredoxin homolog YbbN functions as a chaperone rather than as an
RT oxidoreductase.";
RL Biochem. Biophys. Res. Commun. 374:668-672(2008).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=21195694; DOI=10.1016/j.bbrc.2010.12.122;
RA Le H.T., Gautier V., Kthiri F., Kohiyama M., Katayama T., Richarme G.;
RT "DNA replication defects in a mutant deficient in the thioredoxin homolog
RT YbbN.";
RL Biochem. Biophys. Res. Commun. 405:52-57(2011).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP CYS-38 AND CYS-63.
RX PubMed=29754824; DOI=10.1016/j.molcel.2018.04.002;
RA Goemans C.V., Vertommen D., Agrebi R., Collet J.F.;
RT "CnoX is a chaperedoxin: a holdase that protects its substrates from
RT irreversible oxidation.";
RL Mol. Cell 70:614-627(2018).
RN [8] {ECO:0007744|PDB:3QOU}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), FUNCTION, SUBUNIT, AND DOMAIN.
RX PubMed=21498507; DOI=10.1074/jbc.m111.238741;
RA Lin J., Wilson M.A.;
RT "Escherichia coli thioredoxin-like protein YbbN contains an atypical
RT tetratricopeptide repeat motif and is a negative regulator of GroEL.";
RL J. Biol. Chem. 286:19459-19469(2011).
CC -!- FUNCTION: Chaperedoxin that combines a chaperone activity with a redox-
CC protective function (PubMed:16563353, PubMed:18657513,
CC PubMed:29754824). Involved in the protection against hypochlorous acid
CC (HOCl), the active ingredient of bleach, which kills bacteria by
CC causing protein aggregation (PubMed:29754824). Functions as an
CC efficient holdase chaperone that protects the substrates of the major
CC folding systems GroEL/GroES and DnaK/DnaJ/GrpE from aggregation. In
CC addition, it prevents the irreversible oxidation of its substrates
CC through the formation of mixed disulfide complexes (PubMed:29754824).
CC After bleach stress, it transfers its substrates to the GroEL/GroES and
CC DnaK/DnaJ/GrpE foldases (PubMed:29754824). Lacks oxidoreductase
CC activity (PubMed:21498507, PubMed:29754824).
CC {ECO:0000269|PubMed:16563353, ECO:0000269|PubMed:18657513,
CC ECO:0000269|PubMed:21498507, ECO:0000269|PubMed:29754824}.
CC -!- ACTIVITY REGULATION: The holdase activity is activated by HOCl, via the
CC reversible chlorination of several residues in the TPR domain.
CC Chorination probably increases the hydrophobicity of CnoX and enables
CC it to bind a variety of substrates. Reduced glutathione (GSH) is
CC required to resolve CnoX-substrate complexes.
CC {ECO:0000269|PubMed:29754824}.
CC -!- SUBUNIT: Interacts with a variety of proteins, including multiple
CC ribosomal protein subunits, DnaK and GroEL (PubMed:18657513,
CC PubMed:21498507). The reduced protein is monomeric in solution
CC (PubMed:21498507). Upon oxidation, its oligomeric state changes to
CC tetramers and higher oligomers (PubMed:16563353).
CC {ECO:0000269|PubMed:16563353, ECO:0000269|PubMed:18657513,
CC ECO:0000269|PubMed:21498507}.
CC -!- INTERACTION:
CC P77395; P0A988: dnaN; NbExp=2; IntAct=EBI-545297, EBI-542385;
CC -!- DOMAIN: Contains an N-terminal mobile Trx domain and four atypical
CC tetratricopeptide repeat (TPR) motifs in the C-terminal region. The Trx
CC domain lacks the canonical Cys-x-x-Cys active site of thioredoxins and
CC is not a functional oxidoreductase. {ECO:0000269|PubMed:21498507}.
CC -!- DISRUPTION PHENOTYPE: Mutant is highly sensitive to HOCl
CC (PubMed:29754824). Disruption mutant displays increased sensitivity to
CC heat stress, but not to oxidative, UV, osmotic and pH stresses.
CC Mutation does not affect the redox state of cytoplasmic, membrane and
CC periplasmic proteins, but mutant shows a decreased expression of
CC several cytoplasmic proteins (PubMed:18657513). Mutant displays
CC overinitiation, hypermutator and filamentation phenotypes with the
CC occurrence of anucleated cells (PubMed:21195694).
CC {ECO:0000269|PubMed:18657513, ECO:0000269|PubMed:21195694,
CC ECO:0000269|PubMed:29754824}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40246.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U82664; AAB40246.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73594.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76271.1; -; Genomic_DNA.
DR PIR; C64780; C64780.
DR RefSeq; NP_415025.4; NC_000913.3.
DR RefSeq; WP_001300573.1; NZ_SSZK01000009.1.
DR PDB; 3QOU; X-ray; 1.80 A; A=1-284.
DR PDBsum; 3QOU; -.
DR AlphaFoldDB; P77395; -.
DR SMR; P77395; -.
DR BioGRID; 4259853; 9.
DR DIP; DIP-11322N; -.
DR IntAct; P77395; 7.
DR STRING; 511145.b0492; -.
DR SWISS-2DPAGE; P77395; -.
DR jPOST; P77395; -.
DR PaxDb; P77395; -.
DR PRIDE; P77395; -.
DR EnsemblBacteria; AAC73594; AAC73594; b0492.
DR EnsemblBacteria; BAE76271; BAE76271; BAE76271.
DR GeneID; 947119; -.
DR KEGG; ecj:JW5067; -.
DR KEGG; eco:b0492; -.
DR PATRIC; fig|1411691.4.peg.1784; -.
DR EchoBASE; EB3049; -.
DR eggNOG; COG3118; Bacteria.
DR HOGENOM; CLU_046120_1_0_6; -.
DR InParanoid; P77395; -.
DR OMA; QPRNMSM; -.
DR PhylomeDB; P77395; -.
DR BioCyc; EcoCyc:G6268-MON; -.
DR EvolutionaryTrace; P77395; -.
DR PRO; PR:P77395; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0051082; F:unfolded protein binding; IDA:EcoCyc.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:EcoCyc.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:EcoCyc.
DR GO; GO:0036506; P:maintenance of unfolded protein; IDA:EcoCyc.
DR GO; GO:0042026; P:protein refolding; IDA:EcoCyc.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Disulfide bond; Reference proteome;
KW Stress response.
FT CHAIN 1..284
FT /note="Chaperedoxin"
FT /id="PRO_0000168640"
FT DOMAIN 2..111
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 63
FT /note="Interchain (with substrate)"
FT /evidence="ECO:0000269|PubMed:29754824"
FT MUTAGEN 38
FT /note="C->A: Still fully activated as a holdase by HOCl;
FT when associated with A-63."
FT /evidence="ECO:0000269|PubMed:29754824"
FT MUTAGEN 63
FT /note="C->A: Cannot form mixed disulfides with its
FT substrates. Still fully activated as a holdase by HOCl;
FT when associated with A-38."
FT /evidence="ECO:0000269|PubMed:29754824"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:3QOU"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 14..18
FT /evidence="ECO:0007829|PDB:3QOU"
FT TURN 19..23
FT /evidence="ECO:0007829|PDB:3QOU"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:3QOU"
FT TURN 36..41
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:3QOU"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:3QOU"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:3QOU"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:3QOU"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:3QOU"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 216..228
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 232..244
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:3QOU"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 258..265
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:3QOU"
FT HELIX 276..283
FT /evidence="ECO:0007829|PDB:3QOU"
SQ SEQUENCE 284 AA; 31791 MW; B09092A90F0588B2 CRC64;
MSVENIVNIN ESNLQQVLEQ SMTTPVLFYF WSERSQHCLQ LTPILESLAA QYNGQFILAK
LDCDAEQMIA AQFGLRAIPT VYLFQNGQPV DGFQGPQPEE AIRALLDKVL PREEELKAQQ
AMQLMQESNY TDALPLLKDA WQLSNQNGEI GLLLAETLIA LNRSEDAEAV LKTIPLQDQD
TRYQGLVAQI ELLKQAADTP EIQQLQQQVA ENPEDAALAT QLALQLHQVG RNEEALELLF
GHLRKDLTAA DGQTRKTFQE ILAALGTGDA LASKYRRQLY ALLY
