AHPC_ECOLI
ID AHPC_ECOLI Reviewed; 187 AA.
AC P0AE08; P26427;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Alkyl hydroperoxide reductase C;
DE EC=1.11.1.26 {ECO:0000269|PubMed:11717276};
DE AltName: Full=Alkyl hydroperoxide reductase protein C22;
DE AltName: Full=Peroxiredoxin;
DE AltName: Full=SCRP-23;
DE AltName: Full=Sulfate starvation-induced protein 8;
DE Short=SSI8;
DE AltName: Full=Thioredoxin peroxidase;
GN Name=ahpC; OrderedLocusNames=b0605, JW0598;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1592833; DOI=10.1128/jb.174.11.3826-3827.1992;
RA Smillie D.A., Hayward R.S., Suzuki T., Fujita N., Ishihama A.;
RT "Locations of genes encoding alkyl hydroperoxide reductase on the physical
RT map of the Escherichia coli K-12 genome.";
RL J. Bacteriol. 174:3826-3827(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
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 [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 2-31.
RX PubMed=1575737; DOI=10.1016/0006-291x(92)90636-y;
RA Ueshima R., Fujita N., Ishihama A.;
RT "Identification of Escherichia coli proteins cross-reacting with antibodies
RT against region 2.2 peptide of RNA polymerase sigma subunit.";
RL Biochem. Biophys. Res. Commun. 184:634-639(1992).
RN [7]
RP PROTEIN SEQUENCE OF 2-28 AND 70-81.
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 [8]
RP PROTEIN SEQUENCE OF 2-21, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=7499381; DOI=10.1074/jbc.270.48.28635;
RA Cha M.-K., Kim H.-K., Kim I.-H.;
RT "Thioredoxin-linked 'thiol peroxidase' from periplasmic space of
RT Escherichia coli.";
RL J. Biol. Chem. 270:28635-28641(1995).
RN [9]
RP PROTEIN SEQUENCE OF 2-14.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL Submitted (SEP-1994) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 2-11.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8774726; DOI=10.1111/j.1432-1033.1996.0773u.x;
RA Quadroni M., Staudenmann W., Kertesz M.A., James P.;
RT "Analysis of global responses by protein and peptide fingerprinting of
RT proteins isolated by two-dimensional gel electrophoresis. Application to
RT the sulfate-starvation response of Escherichia coli.";
RL Eur. J. Biochem. 239:773-781(1996).
RN [11]
RP PROTEIN SEQUENCE OF 2-5.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [12]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [13]
RP FUNCTION.
RX PubMed=11717276; DOI=10.1128/jb.183.24.7173-7181.2001;
RA Seaver L.C., Imlay J.A.;
RT "Alkyl hydroperoxide reductase is the primary scavenger of endogenous
RT hydrogen peroxide in Escherichia coli.";
RL J. Bacteriol. 183:7173-7181(2001).
RN [14]
RP ROLE IN HYDROXYUREA RESISTANCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-93; LYS-153; LYS-169 AND
RP LYS-171, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [16]
RP SUBUNIT.
RX PubMed=25372677; DOI=10.1107/s1399004714019233;
RA Dip P.V., Kamariah N., Subramanian Manimekalai M.S., Nartey W.,
RA Balakrishna A.M., Eisenhaber F., Eisenhaber B., Grueber G.;
RT "Structure, mechanism and ensemble formation of the alkylhydroperoxide
RT reductase subunits AhpC and AhpF from Escherichia coli.";
RL Acta Crystallogr. D 70:2848-2862(2014).
RN [17] {ECO:0007744|PDB:5B8A, ECO:0007744|PDB:5B8B}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 162-186, AND DISULFIDE BONDS.
RX PubMed=27892488; DOI=10.1038/srep37610;
RA Kamariah N., Sek M.F., Eisenhaber B., Eisenhaber F., Grueber G.;
RT "Transition steps in peroxide reduction and a molecular switch for peroxide
RT robustness of prokaryotic peroxiredoxins.";
RL Sci. Rep. 6:37610-37610(2016).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides. Is the primary scavenger for endogenously
CC generated hydrogen peroxides. {ECO:0000269|PubMed:11717276}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hydroperoxide + H(+) + NADH = an alcohol + H2O + NAD(+);
CC Xref=Rhea:RHEA:62628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.11.1.26;
CC Evidence={ECO:0000269|PubMed:11717276};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
CC assemble to form a ring-like decamer (PubMed:7499381).
CC {ECO:0000269|PubMed:7499381}.
CC -!- INTERACTION:
CC P0AE08; P0AE08: ahpC; NbExp=2; IntAct=EBI-547397, EBI-547397;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7499381}.
CC -!- INDUCTION: Repressed by sulfate or cysteine.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to hydroxyurea, probably
CC because more reactive oxygen species accumulate.
CC {ECO:0000269|PubMed:20005847}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this typical 2-Cys
CC peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC intersubunit disulfide. The disulfide is subsequently reduced by AhpF.
CC {ECO:0000250|UniProtKB:P0A251}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D13187; BAA02485.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40806.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73706.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35235.1; -; Genomic_DNA.
DR PIR; C64794; JN0289.
DR RefSeq; NP_415138.1; NC_000913.3.
DR RefSeq; WP_000052796.1; NZ_STEB01000031.1.
DR PDB; 5B8A; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J=1-186.
DR PDB; 5B8B; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J=1-186.
DR PDBsum; 5B8A; -.
DR PDBsum; 5B8B; -.
DR AlphaFoldDB; P0AE08; -.
DR SMR; P0AE08; -.
DR BioGRID; 4259893; 40.
DR BioGRID; 849610; 4.
DR ComplexPortal; CPX-4862; Alkyl hydroperoxide reductase complex.
DR DIP; DIP-36164N; -.
DR IntAct; P0AE08; 36.
DR STRING; 511145.b0605; -.
DR PeroxiBase; 4830; EcoAhpC.
DR iPTMnet; P0AE08; -.
DR SWISS-2DPAGE; P0AE08; -.
DR jPOST; P0AE08; -.
DR PaxDb; P0AE08; -.
DR PRIDE; P0AE08; -.
DR EnsemblBacteria; AAC73706; AAC73706; b0605.
DR EnsemblBacteria; BAA35235; BAA35235; BAA35235.
DR GeneID; 66671119; -.
DR GeneID; 945225; -.
DR KEGG; ecj:JW0598; -.
DR KEGG; eco:b0605; -.
DR PATRIC; fig|1411691.4.peg.1663; -.
DR EchoBASE; EB1357; -.
DR eggNOG; COG0450; Bacteria.
DR HOGENOM; CLU_042529_21_3_6; -.
DR InParanoid; P0AE08; -.
DR OMA; FWYPKDF; -.
DR PhylomeDB; P0AE08; -.
DR BioCyc; EcoCyc:EG11384-MON; -.
DR BioCyc; MetaCyc:EG11384-MON; -.
DR BRENDA; 1.11.1.26; 2026.
DR PRO; PR:P0AE08; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009321; C:alkyl hydroperoxide reductase complex; IDA:EcoCyc.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0102039; F:alkylhydroperoxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0032843; F:hydroperoxide reductase activity; IDA:EcoliWiki.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; IMP:EcoliWiki.
DR GO; GO:0004601; F:peroxidase activity; IGI:EcoliWiki.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0009970; P:cellular response to sulfate starvation; IDA:EcoliWiki.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:ComplexPortal.
DR GO; GO:0033195; P:response to alkyl hydroperoxide; IMP:EcoCyc.
DR GO; GO:0033194; P:response to hydroperoxide; IMP:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IC:ComplexPortal.
DR GO; GO:0019290; P:siderophore biosynthetic process; IMP:CACAO.
DR InterPro; IPR017559; AhpC.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681:SF121; PTHR10681:SF121; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR03137; AhpC; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Antioxidant; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Oxidoreductase; Peroxidase;
KW Redox-active center; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1575737,
FT ECO:0000269|PubMed:7499381, ECO:0000269|PubMed:8774726,
FT ECO:0000269|PubMed:9298646, ECO:0000269|PubMed:9600841,
FT ECO:0000269|Ref.9"
FT CHAIN 2..187
FT /note="Alkyl hydroperoxide reductase C"
FT /id="PRO_0000135115"
FT DOMAIN 2..157
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 47
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000305|PubMed:27892488"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 93
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 153
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 169
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 171
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT DISULFID 47
FT /note="Interchain (with C-166); in linked form"
FT /evidence="ECO:0000269|PubMed:27892488,
FT ECO:0007744|PDB:5B8A"
FT DISULFID 166
FT /note="Interchain (with C-47); in linked form"
FT /evidence="ECO:0000269|PubMed:27892488,
FT ECO:0007744|PDB:5B8A"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:5B8A"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:5B8A"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:5B8A"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:5B8A"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:5B8A"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:5B8A"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:5B8A"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:5B8A"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:5B8A"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:5B8A"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:5B8A"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:5B8A"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:5B8A"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:5B8A"
FT HELIX 145..159
FT /evidence="ECO:0007829|PDB:5B8A"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:5B8A"
SQ SEQUENCE 187 AA; 20761 MW; 40AB796E6F5CC2D6 CRC64;
MSLINTKIKP FKNQAFKNGE FIEITEKDTE GRWSVFFFYP ADFTFVCPTE LGDVADHYEE
LQKLGVDVYA VSTDTHFTHK AWHSSSETIA KIKYAMIGDP TGALTRNFDN MREDEGLADR
ATFVVDPQGI IQAIEVTAEG IGRDASDLLR KIKAAQYVAS HPGEVCPAKW KEGEATLAPS
LDLVGKI
