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Alkyl hydroperoxide reductase C (EC 1.11.1.15) (Alkyl hydroperoxide reductase protein C22) (Peroxiredoxin) (SCRP-23) (Sulfate starvation-induced protein 8) (SSI8) (Thioredoxin peroxidase)

 AHPC_ECOLI              Reviewed;         187 AA.
P0AE08; P26427;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 109.
RecName: Full=Alkyl hydroperoxide reductase C;
EC=1.11.1.15 {ECO:0000269|PubMed:11717276};
AltName: Full=Alkyl hydroperoxide reductase protein C22;
AltName: Full=Peroxiredoxin;
AltName: Full=SCRP-23;
AltName: Full=Sulfate starvation-induced protein 8;
Short=SSI8;
AltName: Full=Thioredoxin peroxidase;
Name=ahpC; OrderedLocusNames=b0605, JW0598;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=1592833; DOI=10.1128/jb.174.11.3826-3827.1992;
Smillie D.A., Hayward R.S., Suzuki T., Fujita N., Ishihama A.;
"Locations of genes encoding alkyl hydroperoxide reductase on the
physical map of the Escherichia coli K-12 genome.";
J. Bacteriol. 174:3826-3827(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[3]
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.
[4]
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).
[5]
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).
[6]
PROTEIN SEQUENCE OF 2-31.
PubMed=1575737; DOI=10.1016/0006-291X(92)90636-Y;
Ueshima R., Fujita N., Ishihama A.;
"Identification of Escherichia coli proteins cross-reacting with
antibodies against region 2.2 peptide of RNA polymerase sigma
subunit.";
Biochem. Biophys. Res. Commun. 184:634-639(1992).
[7]
PROTEIN SEQUENCE OF 2-28 AND 70-81.
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).
[8]
PROTEIN SEQUENCE OF 2-21, AND SUBCELLULAR LOCATION.
STRAIN=K12;
PubMed=7499381; DOI=10.1074/jbc.270.48.28635;
Cha M.-K., Kim H.-K., Kim I.-H.;
"Thioredoxin-linked 'thiol peroxidase' from periplasmic space of
Escherichia coli.";
J. Biol. Chem. 270:28635-28641(1995).
[9]
PROTEIN SEQUENCE OF 2-14.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J.,
Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A.,
Hochstrasser D.F.;
Submitted (SEP-1994) to UniProtKB.
[10]
PROTEIN SEQUENCE OF 2-11.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=8774726; DOI=10.1111/j.1432-1033.1996.0773u.x;
Quadroni M., Staudenmann W., Kertesz M.A., James P.;
"Analysis of global responses by protein and peptide fingerprinting of
proteins isolated by two-dimensional gel electrophoresis. Application
to the sulfate-starvation response of Escherichia coli.";
Eur. J. Biochem. 239:773-781(1996).
[11]
PROTEIN SEQUENCE OF 2-5.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M.,
Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D.,
Williams K.L., Hochstrasser D.F.;
"Protein identification with N and C-terminal sequence tags in
proteome projects.";
J. Mol. Biol. 278:599-608(1998).
[12]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[13]
FUNCTION.
PubMed=11717276; DOI=10.1128/JB.183.24.7173-7181.2001;
Seaver L.C., Imlay J.A.;
"Alkyl hydroperoxide reductase is the primary scavenger of endogenous
hydrogen peroxide in Escherichia coli.";
J. Bacteriol. 183:7173-7181(2001).
[14]
ROLE IN HYDROXYUREA RESISTANCE, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
Walker G.C.;
"Hydroxyurea induces hydroxyl radical-mediated cell death in
Escherichia coli.";
Mol. Cell 36:845-860(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-93; LYS-153; LYS-169
AND LYS-171, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[16]
SUBUNIT.
PubMed=25372677; DOI=10.1107/S1399004714019233;
Dip P.V., Kamariah N., Subramanian Manimekalai M.S., Nartey W.,
Balakrishna A.M., Eisenhaber F., Eisenhaber B., Grueber G.;
"Structure, mechanism and ensemble formation of the alkylhydroperoxide
reductase subunits AhpC and AhpF from Escherichia coli.";
Acta Crystallogr. D 70:2848-2862(2014).
[17] {ECO:0000244|PDB:5B8A, ECO:0000244|PDB:5B8B}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 162-186, AND DISULFIDE
BONDS.
PubMed=27892488; DOI=10.1038/srep37610;
Kamariah N., Sek M.F., Eisenhaber B., Eisenhaber F., Grueber G.;
"Transition steps in peroxide reduction and a molecular switch for
peroxide robustness of prokaryotic peroxiredoxins.";
Sci. Rep. 6:37610-37610(2016).
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Plays a role in cell protection against
oxidative stress by detoxifying peroxides. Is the primary
scavenger for endogenously generated hydrogen peroxides.
{ECO:0000269|PubMed:11717276}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:11717276}.
-!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
assemble to form a ring-like decamer (PubMed:7499381).
{ECO:0000269|PubMed:7499381}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-547397, EBI-547397;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7499381}.
-!- INDUCTION: Repressed by sulfate or cysteine.
-!- DISRUPTION PHENOTYPE: Increased sensitivity to hydroxyurea,
probably because more reactive oxygen species accumulate.
{ECO:0000269|PubMed:20005847}.
-!- MISCELLANEOUS: The active site is a conserved redox-active
cysteine residue, the peroxidatic cysteine (C(P)), which makes the
nucleophilic attack on the peroxide substrate. The peroxide
oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
then reacts with another cysteine residue, the resolving cysteine
(C(R)), to form a disulfide bridge. The disulfide is subsequently
reduced by an appropriate electron donor to complete the catalytic
cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by
the other dimeric subunit to form an intersubunit disulfide. The
disulfide is subsequently reduced by AhpF.
{ECO:0000250|UniProtKB:P0A251}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D13187; BAA02485.1; -; Genomic_DNA.
EMBL; U82598; AAB40806.1; -; Genomic_DNA.
EMBL; U00096; AAC73706.1; -; Genomic_DNA.
EMBL; AP009048; BAA35235.1; -; Genomic_DNA.
PIR; C64794; JN0289.
RefSeq; NP_415138.1; NC_000913.3.
RefSeq; WP_000052796.1; NZ_LN832404.1.
PDB; 5B8A; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J=1-186.
PDB; 5B8B; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J=1-186.
PDBsum; 5B8A; -.
PDBsum; 5B8B; -.
ProteinModelPortal; P0AE08; -.
SMR; P0AE08; -.
BioGrid; 4259893; 12.
BioGrid; 849610; 1.
DIP; DIP-36164N; -.
IntAct; P0AE08; 36.
MINT; MINT-1241588; -.
STRING; 316385.ECDH10B_0674; -.
PeroxiBase; 4830; EcoAhpC.
iPTMnet; P0AE08; -.
SWISS-2DPAGE; P0AE08; -.
PaxDb; P0AE08; -.
PRIDE; P0AE08; -.
EnsemblBacteria; AAC73706; AAC73706; b0605.
EnsemblBacteria; BAA35235; BAA35235; BAA35235.
GeneID; 945225; -.
KEGG; ecj:JW0598; -.
KEGG; eco:b0605; -.
PATRIC; fig|1411691.4.peg.1663; -.
EchoBASE; EB1357; -.
EcoGene; EG11384; ahpC.
eggNOG; ENOG4105D3R; Bacteria.
eggNOG; COG0450; LUCA.
HOGENOM; HOG000022343; -.
InParanoid; P0AE08; -.
KO; K03386; -.
PhylomeDB; P0AE08; -.
BioCyc; EcoCyc:EG11384-MONOMER; -.
BioCyc; MetaCyc:EG11384-MONOMER; -.
BRENDA; 1.11.1.15; 2026.
PRO; PR:P0AE08; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0009321; C:alkyl hydroperoxide reductase complex; IDA:EcoCyc.
GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0032843; F:hydroperoxide reductase activity; IDA:EcoliWiki.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; IMP:EcoliWiki.
GO; GO:0004601; F:peroxidase activity; IGI:EcoliWiki.
GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0009970; P:cellular response to sulfate starvation; IDA:EcoliWiki.
GO; GO:0033214; P:iron assimilation by chelation and transport; IMP:CACAO.
GO; GO:0033195; P:response to alkyl hydroperoxide; IMP:EcoCyc.
GO; GO:0033194; P:response to hydroperoxide; IMP:EcoCyc.
InterPro; IPR017559; AhpC.
InterPro; IPR000866; AhpC/TSA.
InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
InterPro; IPR019479; Peroxiredoxin_C.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
PANTHER; PTHR10681:SF121; PTHR10681:SF121; 1.
Pfam; PF10417; 1-cysPrx_C; 1.
Pfam; PF00578; AhpC-TSA; 1.
PIRSF; PIRSF000239; AHPC; 1.
SUPFAM; SSF52833; SSF52833; 1.
TIGRFAMs; TIGR03137; AhpC; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Antioxidant; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; Oxidoreductase; Peroxidase;
Redox-active center; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1575737,
ECO:0000269|PubMed:7499381,
ECO:0000269|PubMed:8774726,
ECO:0000269|PubMed:9298646,
ECO:0000269|PubMed:9600841,
ECO:0000269|Ref.9}.
CHAIN 2 187 Alkyl hydroperoxide reductase C.
/FTId=PRO_0000135115.
DOMAIN 2 157 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 47 47 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000305|PubMed:27892488}.
MOD_RES 17 17 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 93 93 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 153 153 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 169 169 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 171 171 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
DISULFID 47 47 Interchain (with C-166); in linked form.
{ECO:0000244|PDB:5B8A,
ECO:0000269|PubMed:27892488}.
DISULFID 166 166 Interchain (with C-47); in linked form.
{ECO:0000244|PDB:5B8A,
ECO:0000269|PubMed:27892488}.
STRAND 12 17 {ECO:0000244|PDB:5B8A}.
STRAND 20 25 {ECO:0000244|PDB:5B8A}.
HELIX 26 29 {ECO:0000244|PDB:5B8A}.
STRAND 32 38 {ECO:0000244|PDB:5B8A}.
HELIX 49 56 {ECO:0000244|PDB:5B8A}.
HELIX 58 63 {ECO:0000244|PDB:5B8A}.
STRAND 66 74 {ECO:0000244|PDB:5B8A}.
HELIX 76 85 {ECO:0000244|PDB:5B8A}.
HELIX 87 90 {ECO:0000244|PDB:5B8A}.
STRAND 94 98 {ECO:0000244|PDB:5B8A}.
HELIX 103 107 {ECO:0000244|PDB:5B8A}.
TURN 113 116 {ECO:0000244|PDB:5B8A}.
STRAND 120 125 {ECO:0000244|PDB:5B8A}.
STRAND 129 137 {ECO:0000244|PDB:5B8A}.
HELIX 145 159 {ECO:0000244|PDB:5B8A}.
STRAND 172 174 {ECO:0000244|PDB:5B8A}.
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


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