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Protein

Alkyl hydroperoxide reductase subunit C

Gene

ahpC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Directly reduces organic hydroperoxides in its reduced dithiol form.

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei47 – 471Cysteine sulfenic acid (-SOH) intermediateBy similarity

GO - Molecular functioni

  • hydroperoxide reductase activity Source: EcoliWiki
  • identical protein binding Source: IntAct
  • oxidoreductase activity, acting on peroxide as acceptor Source: EcoliWiki
  • peroxidase activity Source: EcoliWiki
  • peroxiredoxin activity Source: UniProtKB-EC

GO - Biological processi

  • cellular response to sulfate starvation Source: EcoliWiki
  • iron assimilation by chelation and transport Source: CACAO
  • response to alkyl hydroperoxide Source: EcoCyc
  • response to hydroperoxide Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciEcoCyc:EG11384-MONOMER.
ECOL316407:JW0598-MONOMER.
MetaCyc:EG11384-MONOMER.
BRENDAi1.11.1.15. 2026.

Protein family/group databases

PeroxiBasei4830. EcoAhpC.

Names & Taxonomyi

Protein namesi
Recommended name:
Alkyl hydroperoxide reductase subunit C (EC:1.11.1.15)
Alternative name(s):
Alkyl hydroperoxide reductase protein C22
Peroxiredoxin
SCRP-23
Sulfate starvation-induced protein 8
Short name:
SSI8
Thioredoxin peroxidase
Gene namesi
Name:ahpC
Ordered Locus Names:b0605, JW0598
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11384. ahpC.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Increased sensitivity to hydroxyurea, probably because more reactive oxygen species accumulate.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed6 Publications
Chaini2 – 187186Alkyl hydroperoxide reductase subunit CPRO_0000135115Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171N6-acetyllysine1 Publication
Disulfide bondi47 – 47Interchain (with C-166); in linked formBy similarity
Modified residuei93 – 931N6-acetyllysine1 Publication
Modified residuei153 – 1531N6-acetyllysine1 Publication
Disulfide bondi166 – 166Interchain (with C-47); in linked formBy similarity
Modified residuei169 – 1691N6-acetyllysine1 Publication
Modified residuei171 – 1711N6-acetyllysine1 Publication

Post-translational modificationi

The Cys-47-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-47 (probably Cys-SOH) rapidly reacts with Cys-166-SH of the other subunit to form an intermolecular disulfide. This disulfide is subsequently reduced by thioredoxin (By similarity).By similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiP0AE08.
PRIDEiP0AE08.

2D gel databases

SWISS-2DPAGEP0AE08.

Expressioni

Inductioni

Repressed by sulfate or cysteine.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-547397,EBI-547397

Protein-protein interaction databases

BioGridi849610. 1 interaction.
DIPiDIP-36164N.
IntActiP0AE08. 33 interactions.
MINTiMINT-1241588.
STRINGi511145.b0605.

Structurei

3D structure databases

ProteinModelPortaliP0AE08.
SMRiP0AE08. Positions 1-167.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 157156ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the AhpC/TSA family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0450.
HOGENOMiHOG000022343.
InParanoidiP0AE08.
KOiK03386.
OMAiFHKGEFV.
OrthoDBiEOG67X1XH.
PhylomeDBiP0AE08.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR017559. AhpC.
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR03137. AhpC. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AE08-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLINTKIKP FKNQAFKNGE FIEITEKDTE GRWSVFFFYP ADFTFVCPTE
60 70 80 90 100
LGDVADHYEE LQKLGVDVYA VSTDTHFTHK AWHSSSETIA KIKYAMIGDP
110 120 130 140 150
TGALTRNFDN MREDEGLADR ATFVVDPQGI IQAIEVTAEG IGRDASDLLR
160 170 180
KIKAAQYVAS HPGEVCPAKW KEGEATLAPS LDLVGKI
Length:187
Mass (Da):20,761
Last modified:January 23, 2007 - v2
Checksum:i40AB796E6F5CC2D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13187 Genomic DNA. Translation: BAA02485.1.
U82598 Genomic DNA. Translation: AAB40806.1.
U00096 Genomic DNA. Translation: AAC73706.1.
AP009048 Genomic DNA. Translation: BAA35235.1.
PIRiC64794. JN0289.
RefSeqiNP_415138.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC73706; AAC73706; b0605.
BAA35235; BAA35235; BAA35235.
GeneIDi945225.
KEGGiecj:Y75_p0595.
eco:b0605.
PATRICi32116388. VBIEscCol129921_0634.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13187 Genomic DNA. Translation: BAA02485.1.
U82598 Genomic DNA. Translation: AAB40806.1.
U00096 Genomic DNA. Translation: AAC73706.1.
AP009048 Genomic DNA. Translation: BAA35235.1.
PIRiC64794. JN0289.
RefSeqiNP_415138.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP0AE08.
SMRiP0AE08. Positions 1-167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi849610. 1 interaction.
DIPiDIP-36164N.
IntActiP0AE08. 33 interactions.
MINTiMINT-1241588.
STRINGi511145.b0605.

Protein family/group databases

PeroxiBasei4830. EcoAhpC.

2D gel databases

SWISS-2DPAGEP0AE08.

Proteomic databases

PaxDbiP0AE08.
PRIDEiP0AE08.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73706; AAC73706; b0605.
BAA35235; BAA35235; BAA35235.
GeneIDi945225.
KEGGiecj:Y75_p0595.
eco:b0605.
PATRICi32116388. VBIEscCol129921_0634.

Organism-specific databases

EchoBASEiEB1357.
EcoGeneiEG11384. ahpC.

Phylogenomic databases

eggNOGiCOG0450.
HOGENOMiHOG000022343.
InParanoidiP0AE08.
KOiK03386.
OMAiFHKGEFV.
OrthoDBiEOG67X1XH.
PhylomeDBiP0AE08.

Enzyme and pathway databases

BioCyciEcoCyc:EG11384-MONOMER.
ECOL316407:JW0598-MONOMER.
MetaCyc:EG11384-MONOMER.
BRENDAi1.11.1.15. 2026.

Miscellaneous databases

PROiP0AE08.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR017559. AhpC.
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR03137. AhpC. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Locations of genes encoding alkyl hydroperoxide reductase on the physical map of the Escherichia coli K-12 genome."
    Smillie D.A., Hayward R.S., Suzuki T., Fujita N., Ishihama A.
    J. Bacteriol. 174:3826-3827(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. "Sequence of minutes 4-25 of Escherichia coli."
    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.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Identification of Escherichia coli proteins cross-reacting with antibodies against region 2.2 peptide of RNA polymerase sigma subunit."
    Ueshima R., Fujita N., Ishihama A.
    Biochem. Biophys. Res. Commun. 184:634-639(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-31.
  7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-28 AND 70-81.
    Strain: K12 / EMG2.
  8. "Thioredoxin-linked 'thiol peroxidase' from periplasmic space of Escherichia coli."
    Cha M.-K., Kim H.-K., Kim I.-H.
    J. Biol. Chem. 270:28635-28641(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21.
    Strain: K12.
  9. Cited for: PROTEIN SEQUENCE OF 2-14.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  10. "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."
    Quadroni M., Staudenmann W., Kertesz M.A., James P.
    Eur. J. Biochem. 239:773-781(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  11. Cited for: PROTEIN SEQUENCE OF 2-5.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  12. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  13. "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia coli."
    Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J., Walker G.C.
    Mol. Cell 36:845-860(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN HYDROXYUREA RESISTANCE, DISRUPTION PHENOTYPE.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  14. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-93; LYS-153; LYS-169 AND LYS-171, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiAHPC_ECOLI
AccessioniPrimary (citable) accession number: P0AE08
Secondary accession number(s): P26427
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.