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P0AE08

- AHPC_ECOLI

UniProt

P0AE08 - AHPC_ECOLI

Protein

Alkyl hydroperoxide reductase subunit C

Gene

ahpC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    1. hydroperoxide reductase activity Source: EcoliWiki
    2. identical protein binding Source: IntAct
    3. oxidoreductase activity, acting on peroxide as acceptor Source: EcoliWiki
    4. peroxidase activity Source: EcoliWiki
    5. peroxiredoxin activity Source: UniProtKB-EC
    6. protein binding Source: EcoCyc

    GO - Biological processi

    1. cellular response to sulfate starvation Source: EcoliWiki
    2. iron assimilation by chelation and transport Source: CACAO
    3. response to alkyl hydroperoxide Source: EcoCyc
    4. response to hydroperoxide Source: EcoCyc

    Keywords - Molecular functioni

    Antioxidant, Oxidoreductase, Peroxidase

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11384-MONOMER.
    ECOL316407:JW0598-MONOMER.
    MetaCyc:EG11384-MONOMER.

    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11384. ahpC.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: EcoliWiki
    2. cytosol Source: UniProtKB
    3. membrane Source: UniProtKB

    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.

    PTM databases

    PhosSiteiP0809369.

    Expressioni

    Inductioni

    Repressed by sulfate or cysteine.

    Gene expression databases

    GenevestigatoriP0AE08.

    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.
    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.
    KOiK03386.
    OMAiHWEGTAV.
    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

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    MSLINTKIKP FKNQAFKNGE FIEITEKDTE GRWSVFFFYP ADFTFVCPTE    50
    LGDVADHYEE LQKLGVDVYA VSTDTHFTHK AWHSSSETIA KIKYAMIGDP 100
    TGALTRNFDN MREDEGLADR ATFVVDPQGI IQAIEVTAEG IGRDASDLLR 150
    KIKAAQYVAS HPGEVCPAKW KEGEATLAPS LDLVGKI 187
    Length:187
    Mass (Da):20,761
    Last modified:January 23, 2007 - v2
    Checksum:i40AB796E6F5CC2D6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_488895.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73706; AAC73706; b0605.
    BAA35235; BAA35235; BAA35235.
    GeneIDi12930899.
    945225.
    KEGGiecj:Y75_p0595.
    eco:b0605.
    PATRICi32116388. VBIEscCol129921_0634.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi C64794. JN0289.
    RefSeqi NP_415138.1. NC_000913.3.
    YP_488895.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P0AE08.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 849610. 1 interaction.
    DIPi DIP-36164N.
    IntActi P0AE08. 33 interactions.
    MINTi MINT-1241588.
    STRINGi 511145.b0605.

    Protein family/group databases

    PeroxiBasei 4830. EcoAhpC.

    PTM databases

    PhosSitei P0809369.

    2D gel databases

    SWISS-2DPAGE P0AE08.

    Proteomic databases

    PaxDbi P0AE08.
    PRIDEi P0AE08.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73706 ; AAC73706 ; b0605 .
    BAA35235 ; BAA35235 ; BAA35235 .
    GeneIDi 12930899.
    945225.
    KEGGi ecj:Y75_p0595.
    eco:b0605.
    PATRICi 32116388. VBIEscCol129921_0634.

    Organism-specific databases

    EchoBASEi EB1357.
    EcoGenei EG11384. ahpC.

    Phylogenomic databases

    eggNOGi COG0450.
    HOGENOMi HOG000022343.
    KOi K03386.
    OMAi HWEGTAV.
    OrthoDBi EOG67X1XH.
    PhylomeDBi P0AE08.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG11384-MONOMER.
    ECOL316407:JW0598-MONOMER.
    MetaCyc:EG11384-MONOMER.

    Miscellaneous databases

    PROi P0AE08.

    Gene expression databases

    Genevestigatori P0AE08.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR017559. AhpC.
    IPR000866. AhpC/TSA.
    IPR024706. Peroxiredoxin_AhpC-typ.
    IPR019479. Peroxiredoxin_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF10417. 1-cysPrx_C. 1 hit.
    PF00578. AhpC-TSA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000239. AHPC. 1 hit.
    SUPFAMi SSF52833. SSF52833. 1 hit.
    TIGRFAMsi TIGR03137. AhpC. 1 hit.
    PROSITEi PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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: October 1, 2014
    This is version 82 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