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P0AE08

- AHPC_ECOLI

UniProt

P0AE08 - AHPC_ECOLI

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Protein
Alkyl hydroperoxide reductase subunit C
Gene
ahpC, b0605, JW0598
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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) intermediate By 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
Complete GO annotation...

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
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed6 Publications
Chaini2 – 187186Alkyl hydroperoxide reductase subunit C
PRO_0000135115Add
BLAST

Amino acid modifications

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

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 157156Thioredoxin
Add
BLAST

Sequence similaritiesi

Belongs to the AhpC/TSA family.
Contains 1 thioredoxin domain.

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

« Hide

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

« 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. "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 11, 2014
This is version 81 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