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P0AE08 (AHPC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ahpC
Ordered Locus Names:b0605, JW0598
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length187 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Directly reduces organic hydroperoxides in its reduced dithiol form.

Catalytic activity

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

Subunit structure

Homodimer; disulfide-linked, upon oxidation By similarity.

Induction

Repressed by sulfate or cysteine.

Post-translational modification

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.

Sequence similarities

Belongs to the AhpC/TSA family.

Contains 1 thioredoxin domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-547397,EBI-547397

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
Chain2 – 187186Alkyl hydroperoxide reductase subunit C
PRO_0000135115

Regions

Domain2 – 157156Thioredoxin

Sites

Active site471Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Modified residue171N6-acetyllysine Ref.13
Modified residue931N6-acetyllysine Ref.13
Modified residue1531N6-acetyllysine Ref.13
Modified residue1691N6-acetyllysine Ref.13
Modified residue1711N6-acetyllysine Ref.13
Disulfide bond47Interchain (with C-166); in linked form By similarity
Disulfide bond166Interchain (with C-47); in linked form By similarity

Sequences

Sequence LengthMass (Da)Tools
P0AE08 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 40AB796E6F5CC2D6

FASTA18720,761
        10         20         30         40         50         60 
MSLINTKIKP FKNQAFKNGE FIEITEKDTE GRWSVFFFYP ADFTFVCPTE LGDVADHYEE 

        70         80         90        100        110        120 
LQKLGVDVYA VSTDTHFTHK AWHSSSETIA KIKYAMIGDP TGALTRNFDN MREDEGLADR 

       130        140        150        160        170        180 
ATFVVDPQGI IQAIEVTAEG IGRDASDLLR KIKAAQYVAS HPGEVCPAKW KEGEATLAPS 


LDLVGKI 

« Hide

References

« Hide 'large scale' references
[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]"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."
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. expand/collapse author list , 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.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
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]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]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
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]"Protein identification with N and C-terminal sequence tags in proteome projects."
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.
J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13187 Genomic DNA. Translation: BAA02485.1.
U82598 Genomic DNA. Translation: AAB40806.1.
U00096 Genomic DNA. Translation: AAC73706.1.
AP009048 Genomic DNA. Translation: BAA35235.1.
PIRJN0289. C64794.
RefSeqNP_415138.1. NC_000913.3.
YP_488895.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0AE08.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid849610. 1 interaction.
DIPDIP-36164N.
IntActP0AE08. 33 interactions.
MINTMINT-1241588.
STRING511145.b0605.

Protein family/group databases

PeroxiBase4830. EcoAhpC.

PTM databases

PhosSiteP0809369.

2D gel databases

SWISS-2DPAGEP0AE08.

Proteomic databases

PaxDbP0AE08.
PRIDEP0AE08.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73706; AAC73706; b0605.
BAA35235; BAA35235; BAA35235.
GeneID12930899.
945225.
KEGGecj:Y75_p0595.
eco:b0605.
PATRIC32116388. VBIEscCol129921_0634.

Organism-specific databases

EchoBASEEB1357.
EcoGeneEG11384. ahpC.

Phylogenomic databases

eggNOGCOG0450.
HOGENOMHOG000022343.
KOK03386.
OMAHWEGTAV.
OrthoDBEOG67X1XH.
PhylomeDBP0AE08.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP0AE08.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR017559. AhpC.
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFPIRSF000239. AHPC. 1 hit.
SUPFAMSSF52833. SSF52833. 1 hit.
TIGRFAMsTIGR03137. AhpC. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP0AE08.

Entry information

Entry nameAHPC_ECOLI
AccessionPrimary (citable) accession number: P0AE08
Secondary accession number(s): P26427
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene