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Reviewed, UniProtKB/Swiss-Prot P0AE08 (AHPC_ECOLI)

Last modified February 9, 2010. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alkyl hydroperoxide reductase subunit C
    EC=1.11.1.15
Alternative name(s):
    Peroxiredoxin
    Thioredoxin peroxidase
    Alkyl hydroperoxide reductase protein C22
    SCRP-23
    Sulfate starvation-induced protein 8
      Short name=SSI8
Gene names
Name: ahpC
Ordered Locus Names: b0605, JW0598
OrganismEscherichia coli (strain K12) [Complete 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.

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.12
Modified residue931N6-acetyllysine Ref.12
Modified residue1531N6-acetyllysine Ref.12
Modified residue1691N6-acetyllysine Ref.12
Modified residue1711N6-acetyllysine Ref.12
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
P0AE08-1 [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: 1592833] [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: 8905232] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 1575737] [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: 9298646] [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: 7499381] [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: 8774726] [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: 9600841] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-5.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[12]"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: 18723842] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-93; LYS-153; LYS-169 AND LYS-171, MASS SPECTROMETRY.

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.
RefSeqAP_001253.1.
NP_415138.1.

3D structure databases

SMRP0AE08. Positions 2-187.
ModBaseSearch...

Protein-protein interaction databases

IntActP0AE08. 31 interactions.
STRINGP0AE08.

Protein family/group databases

PeroxiBase4830. EcoAhpC.

PTM databases

PhosSiteP0AE08.

2-D gel databases

SWISS-2DPAGEP0AE08.
2DBase-EcoliP0AE08.
ECO2DBASEB020.9. 6TH EDITION.

Proteomic databases

PRIDEP0AE08.

Genome annotation databases

GeneID945225.
GenomeReviewsGene locus JW0598 in contig AP009048_GR.
Gene locus b0605 in contig U00096_GR.
KEGGecj:JW0598.
eco:b0605.

Organism-specific databases

EchoBASEEB1357.
EcoGeneEG11384. ahpC.
CMRSearch...

Phylogenomic databases

eggNOGCOG0450.
HOGENOMHBG493509.
OMAGDLADHY.

Enzyme and pathway databases

BioCycEcoCyc:EG11384-MONOMER.
ECOL168927:B0605-MONOMER.
MetaCyc:EG11384-MONOMER.

Gene expression databases

GenevestigatorP0AE08.

Family and domain databases

InterProIPR000866. Alkyl_hydroperoxide_Rdtase.
IPR017559. Peroxiredoxin.
IPR019479. Peroxiredoxin_C.
IPR017936. Thioredoxin-like.
IPR012336. Thioredoxin-like_fold.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
TIGRFAMsTIGR03137. AhpC. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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: February 9, 2010
This is version 46 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents