Alkyl hydroperoxide reductase subunit C - Escherichia coli (strain K12)

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P0AE08 (AHPC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 73. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	ahpC
Ordered Locus Names:	b0605, JW0598

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	187 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Domain	Redox-active center
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Acetylation Disulfide bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to sulfate starvation Inferred from direct assay Ref.10. Source: EcoliWiki response to alkyl hydroperoxide Inferred from mutant phenotype PubMed 2649484. Source: EcoCyc
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	hydroperoxide reductase activity Inferred from direct assay PubMed 7644465. Source: EcoliWiki peroxidase activity Inferred from genetic interaction PubMed 11717276. Source: EcoliWiki peroxiredoxin activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Chain

2 – 187

186

Alkyl hydroperoxide reductase subunit C

PRO_0000135115

Regions

Domain

2 – 157

156

Thioredoxin

Sites

Active site

Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Modified residue

N6-acetyllysine Ref.13

Modified residue

N6-acetyllysine Ref.13

Modified residue

153

N6-acetyllysine Ref.13

Modified residue

169

N6-acetyllysine Ref.13

Modified residue

171

N6-acetyllysine Ref.13

Disulfide bond

Interchain (with C-166); in linked form By similarity

Disulfide bond

166

Interchain (with C-47); in linked form By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P0AE08 [UniParc].

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

187

20,761

        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' referencesShow '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. 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 277:1453-1474(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, 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.
PIR	JN0289. C64794.
RefSeq	NP_415138.1. NC_000913.2. YP_488895.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0AE08.
SMR	P0AE08. Positions 2-169.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-36164N.
IntAct	P0AE08. 31 interactions.
MINT	MINT-1241588.
STRING	511145.b0605.
Protein family/group databases
PeroxiBase	4830. EcoAhpC.
PTM databases
PhosSite	P0809369.
2D gel databases
SWISS-2DPAGE	P0AE08.
Proteomic databases
PaxDb	P0AE08.
PRIDE	P0AE08.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73706; AAC73706; b0605. BAA35235; BAA35235; BAA35235.
GeneID	12930899. 945225.
KEGG	ecj:Y75_p0595. eco:b0605.
PATRIC	32116388. VBIEscCol129921_0634.
Organism-specific databases
EchoBASE	EB1357.
EcoGene	EG11384. ahpC.
Phylogenomic databases
eggNOG	COG0450.
HOGENOM	HOG000022343.
KO	K03386.
OMA	FHKGEFV.
ProtClustDB	PRK10382.
Enzyme and pathway databases
BioCyc	EcoCyc:EG11384-MONOMER. ECOL316407:JW0598-MONOMER. MetaCyc:EG11384-MONOMER.
Gene expression databases
Genevestigator	P0AE08.
Family and domain databases
Gene3D	3.40.30.10. 1 hit.
InterPro	IPR017559. AhpC. IPR000866. AhpC/TSA. IPR024706. Peroxiredoxin_AhpC-typ. IPR019479. Peroxiredoxin_C. IPR012336. Thioredoxin-like_fold. [Graphical view]
PANTHER	PTHR10681:SF7. PTHR10681:SF7. 1 hit.
Pfam	PF10417. 1-cysPrx_C. 1 hit. PF00578. AhpC-TSA. 1 hit. [Graphical view]
PIRSF	PIRSF000239. AHPC. 1 hit.
SUPFAM	SSF52833. Thiordxn-like_fd. 1 hit.
TIGRFAMs	TIGR03137. AhpC. 1 hit.
PROSITE	PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AHPC_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents