Reviewed, UniProtKB/Swiss-Prot P0AE08 (AHPC_ECOLI)

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Complete 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
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW xenobiotic metabolic process Inferred from mutant phenotype. Source: UniProtKB
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB membrane Inferred from direct assay. Source: UniProtKB
Molecular function	peroxiredoxin activity Inferred from mutant phenotype. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	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	47	1	Cysteine sulfenic acid (-SOH) intermediate By similarity
Amino acid modifications
	Modified residue	17	1	N6-acetyllysine Ref.12
	Modified residue	93	1	N6-acetyllysine Ref.12
	Modified residue	153	1	N6-acetyllysine Ref.12
	Modified residue	169	1	N6-acetyllysine Ref.12
	Modified residue	171	1	N6-acetyllysine Ref.12
	Disulfide bond	47		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)
	P0AE08-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 40AB796E6F5CC2D6	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

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: 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. , 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.
PIR	JN0289. C64794.
RefSeq	AP_001253.1. NP_415138.1.
3D structure databases
SMR	P0AE08. Positions 2-187.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0AE08. 31 interactions.
STRING	P0AE08.
Protein family/group databases
PeroxiBase	4830. EcoAhpC.
PTM databases
PhosSite	P0AE08.
2-D gel databases
SWISS-2DPAGE	P0AE08.
2DBase-Ecoli	P0AE08.
ECO2DBASE	B020.9. 6TH EDITION.
Proteomic databases
PRIDE	P0AE08.
Genome annotation databases
GeneID	945225.
GenomeReviews	Gene locus JW0598 in contig AP009048_GR. Gene locus b0605 in contig U00096_GR.
KEGG	ecj:JW0598. eco:b0605.
Organism-specific databases
EchoBASE	EB1357.
EcoGene	EG11384. ahpC.
CMR	Search...
Phylogenomic databases
eggNOG	COG0450.
HOGENOM	HBG493509.
OMA	GDLADHY.
Enzyme and pathway databases
BioCyc	EcoCyc:EG11384-MONOMER. ECOL168927:B0605-MONOMER. MetaCyc:EG11384-MONOMER.
Gene expression databases
Genevestigator	P0AE08.
Family and domain databases
InterPro	IPR000866. Alkyl_hydroperoxide_Rdtase. IPR017559. Peroxiredoxin. IPR019479. Peroxiredoxin_C. IPR017936. Thioredoxin-like. IPR012336. Thioredoxin-like_fold. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF10417. 1-cysPrx_C. 1 hit. PF00578. AhpC-TSA. 1 hit. [Graphical view]
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:	February 9, 2010
This is version 46 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)