Reviewed, UniProtKB/Swiss-Prot P0AE11 (AHPC_SHIFL)

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:	SF0524, S0529

Organism

Shigella flexneri [Complete proteome] [HAMAP]

Taxonomic identifier

623 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

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

General annotation (Comments)

Function	Directly reduces organic hydroperoxides in its reduced dithiol form By similarity.
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
Subunit structure	Homodimer; disulfide-linked, upon oxidation By similarity.
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
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	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	1	1	Removed By similarity
	Chain	2 – 187	186	Alkyl hydroperoxide reductase subunit C		PRO_0000135121
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 By similarity
	Modified residue	93	1	N6-acetyllysine By similarity
	Modified residue	153	1	N6-acetyllysine By similarity
	Modified residue	169	1	N6-acetyllysine By similarity
	Modified residue	171	1	N6-acetyllysine By similarity
	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)
	P0AE11-1 [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

[1]

"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J. Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a.

[2]

"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE005674 Genomic DNA. Translation: AAN42170.1. AE014073 Genomic DNA. Translation: AAP16040.1.
RefSeq	NP_706463.1. NP_836234.1.
3D structure databases
HSSP	HSSP built from PDB template 1N8J based on UniProtKB P19479.
SMR	P0AE11. Positions 2-187.
ModBase	Search...
Proteomic databases
PRIDE	P0AE11.
Genome annotation databases
GeneID	1023440. 1076966.
GenomeReviews	Gene locus SF0524 in contig AE005674_GR. Gene locus S0529 in contig AE014073_GR.
KEGG	sfl:SF0524. sfx:S0529.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0AE11.
OMA	GDLADHY.
Enzyme and pathway databases
BioCyc	SFLE198214:AAN42170.1-MON.
BRENDA	1.11.1.15. 189495.
Family and domain databases
InterPro	IPR000866. Alkyl_hydroperoxide_Rdtase. IPR017559. Peroxiredoxin. IPR019479. Peroxiredoxin_C. IPR017936. Thioredoxin-like. 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_SHIFL

Accession

Primary (citable) accession number: P0AE11
Secondary accession number(s): P26427

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 34 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)