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Reviewed, UniProtKB/Swiss-Prot P99074 (AHPC_STAAN)

Last modified November 25, 2008. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
Gene names
Name: ahpC
Ordered Locus Names: SA0366
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length189 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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' + H(2)O + ROH.

Subunit structure

Homodimer; disulfide-linked, upon oxidation By similarity.

Post-translational modification

The Cys-49-SH group is the primary site of oxidation by H(2)O(2), and the oxidized Cys-49 (probably Cys-SOH) rapidly reacts with Cys-168-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

   DomainRedox-active center
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionperoxiredoxin activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 189189Alkyl hydroperoxide reductase subunit C
PRO_0000135124

Regions

Domain2 – 159158Thioredoxin

Sites

Active site491Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Disulfide bond49Interchain (with C-168); in linked form By similarity
Disulfide bond168Interchain (with C-49); in linked form By similarity

Sequences

Sequence LengthMass (Da)Tools
P99074-1 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: B7134A9C84066B73

FASTA18920,977
        10         20         30         40         50         60 
MSLINKEILP FTAQAFDPKK DQFKEVTQED LKGSWSVVCF YPADFSFVCP TELEDLQNQY 

        70         80         90        100        110        120 
EELQKLGVNV FSVSTDTHFV HKAWHDHSDA ISKITYTMIG DPSQTITRNF DVLDEATGLA 

       130        140        150        160        170        180 
QRGTFIIDPD GVVQASEINA DGIGRDASTL AHKIKAAQYV RKNPGEVCPA KWEEGAKTLQ 


PGLDLVGKI 

« Hide

References

« Hide 'large scale' references
[1]"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. expand/collapse author list , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth."
Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.
J. Microbiol. Methods 60:247-257(2005) [PubMed: 15590099] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[3]"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
Vaezzadeh A.R., Deshusses J., Lescuye P., Hochstrasser D.F.
Submitted (OCT-2007) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases

BA000018 Genomic DNA. Translation: BAB41593.1.
PIRF89804.
RefSeqNP_373615.1.

3D structure databases

HSSPHSSP built from PDB template 1N8J based on UniProtKB P19479.
ModBaseSearch...

2-D gel databases

SWISS-2DPAGEP99074.

Genome annotation databases

GeneID1123148.
GenomeReviewsGene locus SA0366 in contig BA000018_GR.
KEGGsau:SA0366.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP99074.

Enzyme and pathway databases

BioCycSAUR158879:SA0366-MON.

Family and domain databases

InterProIPR000866. AhpC-TSA.
IPR017559. Peroxiredoxin.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF00578. AhpC-TSA. 1 hit.
[Graphical view]
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAHPC_STAAN
AccessionPrimary (citable) accession number: P99074
Secondary accession number(s): Q53647
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: November 25, 2008
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

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