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UniProtKB/Swiss-Prot entry P80239


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AHPC_BACSU
Primary accession number P80239
Secondary accession number P53562
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on October 1, 1996 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 64)
Name and origin of the protein
Protein name Alkyl hydroperoxide reductase subunit C
Synonyms EC 1.11.1.15
Peroxiredoxin
Thioredoxin peroxidase
Alkyl hydroperoxide reductase protein C22
General stress protein 22
Gene name
Name: ahpC
OrderedLocusNames: BSU40090
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
Kasahara Y., Nakai S., Yoshikawa H., Ogasawara N.;
"36kb sequence between gntZ and trnY of B. subtilis genome.";
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[3]
PROTEIN SEQUENCE OF 1-41.
STRAIN=168 / YB886;
PubMed=8180695 [NCBI, ExPASy, EBI, Israel, Japan]
Hartford O.M., Dowds B.C.A.;
"Isolation and characterization of a hydrogen peroxide resistant mutant of Bacillus subtilis.";
Microbiology 140:297-304(1994).
[4]
PROTEIN SEQUENCE OF 1-14.
STRAIN=168 / IS58;
PubMed=8012595 [NCBI, ExPASy, EBI, Israel, Japan]
Voelker U., Engelmann S., Maul B., Riethdorf S., Voelker A., Schmid R., Mach H., Hecker M.;
"Analysis of the induction of general stress proteins of Bacillus subtilis.";
Microbiology 140:741-752(1994).
Comments
  • FUNCTION: Directly reduces organic hydroperoxides in its reduced dithiol form.
  • CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
  • SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By similarity).
  • INDUCTION: By heat shock, salt stress, oxidative stress and glucose limitation.
  • PTM: The Cys-47-SH group is the primary site of oxidation by H(2)O(2), 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.
  • SIMILARITY: Belongs to the ahpC/TSA family.
  • SIMILARITY: Contains 1 thioredoxin domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D78193; BAA11268.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99124; CAB16046.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR F69583; F69583.
RefSeq NP_391889.1; -.
3D structure databases
HSSP P19479; 1N8J. [HSSP ENTRY / PDB]
ModBase P80239.
Protein family/group databases
PeroxiBase 4904; BsAhpC.
Enzyme and pathway databases
BioCyc BSUB224308:BSU4006-MON; -.
Organism-specific databases
SubtiList BG11385; ahpC. [Micado]
Ontologies
GO
GO:0051920; Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006950; Biological process: response to stress (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000866; AhpC-TSA.
IPR017559; Peroxiredoxin.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF00578; AhpC-TSA; 1.
Pfam graphical view of domain structure.
PROSITE PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P80239.
Genome annotation databases
GeneID 938147; -.
GenomeReviews AL009126_GR; BSU40090.
KEGG bsu:BSU40090; -.
NMPDR fig|224308.1.peg.4015; -.
Phylogenomic databases
HOGENOM P80239; -.
Genome annotation databases
CMR P80239; BSU40090.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Antioxidant; Complete proteome; Direct protein sequencing; Oxidoreductase; Peroxidase; Redox-active center; Stress response.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   187  187     Alkyl hydroperoxide reductase subunit C. PRO_0000135113
DOMAIN   2   157  156     Thioredoxin. 
ACT_SITE   47    47        Cysteine sulfenic acid (-SOH) intermediate (By similarity). 
DISULFID   47    47        Interchain (with C-166); in linked form (By similarity). 
DISULFID   166   166        Interchain (with C-47); in linked form (By similarity). 
CONFLICT   2     2        Missing (in Ref. 4; AA sequence). 
CONFLICT   8     8        V -> VV (in Ref. 4; AA sequence). 
Sequence information
Length: 187 AA [This is the length of the unprocessed precursor] Molecular weight: 20627 Da [This is the MW of the unprocessed precursor] CRC64: 10DF6643BC90F54E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLIGKEVLP FEAKAFKNGE FIDVTNEDLK GQWSVFCFYP ADFSFVCPTE LEDLQEQYAA 

        70         80         90        100        110        120 
LKELGVEVYS VSTDTHFVHK GWHDSSEKIS KITYAMIGDP SQTISRNFDV LDEETGLADR 

       130        140        150        160        170        180 
GTFIIDPDGV IQTVEINAGG IGRDASNLVN KVKAAQYVRQ NPGEVCPAKW EEGGETLTPS 


LDLVGKI 

P80239 in FASTA format

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