P80239 (AHPC_BACSU) Reviewed, UniProtKB/Swiss-Prot

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
General stress protein 22
Peroxiredoxin
Thioredoxin peroxidase

Gene names

Name:	ahpC
Ordered Locus Names:	BSU40090

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	187 AA.
Sequence status	Complete.
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	By heat shock, salt stress, oxidative stress and glucose limitation.
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.
Sequence similarities	Belongs to the AhpC/TSA family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Biological process	Stress response
Domain	Redox-active center
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW 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
	Chain	1 – 187	187	Alkyl hydroperoxide reductase subunit C		PRO_0000135113
Regions
	Domain	2 – 157	156	Thioredoxin
Sites
	Active site	47	1	Cysteine sulfenic acid (-SOH) intermediate By similarity
Amino acid modifications
	Disulfide bond	47		Interchain (with C-166); in linked form By similarity
	Disulfide bond	166		Interchain (with C-47); in linked form By similarity
Experimental info
	Sequence conflict	2	1	Missing AA sequence Ref.4
	Sequence conflict	8	1	V → VV AA sequence Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P80239 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 10DF6643BC90F54E	FASTA	187	20,627
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of the 36-kb region between gntZ and trnY genes of Bacillus subtilis genome." Kasahara Y., Nakai S., Ogasawara N. DNA Res. 4:155-159(1997) [PubMed: 9205843] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." 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. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Isolation and characterization of a hydrogen peroxide resistant mutant of Bacillus subtilis." Hartford O.M., Dowds B.C.A. Microbiology 140:297-304(1994) [PubMed: 8180695] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-41. Strain: 168 / YB886 / BG214.
[4]	"Analysis of the induction of general stress proteins of Bacillus subtilis." Voelker U., Engelmann S., Maul B., Riethdorf S., Voelker A., Schmid R., Mach H., Hecker M. Microbiology 140:741-752(1994) [PubMed: 8012595] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-14. Strain: 168 / IS58.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D78193 Genomic DNA. Translation: BAA11268.1. AL009126 Genomic DNA. Translation: CAB16046.1.
PIR	F69583.
RefSeq	NP_391889.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P80239.
SMR	P80239. Positions 2-166.
ModBase	Search...
Protein family/group databases
PeroxiBase	4904. BsAhpC.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000000483; EBBACP00000000483; EBBACG00000000481.
GeneID	938147.
GenomeReviews	Gene locus BSU40090 in contig AL009126_GR.
KEGG	bsu:BSU40090.
NMPDR	fig|224308.1.peg.4015.
PATRIC	18980088. VBIBacSub10457_4206.
Organism-specific databases
GenoList	BSU40090. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000000759.
HOGENOM	HBG493509.
OMA	GDLADHY.
PhylomeDB	P80239.
ProtClustDB	CLSK888184.
Enzyme and pathway databases
BioCyc	BSUB:BSU40090-MONOMER.
Family and domain databases
InterPro	IPR017559. AhpC. IPR000866. AhpC/TSA. IPR024706. Peroxiredoxin_AhpC-typ. IPR019479. Peroxiredoxin_C. IPR012336. Thioredoxin-like_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KO	K03386.
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_BACSU

Accession

Primary (citable) accession number: P80239
Secondary accession number(s): P53562

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program