Reviewed, UniProtKB/Swiss-Prot P99118 (AHPF_STAAN)

Names and origin

Protein names

Recommended name:
    Alkyl hydroperoxide reductase subunit F
    EC=1.6.4.-

Gene names

Name:	ahpF
Ordered Locus Names:	SA0365

Organism

Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP]

Taxonomic identifier

158879 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	507 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the ahpC protein By similarity.
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	Homodimer By similarity.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD NADP
Molecular function	Oxidoreductase
PTM	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	FAD binding Inferred from electronic annotation. Source: InterPro NAD or NADH binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on NADH or NADPH Inferred from electronic annotation. Source: InterPro protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 507	507	Alkyl hydroperoxide reductase subunit F		PRO_0000166780
Regions
	Nucleotide binding	207 – 222	16	FAD By similarity
	Nucleotide binding	347 – 361	15	NAD or NADP By similarity
	Nucleotide binding	467 – 477	11	FAD By similarity
Amino acid modifications
	Disulfide bond	335 ↔ 338		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P99118-1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 6366693533CCD117	FASTA	507	54,708
	10 20 30 40 50 60 MLNADLKQQL KQLLELMEGN VEFVASLGSD EKSKELKELL TEISDMSPRL SLSEKSLKRT 70 80 90 100 110 120 PSFSVNRPGE ETGVTFAGIP LGHEFNSLVL AILQVSGRAP KEKQSIIDQI KNLEGSFHFE 130 140 150 160 170 180 TFISLTCQKC PDVVQALNLM SVINPNITHS MIDGAVFREE SENIMAVPAV FLNGEEFGNG 190 200 210 220 230 240 RMTIQDILSK LGSTADASEF ENKEPYDVLI VGGGPASGSA AIYTARKGLR TGIVADRIGG 250 260 270 280 290 300 QVNDTAGIEN FITVKETTGS EFSSNLAAHI DQYDIDAMTG IRATDIEKTD EAIKVTLENG 310 320 330 340 350 360 AVLESKTVII ATGAGWRKLN IPGEEQLINK GVAFCPHCDG PLFENKDVAV IGGGNSGVEA 370 380 390 400 410 420 AIDLAGIVNH VTLFEFASEL KADNVLQDRL RSLSNVDIKT NAKTTEVVGE DHVTGIRYED 430 440 450 460 470 480 MSTGEEHLLN LDGIFVQIGL LPNTSWLKDA VELNERGEIV IDRNNNTNVP GIFAAGDVTD 490 500 QKNKQIIISM GAGANAALNA FDYIIRN

References

	« Hide 'large scale' referencesShow '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. , 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., Lescuyer P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000018 Genomic DNA. Translation: BAB41592.1.
PIR	E89804.
RefSeq	NP_373614.1.
3D structure databases
HSSP	HSSP built from PDB template 1FL2 based on UniProtKB P35340.
ModBase	Search...
2-D gel databases
SWISS-2DPAGE	P99118.
Genome annotation databases
GeneID	1123147.
GenomeReviews	Gene locus SA0365 in contig BA000018_GR.
KEGG	sau:SA0365.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P99118.
OMA	P99118. ELEGVFV.
Enzyme and pathway databases
BioCyc	SAUR158879:SA0365-MON.
Family and domain databases
InterPro	IPR012081. Alkyl_hydroperoxide_Rdtase_suF. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR002109. Glutaredoxin. IPR008255. Pyr_nucl-diS_OxRdtase_2_AS. IPR001327. Pyr_OxRdtase_NAD_bd. IPR000103. Pyridine_nuc-diS_OxRdtase_2. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 2 hits.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PIRSF	PIRSF000238. AhpF. 1 hit.
PRINTS	PR00368. FADPNR. PR00469. PNDRDTASEII.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR03140. AhpF. 1 hit.
PROSITE	PS51354. GLUTAREDOXIN_2. 1 hit. PS00573. PYRIDINE_REDOX_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AHPF_STAAN

Accession

Primary (citable) accession number: P99118
Secondary accession number(s): Q99WJ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	June 16, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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