ID   AHPF_ACICA              Reviewed;          16 AA.
AC   P82955;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   23-FEB-2022, entry version 38.
DE   RecName: Full=Alkyl hydroperoxide reductase subunit F;
DE            EC=1.8.1.-;
DE   Flags: Fragment;
GN   Name=ahpF;
OS   Acinetobacter calcoaceticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=471 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND INDUCTION.
RC   STRAIN=69-V;
RX   PubMed=11425483; DOI=10.1111/j.1574-6968.2001.tb10723.x;
RA   Benndorf D., Loffhagen N., Babel W.;
RT   "Protein synthesis patterns in Acinetobacter calcoaceticus induced by
RT   phenol and catechol show specificities of responses to chemostress.";
RL   FEMS Microbiol. Lett. 200:247-252(2001).
CC   -!- FUNCTION: Serves to protect the cell against DNA damage by alkyl
CC       hydroperoxides. It can use either NADH or NADPH as electron donor for
CC       direct reduction of redox dyes or of alkyl hydroperoxides when combined
CC       with the AhpC protein (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P35340}.
CC   -!- INDUCTION: By oxidative stress and catechol, and very weakly by heat
CC       shock. {ECO:0000269|PubMed:11425483}.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Flavoprotein; NAD; NADP; Oxidoreductase;
KW   Redox-active center; Stress response.
FT   CHAIN           1..>16
FT                   /note="Alkyl hydroperoxide reductase subunit F"
FT                   /id="PRO_0000166773"
FT   NON_TER         16
FT                   /evidence="ECO:0000303|PubMed:11425483"
SQ   SEQUENCE   16 AA;  1931 MW;  E070754AEFCBED15 CRC64;
     MLDQNIXTQL XAYLER