ID   BFR_AZOVI      STANDARD;      PRT;   156 AA.
AC   P22759;
DT   01-AUG-1991 (Rel. 19, Created)
DT   01-MAY-1992 (Rel. 22, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Bacterioferritin (BFR) (Cytochrome B-557.5).
GN   Name=bfr;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=92196129; PubMed=1549605;
RA   Grossman M.J., Hinton S.M., Minak-Bernero V., Slaughter C.,
RA   Stiefel E.I.;
RT   "Unification of the ferritin family of proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:2419-2423(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-70.
RX   MEDLINE=91265528; PubMed=1904771; DOI=10.1016/0167-4838(91)90099-L;
RA   Andrews S.C., Findlay J.B.C., Guest J.R., Harrison P.M., Keen J.N.,
RA   Smith J.M.A.;
RT   "Physical, chemical and immunological properties of the
RT   bacterioferritins of Escherichia coli, Pseudomonas aeruginosa and
RT   Azotobacter vinelandii.";
RL   Biochim. Biophys. Acta 1078:111-116(1991).
CC   -!- FUNCTION: May perform analogous functions in iron detoxification
CC       and storage to that of animal ferritins.
CC   -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per dimer
CC       (By similarity).
CC   -!- SUBUNIT: Oligomer of 24 identical subunits (By similarity).
CC   -!- MISCELLANEOUS: The di-iron binding site functions as active site
CC       where iron ions are oxidized from iron(II) to iron(III) before
CC       they are stored (By similarity).
CC   -!- SIMILARITY: Belongs to the bacterioferritin family.
CC   -!- SIMILARITY: Contains 1 ferritin-like diiron domain.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; M83692; AAA22121.1; -.
DR   PIR; A41983; A41983.
DR   HSSP; P11056; 1BCF.
DR   InterPro; IPR002024; Bacterioferritin.
DR   InterPro; IPR009078; Ferritin/RR_like.
DR   InterPro; IPR008331; Ferritin_Dps.
DR   InterPro; IPR009040; Ferritin_like.
DR   Pfam; PF00210; Ferritin; 1.
DR   PRINTS; PR00601; BACFERRITIN.
DR   ProDom; PD002269; Bacterioferritin; 1.
DR   TIGRFAMs; TIGR00754; bfr; 1.
DR   PROSITE; PS00549; BACTERIOFERRITIN; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
KW   Direct protein sequencing; Heme; Iron; Iron storage; Metal-binding.
FT   DOMAIN        1    145       Ferritin-like diiron.
FT   METAL        18     18       Iron 1 (By similarity).
FT   METAL        51     51       Iron 1 (By similarity).
FT   METAL        51     51       Iron 2 (By similarity).
FT   METAL        52     52       Iron (heme axial ligand) (By similarity).
FT   METAL        54     54       Iron 1 (By similarity).
FT   METAL        94     94       Iron 2 (By similarity).
FT   METAL       127    127       Iron 1 (By similarity).
FT   METAL       127    127       Iron 2 (By similarity).
FT   METAL       130    130       Iron 2 (By similarity).
SQ   SEQUENCE   156 AA;  18105 MW;  468C2F059240A647 CRC64;
     MKGDKIVIQH LNKILGNELI AINQYFLHAR MYEDWGLEKL GKHEYHESID EMKHADKLIK
     RILFLEGLPN LQELGKLLIG EHTKEMLECD LKLEQAGLPD LKAAIAYCES VGDYASRELL
     EDILESEEDH IDWLETQLDL IDKIGLENYL QSQMDE
//