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bfr

Gene
bfr
Protein
Bacterioferritin
Organism
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Length
179 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Similarity
Belongs to the bacterioferritin family.
Mass
19.881 kDa
Sequence
MAGNREDRKAKVIEVLNKARAMELHAIHQYMNQHYSLDDMDYGELAANMKLIAIDEMRHAENFAERIKELGGEPTTQKEGKVVTGQAVPVIYESDADQEDATIEAYSQFLKVCKEQGDIVTARLFERIIEEEQAHLTYYENIGSHIKNLGDTYLAKIAGTPSSTGTASKGFVTATPAAE

Gene
bfr
Protein
Bacterioferritin
Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Length
167 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Similarity
Belongs to the bacterioferritin family.
Mass
19.22 kDa
Sequence
MQGDPEVIEFLNEQLTAELTAINQYFLHAKLQDHKGWTKLAKYTRAESFDEMRHAEVLTDRILLLDGLPNYQRLFHVRVGQSVTEMFQADREVELEAIDRLRRGIEVMRAKHDITSANVFEAILADEEHHIDYLETQLDLIEKLGESLYLSTVIEQTQPDPSGPGSL

Gene
bfr
Protein
Bacterioferritin
Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Length
161 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Similarity
Belongs to the bacterioferritin family.
Mass
18.659 kDa
Sequence
MKGEPKVIERLNDALFLELGAVNQYWLHYRLLNDWGYTRLAKKEREESIEEMHHADKLINRIIFFEGFPNLQTVSPLRIGQNVKEVLEADLKGEYDARASYKESREICDKLGDYVSKQLFDELLADEEGHIDFLETQLDLLAKIGEERYGQLNAAPADEAE

Gene
bfr
Protein
Bacterioferritin
Organism
Brucella suis biovar 1 (strain 1330)
Length
161 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Similarity
Belongs to the bacterioferritin family.
Mass
18.64 kDa
Sequence
MKGEPKVIERLNEALFLELGAVNQYWLHYRLLNDWGYTRLAKKEREESIEEMHHADKLIDRIIFLEGFPNLQTVSPLRIGQNVKEVLEADLKGEYDARASYKESREICDKLGDYVSKQLFDELLADEEGHIDFLETQLDLLAKIGEERYGQLNAAPADEAE

Gene
bfr
Protein
Bacterioferritin
Organism
Rhodobacter capsulatus
Length
161 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Similarity
Belongs to the bacterioferritin family.
Mass
18.173 kDa
Sequence
MKGDAKVIEFLNAALRSELTAISQYWVHFRLQEDWGLAKMAKKSREESIEEMGHADKIIARILFLEGHPNLQKLDPLRIGEGPRETLECDLAGEHDALKLYREARDYCAEVGDIVSKNIFESLITDEEGHVDFLETQISLYDRLGPQGFALLNAAPMDAAE

Gene
bfr
Protein
Bacterioferritin
Organism
Mycobacterium avium
Length
159 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Similarity
Belongs to the bacterioferritin family.
Mass
18.492 kDa
Sequence
MQGDPEVLRLLNEQLTTQLTAINQYFLHSKMQDNWGFTELAEHTRAESFDEMRHAEAITDRILLLDGLPNYQRLFSLRIGQTLREQFEADLAIEYEVMDRLKPAIILCREKQDSTTATLFEQIVADEEKHIDYLETQLELMDKLGVELYSAQCVSRPPS

Gene
bfr
Protein
Bacterioferritin
Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Length
159 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Similarity
Belongs to the bacterioferritin family.
Mass
18.341 kDa
Sequence
MQGDPDVLRLLNEQLTSELTAINQYFLHSKMQDNWGFTELAAHTRAESFDEMRHAEEITDRILLLDGLPNYQRIGSLRIGQTLREQFEADLAIEYDVLNRLKPGIVMCREKQDTTSAVLLEKIVADEEEHIDYLETQLELMDKLGEELYSAQCVSRPPT

Gene
bfr
Protein
Bacterioferritin
Organism
Mycobacterium leprae (strain TN)
Length
159 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex (By similarity). Probably plays a crucial role in the intracellular existence of this organism by functioning as a temporary depository for iron in iron deprivation.
Similarity
Belongs to the bacterioferritin family.
Mass
18.263 kDa
Sequence
MQGDPDVLRLLNEQLTSELTAINQYFLHSKMQENWGFTELAERTRVESFDEMRHAEAITDRILLLDGLPNYQRIGSLRVGQTLREQFEADLAIEYEVMSRLKPGIIMCREKQDSTSAVLLEKIVADEEEHIDYLETQLALMGQLGEELYSAQCVSRPPS

Gene
bfr
Protein
Bacterioferritin
Organism
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Length
159 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Similarity
Belongs to the bacterioferritin family.
Mass
18.479 kDa
Sequence
MQGDPEVLRLLNEQLTSELTAINQYFLHSKMQDNWGFTELAEHTRAESFDEMRHAEAITDRILLLDGLPNYQRLFSLRIGQTLREQFEADLAIEYEVMDRLKPAIILCREKQDSTTATLFEQIVADEEKHIDYLETQLELMDKLGVELYSAQCVSRPPS

Gene
bfr
Protein
Bacterioferritin
Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Length
159 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Similarity
Belongs to the bacterioferritin family.
Mass
18.341 kDa
Sequence
MQGDPDVLRLLNEQLTSELTAINQYFLHSKMQDNWGFTELAAHTRAESFDEMRHAEEITDRILLLDGLPNYQRIGSLRIGQTLREQFEADLAIEYDVLNRLKPGIVMCREKQDTTSAVLLEKIVADEEEHIDYLETQLELMDKLGEELYSAQCVSRPPT

Gene
bfr
Protein
Bacterioferritin
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Length
159 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Similarity
Belongs to the bacterioferritin family.
Mass
18.341 kDa
Sequence
MQGDPDVLRLLNEQLTSELTAINQYFLHSKMQDNWGFTELAAHTRAESFDEMRHAEEITDRILLLDGLPNYQRIGSLRIGQTLREQFEADLAIEYDVLNRLKPGIVMCREKQDTTSAVLLEKIVADEEEHIDYLETQLELMDKLGEELYSAQCVSRPPT

Gene
bfr
Protein
Bacterioferritin
Organism
Serratia marcescens
Length
159 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Similarity
Belongs to the bacterioferritin family.
Mass
18.533 kDa
Sequence
MKGDKKIIAHLNKLLGNELVAINQYFLHARMFKNWGLMRLNDKEYHESIDEMKHADRYIERILFLEGIPNLQDLGKLNIGEDIEEMLRSDLALELAGAKNLREGIAYADSIHDYVSRDLMIDILADEEEHIDWLETELDLIARLGIQNYAQAQILERKE

Gene
bfr
Protein
Bacterioferritin
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Length
158 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Similarity
Belongs to the bacterioferritin family.
Mass
18.495 kDa
Sequence
MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIGEDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG

Gene
bfr
Protein
Bacterioferritin
Organism
Escherichia coli (strain K12)
Length
158 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.
Similarity
Belongs to the bacterioferritin family.
Mass
18.495 kDa
Sequence
MKGDTKVINYLNKLLGNELVAINQYFLHARMFKNWGLKRLNDVEYHESIDEMKHADRYIERILFLEGLPNLQDLGKLNIGEDVEEMLRSDLALELDGAKNLREAIGYADSVHDYVSRDMMIEILRDEEGHIDWLETELDLIQKMGLQNYLQAQIREEG

Gene
bfr
Protein
Bacterioferritin
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
158 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Similarity
Belongs to the bacterioferritin family.
Mass
18.355 kDa
Sequence
MKGDVKIINYLNKLLGNELVAINQYFLHARMFKNWGLTRLNDVEYHESIDEMKHADKYIERILFLEGIPNLQDLGKLGIGEDVEEMLRSDLRLELEGAKDLREAIAYADSVHDYVSRDMMIEILADEEGHIDWLETELDLIAKLGMQNYLQSQIKVTD

Gene
bfr
Protein
Bacterioferritin
Organism
Azotobacter vinelandii
Length
156 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Similarity
Belongs to the bacterioferritin family.
Mass
18.105 kDa
Sequence
MKGDKIVIQHLNKILGNELIAINQYFLHARMYEDWGLEKLGKHEYHESIDEMKHADKLIKRILFLEGLPNLQELGKLLIGEHTKEMLECDLKLEQAGLPDLKAAIAYCESVGDYASRELLEDILESEEDHIDWLETQLDLIDKIGLENYLQSQMDE

Gene
bfr
Protein
Bacterioferritin
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Length
156 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Similarity
Belongs to the bacterioferritin family.
Mass
18.331 kDa
Sequence
MKGKPAVLAQLHKLLRGELAARDQYFIHSRMYQDWGLEKLYSRIDHEMQDETAHASLLIERILFLEETPDLSQQDPIRVGKTVPEMLQYDLDYEYEVIANLKEAMAVCEQEQDYQSRDLLLKILADTEEDHAYWLEKQLGLIEKIGLQNYLQSQMS

Gene
bfr
Protein
Bacterioferritin
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Length
154 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Similarity
Belongs to the bacterioferritin family.
Mass
17.94 kDa
Sequence
MQGHPEVIDYLNTLLTGELAARDQYFIHSRMYEDWGFSKLYERLNHEMEEETQHADALLRRILLLEGTPRMRPDDIHPGTTVPEMLEADLKLERHVRAALAKGIALCEQHKDFVSRDILKAQLADTEEDHAYWLEQQLGLIARMGLENYLQSQI

Gene
bfr
Protein
Bacterioferritin
Organism
Pseudomonas putida
Length
154 amino acids
Function
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Similarity
Belongs to the bacterioferritin family.
Mass
18.001 kDa
Sequence
MQGHPDVINYLVTLLKGELAARDQYFIHSRMYEDWGLTKLYERINHEMEEETQHADALMRRILMLEGTPDMRADDLEVGSTVPEMIEADLKLEYKVRGALCKGIELCELHKDYISRDILRAQLADTEEDHTYWLEKQQGLIKAIGLENYLQSQM

Gene
bfr
Protein
Bacterioferritin
Organism
Nitrobacter winogradskyi
Length
50 amino acids
Function
May act as one of the electron carriers in the reverse electron-transport system from cytochrome c-552 to NADP(+).
Similarity
Belongs to the bacterioferritin family.
Mass
6.055 kDa
Fragment
single
Sequence
MKGDPKVIDYLNKALRHELTAINQYWLHYRLLDNWGIKDLAKKWRAESIE