BFR_MYCTU
ID BFR_MYCTU Reviewed; 159 AA.
AC P9WPQ9; L0T7Y6; O08465; P63697;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Bacterioferritin BfrA {ECO:0000303|PubMed:9634230};
DE Short=Bfr;
DE EC=1.16.3.1;
GN Name=bfr; Synonyms=bfrA; OrderedLocusNames=Rv1876; ORFNames=MTCY180.42c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP CRYSTALLIZATION, AND HEME-BINDING.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18453710; DOI=10.1107/s1744309108007240;
RA Gupta V., Gupta R.K., Khare G., Salunke D.M., Tyagi A.K.;
RT "Cloning, expression, purification, crystallization and preliminary X-ray
RT crystallographic analysis of bacterioferritin A from Mycobacterium
RT tuberculosis.";
RL Acta Crystallogr. F 64:398-401(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=22101841; DOI=10.1128/jb.05553-11;
RA Reddy P.V., Puri R.V., Khera A., Tyagi A.K.;
RT "Iron storage proteins are essential for the survival and pathogenesis of
RT Mycobacterium tuberculosis in THP-1 macrophages and the guinea pig model of
RT infection.";
RL J. Bacteriol. 194:567-575(2012).
RN [5]
RP NOT FOUND IN ENCAPSULIN NANOCOMPARTMENTS.
RC STRAIN=H37Rv;
RX PubMed=24855650; DOI=10.1074/jbc.m114.570119;
RA Contreras H., Joens M.S., McMath L.M., Le V.P., Tullius M.V., Kimmey J.M.,
RA Bionghi N., Horwitz M.A., Fitzpatrick J.A., Goulding C.W.;
RT "Characterization of a Mycobacterium tuberculosis nanocompartment and its
RT potential cargo proteins.";
RL J. Biol. Chem. 289:18279-18289(2014).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) IN COMPLEX WITH IRON IONS AND A
RP DEGRADED PORPHYRIN DERIVATIVE, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19946376; DOI=10.1371/journal.pone.0008028;
RA Gupta V., Gupta R.K., Khare G., Salunke D.M., Tyagi A.K.;
RT "Crystal structure of Bfr A from Mycobacterium tuberculosis: incorporation
RT of selenomethionine results in cleavage and demetallation of haem.";
RL PLoS ONE 4:E8028-E8028(2009).
CC -!- FUNCTION: Iron-storage protein, whose ferroxidase center binds Fe(2+)
CC ions, oxidizes them by dioxygen to Fe(3+), and participates in the
CC subsequent Fe(3+) oxide mineral core formation within the central
CC cavity of the protein complex. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Note=Binds 2 iron ions per subunit. The catalytic dinuclear iron-
CC binding site within each subunit is known as the ferroxidase center.;
CC -!- SUBUNIT: Homooligomer of 24 subunits, arranged as 12 dimers, that are
CC packed together to form an approximately spherical molecule with a
CC central cavity, in which large amounts of iron can be deposited.
CC {ECO:0000269|PubMed:19946376}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:24855650}.
CC Note=Unlike its homolog BfrB, is not found in encapsulin
CC nanocompartments. {ECO:0000269|PubMed:24855650}.
CC -!- DISRUPTION PHENOTYPE: A single deletion is slightly more sensitive to
CC oxidative stress (cumene hydroperoxide and plumbagin). A double bfrA-
CC bfrB mutant grows 40% less well in the presence of an iron chelator, is
CC more sensitive to oxidative stress, has significantly reduced
CC pathological effects in guinea pigs and a marked reduction in its
CC survival in human macrophages. {ECO:0000269|PubMed:22101841}.
CC -!- SIMILARITY: Belongs to the ferritin-like superfamily. Bacterioferritin
CC family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44642.1; -; Genomic_DNA.
DR PIR; A70515; A70515.
DR RefSeq; NP_216392.1; NC_000962.3.
DR RefSeq; WP_003409398.1; NZ_NVQJ01000013.1.
DR PDB; 2WTL; X-ray; 2.59 A; A/B/C/D/E/F=1-159.
DR PDB; 3QB9; X-ray; 2.11 A; A/B/C/D/E/F=1-159.
DR PDB; 3UOF; X-ray; 2.90 A; A/B/C/D/E/F=1-159.
DR PDB; 3UOI; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x=1-159.
DR PDBsum; 2WTL; -.
DR PDBsum; 3QB9; -.
DR PDBsum; 3UOF; -.
DR PDBsum; 3UOI; -.
DR AlphaFoldDB; P9WPQ9; -.
DR SMR; P9WPQ9; -.
DR STRING; 83332.Rv1876; -.
DR PaxDb; P9WPQ9; -.
DR GeneID; 45425849; -.
DR GeneID; 885767; -.
DR KEGG; mtu:Rv1876; -.
DR TubercuList; Rv1876; -.
DR eggNOG; COG2193; Bacteria.
DR OMA; YQRLFHV; -.
DR PhylomeDB; P9WPQ9; -.
DR Reactome; R-HSA-1222449; Mtb iron assimilation by chelation.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0004322; F:ferroxidase activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR GO; GO:0010039; P:response to iron ion; IEP:MTBBASE.
DR CDD; cd00907; Bacterioferritin; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR002024; Bacterioferritin.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009040; Ferritin-like_diiron.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR008331; Ferritin_DPS_dom.
DR Pfam; PF00210; Ferritin; 1.
DR PIRSF; PIRSF002560; Bacterioferritin; 1.
DR PRINTS; PR00601; BACFERRITIN.
DR SUPFAM; SSF47240; SSF47240; 1.
DR TIGRFAMs; TIGR00754; bfr; 1.
DR PROSITE; PS00549; BACTERIOFERRITIN; 1.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Heme; Iron; Iron storage; Metal-binding;
KW Oxidoreductase; Reference proteome; Virulence.
FT CHAIN 1..159
FT /note="Bacterioferritin BfrA"
FT /id="PRO_0000192600"
FT DOMAIN 1..145
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 18
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 51
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 51
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 52
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_note="ligand shared between dimeric partners"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 94
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT HELIX 5..34
FT /evidence="ECO:0007829|PDB:3UOI"
FT HELIX 38..64
FT /evidence="ECO:0007829|PDB:3UOI"
FT HELIX 83..110
FT /evidence="ECO:0007829|PDB:3UOI"
FT HELIX 114..144
FT /evidence="ECO:0007829|PDB:3UOI"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:3UOI"
SQ SEQUENCE 159 AA; 18341 MW; 098B6D7392A9CD60 CRC64;
MQGDPDVLRL LNEQLTSELT AINQYFLHSK MQDNWGFTEL AAHTRAESFD EMRHAEEITD
RILLLDGLPN YQRIGSLRIG QTLREQFEAD LAIEYDVLNR LKPGIVMCRE KQDTTSAVLL
EKIVADEEEH IDYLETQLEL MDKLGEELYS AQCVSRPPT
