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BFR_MYCPA
ID   BFR_MYCPA               Reviewed;         159 AA.
AC   P45430;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Bacterioferritin;
DE            Short=BFR;
DE            EC=1.16.3.1;
DE   AltName: Full=Antigen D;
GN   Name=bfr; Synonyms=bfrA; OrderedLocusNames=MAP_1595;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-42.
RC   STRAIN=C-286;
RX   PubMed=1761687; DOI=10.1128/jcm.29.8.1652-1658.1991;
RA   Brooks B.W., Young N.M., Watson D.C., Robertson R.H., Sugden E.A.,
RA   Nielsen K.H., Becker S.A.;
RT   "Mycobacterium paratuberculosis antigen D: characterization and evidence
RT   that it is a bacterioferritin.";
RL   J. Clin. Microbiol. 29:1652-1658(1991).
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; Evidence={ECO:0000250};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC       {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
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       {ECO:0000250};
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:0000250}.
CC   -!- SIMILARITY: Belongs to the bacterioferritin family. {ECO:0000305}.
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DR   EMBL; AE016958; AAS03912.1; -; Genomic_DNA.
DR   PIR; A44893; A44893.
DR   RefSeq; WP_003876561.1; NC_002944.2.
DR   AlphaFoldDB; P45430; -.
DR   STRING; 262316.MAP_1595; -.
DR   EnsemblBacteria; AAS03912; AAS03912; MAP_1595.
DR   GeneID; 66694109; -.
DR   KEGG; mpa:MAP_1595; -.
DR   eggNOG; COG2193; Bacteria.
DR   HOGENOM; CLU_104506_2_0_11; -.
DR   OMA; YQRLFHV; -.
DR   Proteomes; UP000000580; Chromosome.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
DR   GO; GO:0006826; P:iron ion transport; IEA:InterPro.
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   Direct protein sequencing; Heme; Iron; Iron storage; Metal-binding;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..159
FT                   /note="Bacterioferritin"
FT                   /id="PRO_0000192602"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         51
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         51
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         94
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         127
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         127
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         130
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
SQ   SEQUENCE   159 AA;  18479 MW;  65BEF1425437EEBA CRC64;
     MQGDPEVLRL LNEQLTSELT AINQYFLHSK MQDNWGFTEL AEHTRAESFD EMRHAEAITD
     RILLLDGLPN YQRLFSLRIG QTLREQFEAD LAIEYEVMDR LKPAIILCRE KQDSTTATLF
     EQIVADEEKH IDYLETQLEL MDKLGVELYS AQCVSRPPS
 
 
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