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ID D3VHQ8_XENNA Unreviewed; 158 AA.
AC D3VHQ8;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 16-JAN-2019, entry version 57.
DE RecName: Full=Bacterioferritin {ECO:0000256|PIRNR:PIRNR002560, ECO:0000256|RuleBase:RU000623};
DE EC=1.16.3.1 {ECO:0000256|PIRNR:PIRNR002560};
GN Name=bfr {ECO:0000313|EMBL:CBJ88397.1};
GN OrderedLocusNames=XNC1_0315 {ECO:0000313|EMBL:CBJ88397.1};
OS Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS NCIB 9965 / AN6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88397.1, ECO:0000313|Proteomes:UP000008075};
RN [1] {ECO:0000313|Proteomes:UP000008075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC {ECO:0000313|Proteomes:UP000008075};
RA Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA Suen G.;
RT "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBJ88397.1, ECO:0000313|Proteomes:UP000008075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC {ECO:0000313|Proteomes:UP000008075};
RX PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT photorhabdus: convergent lifestyles from divergent genomes.";
RL PLoS ONE 6:e27909-e27909(2011).
CC -!- FUNCTION: Iron-storage protein, whose ferroxidase center binds
CC Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates
CC in the subsequent Fe(3+) oxide mineral core formation within the
CC central cavity of the protein complex.
CC {ECO:0000256|PIRNR:PIRNR002560}.
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;
CC EC=1.16.3.1; Evidence={ECO:0000256|PIRNR:PIRNR002560};
CC -!- SIMILARITY: Belongs to the bacterioferritin family.
CC {ECO:0000256|PIRNR:PIRNR002560, ECO:0000256|RuleBase:RU000623}.
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DR EMBL; FN667742; CBJ88397.1; -; Genomic_DNA.
DR RefSeq; WP_010847475.1; NC_014228.1.
DR STRING; 406817.XNC1_0315; -.
DR EnsemblBacteria; CBJ88397; CBJ88397; XNC1_0315.
DR KEGG; xne:XNC1_0315; -.
DR eggNOG; ENOG4108UQY; Bacteria.
DR eggNOG; COG2193; LUCA.
DR HOGENOM; HOG000262383; -.
DR KO; K03594; -.
DR OMA; TPEMLKC; -.
DR Proteomes; UP000008075; Chromosome.
DR GO; GO:0005623; C:cell; IEA:GOC.
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 3: Inferred from homology;
DR PRODOM; D3VHQ8.
DR SWISS-2DPAGE; D3VHQ8.
KW Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW Heme {ECO:0000256|PIRNR:PIRNR002560, ECO:0000256|RuleBase:RU000623};
KW Iron {ECO:0000256|PIRNR:PIRNR002560, ECO:0000256|PIRSR:PIRSR002560-1,
KW ECO:0000256|RuleBase:RU000623};
KW Iron storage {ECO:0000256|PIRNR:PIRNR002560,
KW ECO:0000256|RuleBase:RU000623};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR002560,
KW ECO:0000256|PIRSR:PIRSR002560-1, ECO:0000256|RuleBase:RU000623};
KW Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT DOMAIN 1 145 Ferritin-like diiron.
FT {ECO:0000259|PROSITE:PS50905}.
FT METAL 18 18 Iron 1. {ECO:0000256|PIRSR:PIRSR002560-
FT 1}.
FT METAL 46 46 Iron 3. {ECO:0000256|PIRSR:PIRSR002560-
FT 1}.
FT METAL 50 50 Iron 3. {ECO:0000256|PIRSR:PIRSR002560-
FT 1}.
FT METAL 51 51 Iron 1. {ECO:0000256|PIRSR:PIRSR002560-
FT 1}.
FT METAL 51 51 Iron 2. {ECO:0000256|PIRSR:PIRSR002560-
FT 1}.
FT METAL 52 52 Iron (heme axial ligand); shared with
FT dimeric partner. {ECO:0000256|PIRSR:
FT PIRSR002560-1}.
FT METAL 54 54 Iron 1. {ECO:0000256|PIRSR:PIRSR002560-
FT 1}.
FT METAL 94 94 Iron 2. {ECO:0000256|PIRSR:PIRSR002560-
FT 1}.
FT METAL 127 127 Iron 1. {ECO:0000256|PIRSR:PIRSR002560-
FT 1}.
FT METAL 127 127 Iron 2. {ECO:0000256|PIRSR:PIRSR002560-
FT 1}.
FT METAL 130 130 Iron 2. {ECO:0000256|PIRSR:PIRSR002560-
FT 1}.
SQ SEQUENCE 158 AA; 18421 MW; 09EF9BCABB608AFF CRC64;
MKGDKKIIAH LNKLLGNELV AINQYFLHAR MFKNWGLMRL NEVEYHESID EMKHADKFIE
RILFLEGLPN LQDLGKLNIG EDVEEMLRSD LDLELRGAKD LREAIAYADS VHDYVSRDLM
IEVLADEENH IDWLETQLEL ITRIGIQNYI QSQLAEAE
//
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