ID D5U7R8_BRAM5 Unreviewed; 176 AA.
AC D5U7R8;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Ferritin {ECO:0000256|RuleBase:RU361145};
DE EC=1.16.3.2 {ECO:0000256|RuleBase:RU361145};
GN OrderedLocusNames=Bmur_2797 {ECO:0000313|EMBL:ADG72864.1};
OS Brachyspira murdochii (strain ATCC 51284 / DSM 12563 / 56-150) (Serpulina
OS murdochii).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=526224 {ECO:0000313|EMBL:ADG72864.1, ECO:0000313|Proteomes:UP000001915};
RN [1] {ECO:0000313|EMBL:ADG72864.1, ECO:0000313|Proteomes:UP000001915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51284 / DSM 12563 / 56-150
RC {ECO:0000313|Proteomes:UP000001915};
RX PubMed=21304710; DOI=10.4056/sigs.831993;
RA Pati A., Sikorski J., Gronow S., Munk C., Lapidus A., Copeland A.,
RA Glavina Del Tio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F.,
RA Han C., Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Brachyspira murdochii type strain (56-150).";
RL Stand. Genomic Sci. 2:260-269(2010).
CC -!- FUNCTION: Iron-storage protein. {ECO:0000256|RuleBase:RU361145}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 6 H2O + O2 = 12 H(+) + 4 iron(III) oxide-hydroxide;
CC Xref=Rhea:RHEA:11972, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:78619; EC=1.16.3.2;
CC Evidence={ECO:0000256|RuleBase:RU361145};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU361145}.
CC -!- SIMILARITY: Belongs to the ferritin family. Prokaryotic subfamily.
CC {ECO:0000256|RuleBase:RU361145}.
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DR EMBL; CP001959; ADG72864.1; -; Genomic_DNA.
DR RefSeq; WP_013115200.1; NC_014150.1.
DR AlphaFoldDB; D5U7R8; -.
DR STRING; 526224.Bmur_2797; -.
DR KEGG; brm:Bmur_2797; -.
DR eggNOG; COG1528; Bacteria.
DR HOGENOM; CLU_065681_1_0_12; -.
DR OrthoDB; 9801481at2; -.
DR Proteomes; UP000001915; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR CDD; cd01055; Nonheme_Ferritin; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR001519; Ferritin.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009040; Ferritin-like_diiron.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR008331; Ferritin_DPS_dom.
DR InterPro; IPR041719; Ferritin_prok.
DR PANTHER; PTHR11431; FERRITIN; 1.
DR PANTHER; PTHR11431:SF75; FERRITIN; 1.
DR Pfam; PF00210; Ferritin; 1.
DR SUPFAM; SSF47240; Ferritin-like; 1.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU361145};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361145};
KW Iron storage {ECO:0000256|ARBA:ARBA00022434,
KW ECO:0000256|RuleBase:RU361145};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361145}.
FT DOMAIN 3..148
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000259|PROSITE:PS50905"
SQ SEQUENCE 176 AA; 20499 MW; 585E1E869D36BA3B CRC64;
MSIINNEETI KALNVQLNKE LYSASLYFNM ASWCDKQGLK GCSKFLYGHY REELEHFEKF
RDFINKVGGQ ATIGEMHAPQ NDFKSVEDLF ETVVKHEEYI TSCINELVGY SFDKKDYITL
RFLDWFIQEQ LEEQELFNDI LDKIKILGDL KGRNLYTFDK AIGNLDAEKH GTSVSL
//
