ID A0A075WTM3_9BACT Unreviewed; 173 AA.
AC A0A075WTM3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 08-NOV-2023, entry version 37.
DE RecName: Full=Ferritin {ECO:0000256|RuleBase:RU361145};
DE EC=1.16.3.2 {ECO:0000256|RuleBase:RU361145};
GN ORFNames=HL41_08025 {ECO:0000313|EMBL:AIH04609.1};
OS Thermodesulfobacterium commune DSM 2178.
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae;
OC Thermodesulfobacterium.
OX NCBI_TaxID=289377 {ECO:0000313|EMBL:AIH04609.1, ECO:0000313|Proteomes:UP000028481};
RN [1] {ECO:0000313|EMBL:AIH04609.1, ECO:0000313|Proteomes:UP000028481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2178 {ECO:0000313|EMBL:AIH04609.1,
RC ECO:0000313|Proteomes:UP000028481};
RX PubMed=25635017;
RA Bhatnagar S., Badger J.H., Madupu R., Khouri H.M., O'Connor E.M.,
RA Robb F.T., Ward N.L., Eisen J.A.;
RT "Genome Sequence of a Sulfate-Reducing Thermophilic Bacterium,
RT Thermodesulfobacterium commune DSM 2178T (Phylum Thermodesulfobacteria).";
RL Genome Announc. 3:0-0(2015).
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; CP008796; AIH04609.1; -; Genomic_DNA.
DR RefSeq; WP_028841728.1; NZ_JQLF01000006.1.
DR AlphaFoldDB; A0A075WTM3; -.
DR STRING; 289377.HL41_08025; -.
DR PaxDb; 289377-HL41_08025; -.
DR KEGG; tcm:HL41_08025; -.
DR eggNOG; COG1528; Bacteria.
DR HOGENOM; CLU_065681_1_2_0; -.
DR OrthoDB; 9801481at2; -.
DR Proteomes; UP000028481; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000028481}.
FT DOMAIN 1..144
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000259|PROSITE:PS50905"
SQ SEQUENCE 173 AA; 20348 MW; 6BEE67A7A1364CE5 CRC64;
MKKEIEAALN EQIKWEIYSG YLYLSMAAYF DDLGLDGFSK WMKAQTAEEF MHAMKFYKFV
VERDGKVILQ EIPAPPNKWD SPEAVFEFAY NHEKEVTKRI NQLVSLAKKL EDYATDNFLQ
WFVNEQVEEE ASFKTILSKL KLIKNDPQAL FYLDKELGQR PLDLNQLFLT PTE
//