ID L0EX80_LIBCB Unreviewed; 167 AA.
AC L0EX80;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Ferritin {ECO:0000256|RuleBase:RU361145};
DE EC=1.16.3.2 {ECO:0000256|RuleBase:RU361145};
GN OrderedLocusNames=B488_12760 {ECO:0000313|EMBL:AGA65268.1};
OS Liberibacter crescens (strain BT-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Liberibacter.
OX NCBI_TaxID=1215343 {ECO:0000313|EMBL:AGA65268.1, ECO:0000313|Proteomes:UP000010799};
RN [1] {ECO:0000313|EMBL:AGA65268.1, ECO:0000313|Proteomes:UP000010799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BT-1 {ECO:0000313|EMBL:AGA65268.1,
RC ECO:0000313|Proteomes:UP000010799};
RX PubMed=23408754; DOI=10.4056/sigs.3326772;
RA Leonard M.T., Fagen J.R., Davis-Richardson A.G., Davis M.J., Triplett E.W.;
RT "Complete genome sequence of Liberibacter crescens BT-1.";
RL Stand. Genomic Sci. 7:271-283(2012).
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; CP003789; AGA65268.1; -; Genomic_DNA.
DR RefSeq; WP_015273693.1; NC_019907.1.
DR AlphaFoldDB; L0EX80; -.
DR STRING; 1215343.B488_12760; -.
DR KEGG; lcc:B488_12760; -.
DR PATRIC; fig|1215343.11.peg.1317; -.
DR eggNOG; COG1528; Bacteria.
DR HOGENOM; CLU_065681_1_0_5; -.
DR Proteomes; UP000010799; 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:UP000010799}.
FT DOMAIN 1..145
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000259|PROSITE:PS50905"
SQ SEQUENCE 167 AA; 19279 MW; 1F5F0D6BB3585204 CRC64;
MNNEKIHKTL INLINTELEA HLFYLQAAAW AVSHNLQGCY NFLIKQANEE LSHMHKVFNY
LNEQGNKVTF SALQEQKIPV KDIKSLFQLI AEREFSVTQA YDKALEQTLS EKDNATFSFL
QWFINEQHEE NSLFRSILAE IDLIGEGPNS RYLIDQAIGK MADVKKS
//
