ID W8KUV8_9GAMM Unreviewed; 172 AA.
AC W8KUV8;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Ferritin {ECO:0000256|RuleBase:RU361145};
DE EC=1.16.3.2 {ECO:0000256|RuleBase:RU361145};
GN ORFNames=M911_09635 {ECO:0000313|EMBL:AHK79366.1};
OS Ectothiorhodospira haloalkaliphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=421628 {ECO:0000313|EMBL:AHK79366.1, ECO:0000313|Proteomes:UP000019442};
RN [1] {ECO:0000313|EMBL:AHK79366.1, ECO:0000313|Proteomes:UP000019442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A {ECO:0000313|EMBL:AHK79366.1,
RC ECO:0000313|Proteomes:UP000019442};
RX PubMed=25057327; DOI=10.7150/jgen.9123;
RA Singh K.S., Kirksey J., Hoff W.D., Deole R.;
RT "Draft Genome Sequence of the Extremely Halophilic Phototrophic Purple
RT Sulfur Bacterium Halorhodospira halochloris.";
RL J Genomics 2:118-120(2014).
RN [2] {ECO:0000313|Proteomes:UP000019442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A {ECO:0000313|Proteomes:UP000019442};
RA Singh K.S.;
RT "Draft Genome Sequence of extremely halophilic bacteria Halorhodospira
RT halochloris.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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; CP007268; AHK79366.1; -; Genomic_DNA.
DR AlphaFoldDB; W8KUV8; -.
DR KEGG; hhc:M911_09635; -.
DR HOGENOM; CLU_065681_1_2_6; -.
DR OrthoDB; 9801481at2; -.
DR Proteomes; UP000019442; 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:UP000019442}.
FT DOMAIN 1..145
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000259|PROSITE:PS50905"
SQ SEQUENCE 172 AA; 19063 MW; D010B31A6F0DFC84 CRC64;
MISTAMAEKI SNQINREFYS AYLYLALSTE ADNANLRGAA EWFMAKYHEE SAHGLKMVRY
LLDQGAEVTH GAITAPPSQT GSLLAMFERT LEHEQQVTAA IHDIVDQALS EKDHATNIFM
HWFVTEQIEE EATVSDILGR LRLFGDRSEG LLMIDNELAA AAKSMGQGES VA
//
