RUBY_CLOPE
ID RUBY_CLOPE Reviewed; 195 AA.
AC P51591;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Rubrerythrin;
DE Short=Rr;
GN Name=rbr; Synonyms=rubY; OrderedLocusNames=CPE0135;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10543 / DSM 798 / NCIB 8875 / BP6K / Type A;
RX PubMed=8955396; DOI=10.1128/jb.178.24.7152-7158.1996;
RA Lehmann Y., Meile L., Teuber M.;
RT "Rubrerythrin from Clostridium perfringens: cloning of the gene,
RT purification of the protein, and characterization of its superoxide
RT dismutase function.";
RL J. Bacteriol. 178:7152-7158(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC -!- FUNCTION: May provide oxidative stress protection via catalytic
CC reduction of intracellular hydrogen peroxide. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250};
CC Note=Binds 3 Fe(3+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. Possesses two rubredoxin-like centers and two non-
CC sulfur oxo-bridged di-iron centers per dimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR EMBL; X92844; CAA63429.1; -; Genomic_DNA.
DR EMBL; BA000016; BAB79841.1; -; Genomic_DNA.
DR RefSeq; WP_011009633.1; NC_003366.1.
DR AlphaFoldDB; P51591; -.
DR SMR; P51591; -.
DR EnsemblBacteria; BAB79841; BAB79841; BAB79841.
DR KEGG; cpe:CPE0135; -.
DR HOGENOM; CLU_095256_0_1_9; -.
DR OMA; PQAYFEV; -.
DR Proteomes; UP000000818; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd01041; Rubrerythrin; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009040; Ferritin-like_diiron.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR003251; Rubrerythrin.
DR Pfam; PF02915; Rubrerythrin; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Electron transport; Iron; Metal-binding; Reference proteome;
KW Transport.
FT CHAIN 1..195
FT /note="Rubrerythrin"
FT /id="PRO_0000135065"
FT DOMAIN 1..150
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT DOMAIN 157..195
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT BINDING 20
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 53
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 53
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 98
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 101
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 132
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 132
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 135
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 162
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 165
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 178
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 181
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT CONFLICT 146
FT /note="I -> M (in Ref. 1; CAA63429)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="Y -> F (in Ref. 1; CAA63429)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 195 AA; 22158 MW; 6E67C73C9342532C CRC64;
MKSLKGTKTA ENLMKSFAGE CQARTRYTYF SSTARKEGYV QISNIFLETA ENEKEHAKRF
YKFLKDDLQG EAVEINAAYP VELPTDTLTN LKFAAEGEHD ELSNLYPSFA DVADEEGFPE
VAAAFRMIAK AETAHYNRFM KLAKNIEEGK VFKKDEVVLW KCGNCGFIWE GAEAPLKCPA
CLHPQAYFEV FKETY
