RUBY_PORGI
ID RUBY_PORGI Reviewed; 200 AA.
AC Q9AGG3;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Rubrerythrin;
DE Short=Rr;
GN Name=rbr; OrderedLocusNames=PG_0195;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=11972784; DOI=10.1046/j.1365-2958.2002.02892.x;
RA Sztukowska M., Bugno M., Potempa J., Travis J., Kurtz D.M. Jr.;
RT "Role of rubrerythrin in the oxidative stress response of Porphyromonas
RT gingivalis.";
RL Mol. Microbiol. 44:479-488(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
CC -!- FUNCTION: May provide oxidative stress protection via catalytic
CC reduction of intracellular hydrogen peroxide.
CC {ECO:0000303|PubMed:11972784}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P24931}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By exposure to dioxygen and hydrogen peroxide.
CC {ECO:0000269|PubMed:11972784}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ65429.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF333323; AAK19552.1; -; Genomic_DNA.
DR EMBL; AE015924; AAQ65429.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q9AGG3; -.
DR SMR; Q9AGG3; -.
DR STRING; 242619.PG_0195; -.
DR EnsemblBacteria; AAQ65429; AAQ65429; PG_0195.
DR KEGG; pgi:PG_0195; -.
DR eggNOG; COG1592; Bacteria.
DR HOGENOM; CLU_095256_0_1_10; -.
DR OMA; PQAYFEV; -.
DR Proteomes; UP000000588; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; NAS:UniProtKB.
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 2: Evidence at transcript level;
KW Cytoplasm; Electron transport; Iron; Metal-binding; Reference proteome;
KW Transport.
FT CHAIN 1..200
FT /note="Rubrerythrin"
FT /id="PRO_0000135066"
FT DOMAIN 12..155
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT DOMAIN 162..200
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT BINDING 29
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 62
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 62
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 103
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 106
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 137
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 137
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 140
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 167
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 170
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 183
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 186
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
SQ SEQUENCE 200 AA; 22456 MW; D16595E07C081D66 CRC64;
MSIKKKTEMN KSIKGSKTEK HLLMAFAGES QARSRYTFFA SVAKKEGYEQ IAGVFMETAE
QEKEHAKRFF SFLEGGMLEI TASFPAGIIG STAENLRAAA AGENEEWTDL YPAFAETAEE
EGFKEIAAVF RQIAKVEAEH ERRYLALLAH VEDGSVFERT EEIAWQCRNC GYVITSKKAP
KLCPACAHPQ AYFEPMKTNY
