RRBR1_CLOAB
ID RRBR1_CLOAB Reviewed; 181 AA.
AC Q97D82;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Reverse rubrerythrin-1;
DE Short=revRbr 1;
DE AltName: Full=NADH peroxidase;
DE Short=NPXase;
DE Short=Npx;
DE EC=1.11.1.1;
DE AltName: Full=Rubperoxin 1;
DE Short=Rpr 1;
GN Name=rbr3A; Synonyms=hsp21, rpr1; OrderedLocusNames=CA_C3598;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
RN [2]
RP PROTEIN SEQUENCE OF 1-20, GENE NAME, AND INDUCTION BY HEAT; AIR AND
RP H(2)O(2).
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=15336429; DOI=10.1111/j.1574-6968.2004.tb09763.x;
RA May A., Hillmann F., Riebe O., Fischer R.J., Bahl H.;
RT "A rubrerythrin-like oxidative stress protein of Clostridium acetobutylicum
RT is encoded by a duplicated gene and identical to the heat shock protein
RT Hsp21.";
RL FEMS Microbiol. Lett. 238:249-254(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION BY O(2).
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=15280011; DOI=10.1016/j.febslet.2004.06.047;
RA Kawasaki S., Ishikura J., Watamura Y., Niimura Y.;
RT "Identification of O2-induced peptides in an obligatory anaerobe,
RT Clostridium acetobutylicum.";
RL FEBS Lett. 571:21-25(2004).
RN [4]
RP INDUCTION BY VARIOUS ENVIRONMENTAL STRESS CONDITIONS.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=16463182; DOI=10.1007/s00203-006-0091-y;
RA Hillmann F., Fischer R.J., Bahl H.;
RT "The rubrerythrin-like protein Hsp21 of Clostridium acetobutylicum is a
RT general stress protein.";
RL Arch. Microbiol. 185:270-276(2006).
RN [5]
RP H(2)O(2) REDUCTASE ACTIVITY, IRON-BINDING, AND SUBUNIT.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=17485086; DOI=10.1016/j.febslet.2007.04.050;
RA Kawasaki S., Ono M., Watamura Y., Sakai Y., Satoh T., Arai T., Satoh J.,
RA Niimura Y.;
RT "An O2-inducible rubrerythrin-like protein, rubperoxin, is functional as a
RT H2O2 reductase in an obligatory anaerobe Clostridium acetobutylicum.";
RL FEBS Lett. 581:2460-2464(2007).
RN [6]
RP REPRESSION BY PERR.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=18430081; DOI=10.1111/j.1365-2958.2008.06192.x;
RA Hillmann F., Fischer R.J., Saint-Prix F., Girbal L., Bahl H.;
RT "PerR acts as a switch for oxygen tolerance in the strict anaerobe
RT Clostridium acetobutylicum.";
RL Mol. Microbiol. 68:848-860(2008).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=19124587; DOI=10.1128/aem.01425-08;
RA Kawasaki S., Sakai Y., Takahashi T., Suzuki I., Niimura Y.;
RT "O2 and reactive oxygen species detoxification complex, composed of O2-
RT responsive NADH:rubredoxin oxidoreductase-flavoprotein A2-desulfoferrodoxin
RT operon enzymes, rubperoxin, and rubredoxin, in Clostridium
RT acetobutylicum.";
RL Appl. Environ. Microbiol. 75:1021-1029(2009).
RN [8]
RP INDUCTION BY O(2), AND REPRESSION BY PERR.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=19648241; DOI=10.1128/jb.00351-09;
RA Hillmann F., Doring C., Riebe O., Ehrenreich A., Fischer R.J., Bahl H.;
RT "The role of PerR in O2-affected gene expression of Clostridium
RT acetobutylicum.";
RL J. Bacteriol. 191:6082-6093(2009).
CC -!- FUNCTION: Functions as the terminal component of an NADH peroxidase
CC (NADH:H(2)O(2) oxidoreductase) when using NADH:rubredoxin
CC oxidoreductase (NROR) and rubredoxin (Rd) as electron transport
CC intermediaries from NADH to revRbr 1. Plays an important role in the
CC oxidative stress defense system in C.acetobutylicum, an obligate
CC anaerobic bacterium. Also exhibits NADH oxidase (NADH:O(2)
CC oxidoreductase) activity in vitro, which is 100-fold lesser than that
CC of FprA1/2 using the same electron transfer components. Therefore, its
CC predominant function is most likely as a scavenger of its preferred
CC substrate, H(2)O(2). {ECO:0000269|PubMed:19124587}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O2 + NADH = 2 H2O + NAD(+); Xref=Rhea:RHEA:18509,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.11.1.1;
CC Evidence={ECO:0000269|PubMed:19124587};
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. {ECO:0000269|PubMed:17485086}.
CC -!- INDUCTION: Up-regulated by heat and oxidative stress (exposure to air,
CC O(2) and H(2)O(2)) (at mRNA and protein levels). Various other
CC environmental stress conditions such as an increase of the pH of the
CC growth medium from 4.5 to 6.2, addition of the salt NaCl or of the
CC solvent butanol, and lowering the incubation temperature also result in
CC transiently increased transcript levels. Is also expressed under non-
CC stressful conditions. Repressed by PerR. {ECO:0000269|PubMed:15280011,
CC ECO:0000269|PubMed:15336429, ECO:0000269|PubMed:16463182,
CC ECO:0000269|PubMed:18430081, ECO:0000269|PubMed:19648241}.
CC -!- MISCELLANEOUS: This protein has been named 'reverse' rubrerythrin
CC (revRbr) because the order of the two functional domains is reversed
CC compared to 'classical' rubrerythrins: the rubredoxin-like FeS4 domain
CC is located at the N-terminus and the ferritin-like diiron domain at the
CC C-terminus.
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DR EMBL; AE001437; AAK81521.1; -; Genomic_DNA.
DR PIR; F97341; F97341.
DR RefSeq; NP_350181.1; NC_003030.1.
DR RefSeq; WP_010966861.1; NC_003030.1.
DR AlphaFoldDB; Q97D82; -.
DR SMR; Q97D82; -.
DR STRING; 272562.CA_C3598; -.
DR EnsemblBacteria; AAK81521; AAK81521; CA_C3598.
DR GeneID; 45000096; -.
DR KEGG; cac:CA_C3598; -.
DR PATRIC; fig|272562.8.peg.3787; -.
DR eggNOG; COG1592; Bacteria.
DR eggNOG; COG1773; Bacteria.
DR HOGENOM; CLU_113705_1_0_9; -.
DR OMA; NFEGECK; -.
DR OrthoDB; 1681849at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0016692; F:NADH peroxidase activity; ISS:UniProtKB.
DR GO; GO:0071469; P:cellular response to alkaline pH; IDA:UniProtKB.
DR GO; GO:0070417; P:cellular response to cold; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
DR GO; GO:0071453; P:cellular response to oxygen levels; IDA:UniProtKB.
DR GO; GO:0071472; P:cellular response to salt stress; IDA:UniProtKB.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; ISS:UniProtKB.
DR CDD; cd01046; Rubrerythrin_like; 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 InterPro; IPR045236; Rubrerythrin-like.
DR Pfam; PF02915; Rubrerythrin; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW Detoxification; Direct protein sequencing; Electron transport; Iron;
KW Metal-binding; NAD; Oxidoreductase; Peroxidase; Reference proteome;
KW Stress response; Transport.
FT CHAIN 1..181
FT /note="Reverse rubrerythrin-1"
FT /id="PRO_0000405534"
FT DOMAIN 1..35
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT DOMAIN 52..181
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 6
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 22
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 25
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 181 AA; 20093 MW; 18056F8FBD6D1C93 CRC64;
MKKFKCVVCG YIYTGEDAPE KCPVCGAGKD KFVEVKDEGE GWADEHKIGV AKGVDKEVLE
GLRANFTGEC TEVGMYLAMA RQADREGYPE VAEAYKRIAF EEAEHASKFA ELLGEVVVAD
TKTNLQMRVD AEKGACEGKK ELATLAKKLN YDAIHDTVHE MCKDEARHGS AFRGLLNRYF
K
