RUBY2_CLOAB
ID RUBY2_CLOAB Reviewed; 184 AA.
AC Q97ET8;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Rubrerythrin-2;
DE Short=Rr 2;
DE AltName: Full=NADH peroxidase;
DE Short=NPXase;
DE Short=Npx;
DE EC=1.11.1.1;
GN Name=rbr2; OrderedLocusNames=CA_C3018;
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 GENE NAME, AND INDUCTION.
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 NO 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 [4]
RP NO 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 [5]
RP NO INDUCTION BY O(2), AND NO 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) as the electron transport intermediary from NADH
CC to Rbr2. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250};
CC Note=Binds 3 Fe(3+) ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Rubredoxin (Rd) increases the NADH consumption
CC rate by serving as an intermediary electron-transfer shuttle between
CC NROR and Rbr2. {ECO:0000250}.
CC -!- INDUCTION: Various environmental stress conditions, e.g. oxidative
CC stress (exposure to H(2)O(2)) and other stress factors such as salt,
CC increased pH, high concentration of solvents or cold shock, do not lead
CC to increased transcript levels of this gene. However, PubMed:15336429
CC shows that rbr2 is slightly up-regulated after exposure to air, but
CC PubMed:19648241 shows it does not respond to the presence of O(2). Is
CC not repressed by PerR. {ECO:0000269|PubMed:15336429}.
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DR EMBL; AE001437; AAK80959.1; -; Genomic_DNA.
DR PIR; D97271; D97271.
DR RefSeq; NP_349619.1; NC_003030.1.
DR RefSeq; WP_010966300.1; NC_003030.1.
DR AlphaFoldDB; Q97ET8; -.
DR SMR; Q97ET8; -.
DR STRING; 272562.CA_C3018; -.
DR EnsemblBacteria; AAK80959; AAK80959; CA_C3018.
DR GeneID; 44999505; -.
DR KEGG; cac:CA_C3018; -.
DR PATRIC; fig|272562.8.peg.3201; -.
DR eggNOG; COG1592; Bacteria.
DR HOGENOM; CLU_095256_1_0_9; -.
DR OMA; AYAEFVH; -.
DR OrthoDB; 1681849at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016692; F:NADH peroxidase activity; IEA:UniProtKB-EC.
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 Electron transport; Iron; Metal-binding; NAD; Oxidoreductase; Peroxidase;
KW Reference proteome; Transport.
FT CHAIN 1..184
FT /note="Rubrerythrin-2"
FT /id="PRO_0000405533"
FT DOMAIN 2..146
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT DOMAIN 151..184
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00241"
FT BINDING 19
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 52
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 52
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 94
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 97
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 128
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 128
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 131
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 156
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 159
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 171
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
FT BINDING 174
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P24931"
SQ SEQUENCE 184 AA; 20869 MW; C66C44E73B107AD5 CRC64;
MSVKNAMTAD FLRSAYGGES MAHMRYLIWG EEAENSNYPN IGRLFKAIAY SEHIHAKNHF
NVLKEDLYDS SVVAGAVFGS TNLIDNLQGA INGELHEIKQ MYPVYLETAR YQEEKEAERT
FHYALEAEKI HAKLFQDAQD SAKENKDINI GKVYICPVCG FTTLDENIEQ CPICGVKKDK
FQAF
