OHRR_BACSU
ID OHRR_BACSU Reviewed; 147 AA.
AC O34777;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Organic hydroperoxide resistance transcriptional regulator;
GN Name=ohrR; Synonyms=ykmA; OrderedLocusNames=BSU13150;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Devine K.M.;
RT "Sequence of the Bacillus subtilis genome between xlyA and ykoR.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PROTEIN SEQUENCE OF 10-23, AND POST-TRANSLATIONAL MODIFICATIONS AT CYS-15.
RX PubMed=17502599; DOI=10.1073/pnas.0702081104;
RA Lee J.W., Soonsanga S., Helmann J.D.;
RT "A complex thiolate switch regulates the Bacillus subtilis organic peroxide
RT sensor OhrR.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8743-8748(2007).
RN [4]
RP FUNCTION.
RC STRAIN=168;
RX PubMed=11418552; DOI=10.1128/jb.183.14.4134-4141.2001;
RA Fuangthong M., Atichartpongkul S., Mongkolsuk S., Helmann J.D.;
RT "OhrR is a repressor of ohrA, a key organic hydroperoxide resistance
RT determinant in Bacillus subtilis.";
RL J. Bacteriol. 183:4134-4141(2001).
RN [5]
RP OXIDATION AT CYS-15, AND MUTAGENESIS OF CYS-15.
RX PubMed=11983871; DOI=10.1073/pnas.102483199;
RA Fuangthong M., Helmann J.D.;
RT "The OhrR repressor senses organic hydroperoxides by reversible formation
RT of a cysteine-sulfenic acid derivative.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6690-6695(2002).
RN [6]
RP POST-TRANSLATIONAL MODIFICATION AT CYS-15.
RX PubMed=19578333; DOI=10.1038/nchembio.189;
RA Newton G.L., Rawat M., La Clair J.J., Jothivasan V.K., Budiarto T.,
RA Hamilton C.J., Claiborne A., Helmann J.D., Fahey R.C.;
RT "Bacillithiol is an antioxidant thiol produced in Bacilli.";
RL Nat. Chem. Biol. 5:625-627(2009).
RN [7]
RP FUNCTION, PTM, AND POST-TRANSLATIONAL MODIFICATION AT CYS-15.
RX PubMed=24313874; DOI=10.1089/ars.2013.5327;
RA Gaballa A., Chi B.K., Roberts A.A., Becher D., Hamilton C.J., Antelmann H.,
RA Helmann J.D.;
RT "Redox regulation in Bacillus subtilis: The bacilliredoxins BrxA(YphP) and
RT BrxB(YqiW) function in de-bacillithiolation of S-bacillithiolated OhrR and
RT MetE.";
RL Antioxid. Redox Signal. 21:357-367(2014).
RN [8]
RP PTM, AND POST-TRANSLATIONAL MODIFICATION AT CYS-15.
RX PubMed=33722570; DOI=10.1016/j.redox.2021.101935;
RA Gaballa A., Su T.T., Helmann J.D.;
RT "The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr
RT (YpdA) disulfide reductase reduce S-bacillithiolated proteins.";
RL Redox Biol. 42:101935-101935(2021).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-147, AND DIMERIZATION.
RX PubMed=16209951; DOI=10.1016/j.molcel.2005.09.013;
RA Hong M., Fuangthong M., Helmann J.D., Brennan R.G.;
RT "Structure of an OhrR-ohrA operator complex reveals the DNA binding
RT mechanism of the MarR family.";
RL Mol. Cell 20:131-141(2005).
CC -!- FUNCTION: Organic peroxide sensor (PubMed:11418552). Represses the
CC expression of the peroxide-inducible gene ohrA by cooperative binding
CC to two inverted repeat elements (PubMed:11418552, PubMed:24313874).
CC {ECO:0000269|PubMed:11418552, ECO:0000269|PubMed:24313874}.
CC -!- ACTIVITY REGULATION: Inactivated by oxidation of Cys-15 to a sulfenic
CC acid.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Cys-15 is oxidized by organic peroxides to cysteine sulfenic acid
CC (Cys-SOH). This can react with the alpha-amido of the following residue
CC to form the sulfenamide cross-link. Oxidation or cross-linking results
CC in the loss of DNA-binding activity and the inactivation of repressor
CC function. Both the cysteine sulfenic acid and the sulfenamide cross-
CC link can react with free cysteine or bacillithiol (BSH) to form mixed
CC disulfides. Further reduction of OhrR by free sulfhydryl compounds
CC restores repressor activity. {ECO:0000269|PubMed:11983871,
CC ECO:0000269|PubMed:17502599, ECO:0000269|PubMed:19578333,
CC ECO:0000269|PubMed:24313874, ECO:0000269|PubMed:33722570}.
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DR EMBL; AJ002571; CAA05594.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13172.1; -; Genomic_DNA.
DR PIR; E69857; E69857.
DR RefSeq; NP_389198.1; NC_000964.3.
DR RefSeq; WP_003245653.1; NZ_JNCM01000035.1.
DR PDB; 1Z91; X-ray; 2.50 A; A=1-147.
DR PDB; 1Z9C; X-ray; 2.64 A; A/B/C/D/E/F=1-147.
DR PDBsum; 1Z91; -.
DR PDBsum; 1Z9C; -.
DR AlphaFoldDB; O34777; -.
DR SMR; O34777; -.
DR STRING; 224308.BSU13150; -.
DR PaxDb; O34777; -.
DR PRIDE; O34777; -.
DR EnsemblBacteria; CAB13172; CAB13172; BSU_13150.
DR GeneID; 939850; -.
DR KEGG; bsu:BSU13150; -.
DR PATRIC; fig|224308.179.peg.1427; -.
DR eggNOG; COG1846; Bacteria.
DR InParanoid; O34777; -.
DR OMA; MMVLWER; -.
DR PhylomeDB; O34777; -.
DR BioCyc; BSUB:BSU13150-MON; -.
DR EvolutionaryTrace; O34777; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000835; HTH_MarR-typ.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01047; MarR; 1.
DR PRINTS; PR00598; HTHMARR.
DR SMART; SM00347; HTH_MARR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50995; HTH_MARR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; DNA-binding; Oxidation;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..147
FT /note="Organic hydroperoxide resistance transcriptional
FT regulator"
FT /id="PRO_0000054376"
FT DOMAIN 11..141
FT /note="HTH marR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00345"
FT DNA_BIND 57..80
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00345"
FT MOD_RES 15
FT /note="Cysteine sulfenic acid (-SOH); alternate"
FT /evidence="ECO:0000269|PubMed:11983871"
FT MOD_RES 15
FT /note="S-bacillithiol cysteine disulfide; alternate"
FT /evidence="ECO:0000305|PubMed:24313874,
FT ECO:0000305|PubMed:33722570"
FT MOD_RES 15
FT /note="S-cysteinyl cysteine; alternate"
FT /evidence="ECO:0000269|PubMed:24313874"
FT CROSSLNK 15..16
FT /note="N,N-(cysteine-1,S-diyl)phenylalanine (Cys-Phe);
FT alternate"
FT MUTAGEN 15
FT /note="C->G,S: Full repressor activity, but no modulation
FT by peroxide."
FT /evidence="ECO:0000269|PubMed:11983871"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1Z91"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:1Z91"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:1Z91"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:1Z91"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:1Z91"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1Z91"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:1Z91"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1Z91"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:1Z91"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1Z91"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:1Z91"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1Z91"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:1Z91"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1Z91"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:1Z91"
FT HELIX 127..142
FT /evidence="ECO:0007829|PDB:1Z91"
SQ SEQUENCE 147 AA; 17003 MW; 4F277EA9AB5EE861 CRC64;
MENKFDHMKL ENQLCFLLYA SSREMTKQYK PLLDKLNITY PQYLALLLLW EHETLTVKKM
GEQLYLDSGT LTPMLKRMEQ QGLITRKRSE EDERSVLISL TEDGALLKEK AVDIPGTILG
LSKQSGEDLK QLKSALYTLL ETLHQKN
