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Protein

Organic hydroperoxide resistance transcriptional regulator

Gene

ohrR

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Organic peroxide sensor. Represses the expression of the peroxide-inducible gene ohrA by cooperative binding to two inverted repeat elements.1 Publication

Enzyme regulationi

Inactivated by oxidation of Cys-15 to a sulfenic acid.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi57 – 8024H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciBSUB:BSU13150-MONOMER.
RETL1328306-WGS:GSTH-1178-MONOMER.
RETL1328306-WGS:GSTH-2566-MONOMER.
RETL1328306-WGS:GSTH-2766-MONOMER.
RETL1328306-WGS:GSTH-3153-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Organic hydroperoxide resistance transcriptional regulator
Gene namesi
Name:ohrR
Synonyms:ykmA
Ordered Locus Names:BSU13150
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi15 – 151C → G or S: Full repressor activity, but no modulation by peroxide. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 147147Organic hydroperoxide resistance transcriptional regulatorPRO_0000054376Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki15 ↔ 16N,N-(cysteine-1,S-diyl)phenylalanine (Cys-Phe); alternate
Modified residuei15 – 151Cysteine sulfenic acid (-SOH); alternate1 Publication
Modified residuei15 – 151S-bacillithiol cysteine disulfide; alternate
Modified residuei15 – 151S-cysteinyl cysteine; alternate

Post-translational modificationi

Cys-15 is oxidized by organic peroxides to cysteine sulfenic acid (Cys-SOH). This can react with the alpha-amido of the following residue to form the sulfenamide cross-link. Oxidation or cross-linking results in the loss of DNA-binding activity and the inactivation of repressor function. Both the cysteine sulfenic acid and the sulfenamide cross-link can react with free cysteine or bacillithiol to form mixed disulfides. Further reduction of OhrR by free sulfhydryl compounds restores repressor activity.1 Publication

Keywords - PTMi

Oxidation

Proteomic databases

PaxDbiO34777.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100007281.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 123Combined sources
Helixi14 – 2613Combined sources
Helixi30 – 334Combined sources
Turni34 – 363Combined sources
Helixi40 – 5213Combined sources
Beta strandi53 – 564Combined sources
Helixi57 – 626Combined sources
Turni63 – 653Combined sources
Helixi68 – 8114Combined sources
Beta strandi83 – 853Combined sources
Beta strandi95 – 1006Combined sources
Helixi102 – 1054Combined sources
Helixi107 – 1104Combined sources
Turni111 – 1133Combined sources
Helixi114 – 1218Combined sources
Helixi127 – 14216Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z91X-ray2.50A1-147[»]
1Z9CX-ray2.64A/B/C/D/E/F1-147[»]
ProteinModelPortaliO34777.
SMRiO34777. Positions 8-144.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO34777.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 141131HTH marR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HTH marR-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105K56. Bacteria.
ENOG4111TPH. LUCA.
HOGENOMiHOG000221448.
InParanoidiO34777.
OMAiVFCASEC.
OrthoDBiEOG6SR975.
PhylomeDBiO34777.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000835. HTH_MarR-typ.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01047. MarR. 1 hit.
[Graphical view]
PRINTSiPR00598. HTHMARR.
SMARTiSM00347. HTH_MARR. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS50995. HTH_MARR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O34777-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENKFDHMKL ENQLCFLLYA SSREMTKQYK PLLDKLNITY PQYLALLLLW
60 70 80 90 100
EHETLTVKKM GEQLYLDSGT LTPMLKRMEQ QGLITRKRSE EDERSVLISL
110 120 130 140
TEDGALLKEK AVDIPGTILG LSKQSGEDLK QLKSALYTLL ETLHQKN
Length:147
Mass (Da):17,003
Last modified:January 1, 1998 - v1
Checksum:i4F277EA9AB5EE861
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002571 Genomic DNA. Translation: CAA05594.1.
AL009126 Genomic DNA. Translation: CAB13172.1.
PIRiE69857.
RefSeqiNP_389198.1. NC_000964.3.
WP_003245653.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13172; CAB13172; BSU13150.
GeneIDi939850.
KEGGibsu:BSU13150.
PATRICi18974387. VBIBacSub10457_1386.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002571 Genomic DNA. Translation: CAA05594.1.
AL009126 Genomic DNA. Translation: CAB13172.1.
PIRiE69857.
RefSeqiNP_389198.1. NC_000964.3.
WP_003245653.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z91X-ray2.50A1-147[»]
1Z9CX-ray2.64A/B/C/D/E/F1-147[»]
ProteinModelPortaliO34777.
SMRiO34777. Positions 8-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100007281.

Proteomic databases

PaxDbiO34777.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13172; CAB13172; BSU13150.
GeneIDi939850.
KEGGibsu:BSU13150.
PATRICi18974387. VBIBacSub10457_1386.

Phylogenomic databases

eggNOGiENOG4105K56. Bacteria.
ENOG4111TPH. LUCA.
HOGENOMiHOG000221448.
InParanoidiO34777.
OMAiVFCASEC.
OrthoDBiEOG6SR975.
PhylomeDBiO34777.

Enzyme and pathway databases

BioCyciBSUB:BSU13150-MONOMER.
RETL1328306-WGS:GSTH-1178-MONOMER.
RETL1328306-WGS:GSTH-2566-MONOMER.
RETL1328306-WGS:GSTH-2766-MONOMER.
RETL1328306-WGS:GSTH-3153-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO34777.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000835. HTH_MarR-typ.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01047. MarR. 1 hit.
[Graphical view]
PRINTSiPR00598. HTHMARR.
SMARTiSM00347. HTH_MARR. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS50995. HTH_MARR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the Bacillus subtilis genome between xlyA and ykoR."
    Devine K.M.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR."
    Lee J.W., Soonsanga S., Helmann J.D.
    Proc. Natl. Acad. Sci. U.S.A. 104:8743-8748(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 10-23, POST-TRANSLATIONAL MODIFICATIONS AT CYS-15.
  4. "OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis."
    Fuangthong M., Atichartpongkul S., Mongkolsuk S., Helmann J.D.
    J. Bacteriol. 183:4134-4141(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: 168.
  5. "The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative."
    Fuangthong M., Helmann J.D.
    Proc. Natl. Acad. Sci. U.S.A. 99:6690-6695(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: OXIDATION AT CYS-15, MUTAGENESIS OF CYS-15.
  6. Cited for: POST-TRANSLATIONAL MODIFICATION AT CYS-15.
  7. "Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family."
    Hong M., Fuangthong M., Helmann J.D., Brennan R.G.
    Mol. Cell 20:131-141(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-147, DIMERIZATION.

Entry informationi

Entry nameiOHRR_BACSU
AccessioniPrimary (citable) accession number: O34777
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: January 1, 1998
Last modified: February 17, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.