YODB_BACSU
ID YODB_BACSU Reviewed; 112 AA.
AC O34844;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=HTH-type transcriptional regulator YodB;
GN Name=yodB; OrderedLocusNames=BSU19540;
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;
RX PubMed=9734814; DOI=10.1093/dnares/5.3.195;
RA Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A., Ehrlich S.D.,
RA Park S.-H.;
RT "Sequence analysis of the Bacillus subtilis 168 chromosome region between
RT the sspC and odhA loci (184 degrees-180 degrees).";
RL DNA Res. 5:195-201(1998).
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 INDUCTION.
RC STRAIN=168;
RX PubMed=17407181; DOI=10.1002/pmic.200700008;
RA Nguyen V.D., Wolf C., Maeder U., Lalk M., Langer P., Lindequist U.,
RA Hecker M., Antelmann H.;
RT "Transcriptome and proteome analyses in response to 2-methylhydroquinone
RT and 6-brom-2-vinyl-chroman-4-on reveal different degradation systems
RT involved in the catabolism of aromatic compounds in Bacillus subtilis.";
RL Proteomics 7:1391-1408(2007).
RN [4]
RP FUNCTION, AND INDUCTION.
RC STRAIN=168;
RX PubMed=18208493; DOI=10.1111/j.1365-2958.2008.06110.x;
RA Leelakriangsak M., Huyen N.T.T., Toewe S., van Duy N., Becher D.,
RA Hecker M., Antelmann H., Zuber P.;
RT "Regulation of quinone detoxification by the thiol stress sensing
RT DUF24/MarR-like repressor, YodB in Bacillus subtilis.";
RL Mol. Microbiol. 67:1108-1124(2008).
CC -!- FUNCTION: Negatively regulates yodC and azoR1 which may contribute to
CC the degradation of aromatic compounds. Probably positively regulates
CC the catechol-specific transcription of mhqNOP, mhqED, and mhqA.
CC {ECO:0000269|PubMed:18208493}.
CC -!- INDUCTION: Repressed by 2-methylhydroquinone (2-MHQ), diamide and
CC catechol stress. {ECO:0000269|PubMed:17407181,
CC ECO:0000269|PubMed:18208493}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF006665; AAB81174.1; -; Genomic_DNA.
DR EMBL; AF015775; AAB72060.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13845.1; -; Genomic_DNA.
DR PIR; G69902; G69902.
DR RefSeq; NP_389835.1; NC_000964.3.
DR RefSeq; WP_004399427.1; NZ_JNCM01000036.1.
DR PDB; 5HS7; X-ray; 1.70 A; A/B=5-112.
DR PDB; 5HS8; X-ray; 2.00 A; A=5-112.
DR PDB; 5HS9; X-ray; 2.10 A; A/B=5-112.
DR PDBsum; 5HS7; -.
DR PDBsum; 5HS8; -.
DR PDBsum; 5HS9; -.
DR AlphaFoldDB; O34844; -.
DR SMR; O34844; -.
DR STRING; 224308.BSU19540; -.
DR PaxDb; O34844; -.
DR PRIDE; O34844; -.
DR EnsemblBacteria; CAB13845; CAB13845; BSU_19540.
DR GeneID; 939449; -.
DR KEGG; bsu:BSU19540; -.
DR PATRIC; fig|224308.179.peg.2136; -.
DR eggNOG; COG1733; Bacteria.
DR InParanoid; O34844; -.
DR OMA; GEQRFNE; -.
DR PhylomeDB; O34844; -.
DR BioCyc; BSUB:BSU19540-MON; -.
DR PRO; PR:O34844; -.
DR Proteomes; UP000001570; Chromosome.
DR CollecTF; EXPREG_000006a0; -.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IMP:CollecTF.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:CollecTF.
DR CDD; cd00090; HTH_ARSR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011991; ArsR-like_HTH.
DR InterPro; IPR002577; HTH_HxlR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01638; HxlR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51118; HTH_HXLR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..112
FT /note="HTH-type transcriptional regulator YodB"
FT /id="PRO_0000148887"
FT DOMAIN 6..105
FT /note="HTH hxlR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00435"
FT HELIX 7..17
FT /evidence="ECO:0007829|PDB:5HS7"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:5HS7"
FT HELIX 35..41
FT /evidence="ECO:0007829|PDB:5HS7"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:5HS7"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:5HS7"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5HS7"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:5HS7"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:5HS7"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:5HS7"
SQ SEQUENCE 112 AA; 12846 MW; 0F5B4EF7C8A155F9 CRC64;
MGNTMCPKME SAFSLLGKRW NGLIIHVLMD GPKRFKEITE TIPMISQKML AERLKELEQN
EIVERQVLPE TPVKVIYTLT EKGTALQAVF QEMQAWADQF CEPGDTVCEE EK
