ID   MHQD_BACSU              Reviewed;         200 AA.
AC   O34842; Q796B9;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Putative hydrolase MhqD;
DE            EC=3.1.-.-;
GN   Name=mhqD; Synonyms=yodD, yolF; OrderedLocusNames=BSU19560;
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   Ghim S.-Y., Jeong Y.-M., Choi S.-K., Park S.-H.;
RT   "Sequence analysis of the 30 kb region (182') of the Bacillus subtilis
RT   chromosome containing the cge cluster.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
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   [4]
RP   INDUCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=168;
RX   PubMed=17725564; DOI=10.1111/j.1365-2958.2007.05891.x;
RA   Toewe S., Leelakriangsak M., Kobayashi K., Van Duy N., Hecker M., Zuber P.,
RA   Antelmann H.;
RT   "The MarR-type repressor MhqR (YkvE) regulates multiple
RT   dioxygenases/glyoxalases and an azoreductase which confer resistance to 2-
RT   methylhydroquinone and catechol in Bacillus subtilis.";
RL   Mol. Microbiol. 66:40-54(2007).
RN   [5]
RP   INDUCTION, SUBCELLULAR LOCATION, AND NOMENCLATURE.
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).
CC   -!- FUNCTION: Putative hydrolase that may contribute to the degradation of
CC       aromatic compounds. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17407181,
CC       ECO:0000269|PubMed:17725564}.
CC   -!- INDUCTION: Repressed by MhqR. Strongly induced by stress due to
CC       exposure to 2-methylhydroquinone (2-MHQ) and less strongly induced
CC       after diamide or catechol stress. Not induced by oxidative stress due
CC       to hydrogen peroxide or methylglyoxal. {ECO:0000269|PubMed:17407181,
CC       ECO:0000269|PubMed:17725564}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC       family. {ECO:0000305}.
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DR   EMBL; AF015775; AAB72061.1; -; Genomic_DNA.
DR   EMBL; AF006665; AAB81172.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13847.1; -; Genomic_DNA.
DR   PIR; A69903; A69903.
DR   RefSeq; NP_389837.1; NC_000964.3.
DR   RefSeq; WP_003231194.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34842; -.
DR   SMR; O34842; -.
DR   STRING; 224308.BSU19560; -.
DR   ESTHER; bacsu-MHQD; LYsophospholipase_carboxylesterase.
DR   PaxDb; O34842; -.
DR   PRIDE; O34842; -.
DR   EnsemblBacteria; CAB13847; CAB13847; BSU_19560.
DR   GeneID; 940106; -.
DR   KEGG; bsu:BSU19560; -.
DR   PATRIC; fig|224308.179.peg.2138; -.
DR   eggNOG; COG0400; Bacteria.
DR   InParanoid; O34842; -.
DR   OMA; FHYKDVL; -.
DR   PhylomeDB; O34842; -.
DR   BioCyc; BSUB:BSU19560-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002925; Dienelactn_hydro.
DR   Pfam; PF01738; DLH; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Aromatic hydrocarbons catabolism; Cytoplasm; Detoxification; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..200
FT                   /note="Putative hydrolase MhqD"
FT                   /id="PRO_0000381993"
FT   ACT_SITE        100
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        150
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        181
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   200 AA;  22432 MW;  B4DBB73CD5A3E342 CRC64;
     MKHIYEKGTS DNVLLLLHGT GGNEHDLLSL GRFIDPDAHL LGVRGSVLEN GMPRFFKRLS
     EGVFDEKDLV VRTRELKDFI DEAAETHQFN RGRVIAVGYS NGANIAASLL FHYKDVLKGA
     ILHHPMVPIR GIELPDMAGL PVFIGAGKYD PLCTKEESEE LYRYLRDSGA SASVYWQDGG
     HQLTQHEAEQ AREWYKEAIV