(data stored in ACNUC7421 zone)

SWISSPROT: MHQP_BACSU

ID   MHQP_BACSU              Reviewed;         129 AA.
AC   P96694; Q797F8;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   11-DEC-2019, entry version 86.
DE   RecName: Full=Putative oxidoreductase MhqP;
DE            EC=1.-.-.-;
GN   Name=mhqP; Synonyms=ydfP; OrderedLocusNames=BSU05500;
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=9341680; DOI=10.1007/s004380050546;
RA   Beloin C., Ayora S., Exley R., Hirschbein L., Ogasawara N., Kasahara Y.,
RA   Alonso J.C., Le Hegarat F.;
RT   "Characterization of an lrp-like (lrpC) gene from Bacillus subtilis.";
RL   Mol. Gen. Genet. 256:63-71(1997).
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=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   [4]
RP   INDUCTION, IDENTIFICATION OF THE YDFNOP OPERON, 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 oxidoreductase that may contribute to the
CC       degradation of aromatic compounds. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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 DoxX family. {ECO:0000305}.
DR   EMBL; AB001488; BAA19384.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12357.1; -; Genomic_DNA.
DR   PIR; F69781; F69781.
DR   RefSeq; NP_388431.1; NC_000964.3.
DR   RefSeq; WP_003234169.1; NZ_JNCM01000031.1.
DR   STRING; 224308.BSU05500; -.
DR   PaxDb; P96694; -.
DR   PRIDE; P96694; -.
DR   EnsemblBacteria; CAB12357; CAB12357; BSU05500.
DR   GeneID; 938077; -.
DR   KEGG; bsu:BSU05500; -.
DR   PATRIC; fig|224308.179.peg.590; -.
DR   eggNOG; ENOG4108VGI; Bacteria.
DR   eggNOG; COG2259; LUCA.
DR   HOGENOM; HOG000198397; -.
DR   InParanoid; P96694; -.
DR   KO; K15977; -.
DR   OMA; NNGYEYA; -.
DR   PhylomeDB; P96694; -.
DR   BioCyc; BSUB:BSU05500-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase 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   InterPro; IPR032808; DoxX.
DR   Pfam; PF07681; DoxX; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; P96694.
DR   SWISS-2DPAGE; P96694.
KW   Aromatic hydrocarbons catabolism; Cell membrane; Detoxification; Membrane;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..129
FT                   /note="Putative oxidoreductase MhqP"
FT                   /id="PRO_0000382889"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   129 AA;  13276 MW;  AD6CB50FBD02E9E7 CRC64;
     MEDAGLLLIR IMIGVVFLFY GTQKLFGWFG GYGIKGTGQW FESIGVKPGN VAAALSGLGE
     LVSGILFILG VFLPLGAAII TIIMLGAIVK VHGAKGFANG AGGFEYNLVL IAVSIGVALI
     GSGAYALHF
//

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