YCNE_BACSU
ID YCNE_BACSU Reviewed; 95 AA.
AC P94425;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Putative monooxygenase YcnE;
DE EC=1.-.-.-;
GN Name=ycnE; OrderedLocusNames=BSU03870;
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=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
RN [4]
RP POTENTIAL FUNCTION, AND 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).
CC -!- FUNCTION: Putative monooxygenase that may contribute to the degradation
CC of aromatic compounds. {ECO:0000305}.
CC -!- INDUCTION: Strongly induced by stress due to exposure to 6-brom-2-
CC vinyl-chroman-4-on (chromanon) and less strongly induced after exposure
CC to 2-methylhydroquinone (2-MHQ) or catechol stress.
CC {ECO:0000269|PubMed:17407181}.
CC -!- SIMILARITY: Belongs to the LsrG family. {ECO:0000305}.
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DR EMBL; D50453; BAA09019.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12195.1; -; Genomic_DNA.
DR PIR; A69764; A69764.
DR RefSeq; NP_388269.1; NC_000964.3.
DR RefSeq; WP_003234477.1; NZ_JNCM01000031.1.
DR AlphaFoldDB; P94425; -.
DR SMR; P94425; -.
DR STRING; 224308.BSU03870; -.
DR iPTMnet; P94425; -.
DR jPOST; P94425; -.
DR PaxDb; P94425; -.
DR PRIDE; P94425; -.
DR EnsemblBacteria; CAB12195; CAB12195; BSU_03870.
DR GeneID; 938274; -.
DR KEGG; bsu:BSU03870; -.
DR PATRIC; fig|224308.179.peg.410; -.
DR eggNOG; COG1359; Bacteria.
DR InParanoid; P94425; -.
DR OMA; FVMLEQW; -.
DR PhylomeDB; P94425; -.
DR BioCyc; BSUB:BSU03870-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IBA:GO_Central.
DR GO; GO:0004497; F:monooxygenase 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; IPR007138; ABM_dom.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR Pfam; PF03992; ABM; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
DR PROSITE; PS51725; ABM; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Detoxification; Monooxygenase;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..95
FT /note="Putative monooxygenase YcnE"
FT /id="PRO_0000049479"
FT DOMAIN 2..93
FT /note="ABM"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17218307"
SQ SEQUENCE 95 AA; 10944 MW; B7752D15BAA51150 CRC64;
MIVLQAYIKV KPEKREEFLS EAQSLVQHSR AEEGNAQYDL FEKVGEENTF VMLEKWKDEA
AMKFHNETAH FQGFVAKGKE LLSAPLDVVR TELSE
