ID   MTLR_BACSU              Reviewed;         694 AA.
AC   P96574; Q797N1;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Transcriptional regulator MtlR;
DE   AltName: Full=Mannitol operon transcriptional activator;
DE            Short=Mtl operon transcriptional activator;
DE   Includes:
DE     RecName: Full=Putative phosphotransferase enzyme IIB component;
DE              EC=2.7.1.197;
DE     AltName: Full=Putative PTS system EIIB component;
DE   Includes:
DE     RecName: Full=Putative phosphotransferase enzyme IIA component;
DE     AltName: Full=Putative PTS system EIIA component;
GN   Name=mtlR; Synonyms=ydaA; OrderedLocusNames=BSU04160;
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   Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT   "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT   subtilis genome.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
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   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=12897001; DOI=10.1128/jb.185.16.4816-4824.2003;
RA   Watanabe S., Hamano M., Kakeshita H., Bunai K., Tojo S., Yamaguchi H.,
RA   Fujita Y., Wong S.-L., Yamane K.;
RT   "Mannitol-1-phosphate dehydrogenase (MtlD) is required for mannitol and
RT   glucitol assimilation in Bacillus subtilis: possible cooperation of mtl and
RT   gut operons.";
RL   J. Bacteriol. 185:4816-4824(2003).
CC   -!- FUNCTION: Positively regulates the expression of the mtlAFD operon
CC       involved in the uptake and catabolism of mannitol.
CC       {ECO:0000269|PubMed:12897001}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannitol(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC         mannitol 1-phosphate(in) + L-histidyl-[protein];
CC         Xref=Rhea:RHEA:33363, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC         ChEBI:CHEBI:16899, ChEBI:CHEBI:29979, ChEBI:CHEBI:61381,
CC         ChEBI:CHEBI:64837; EC=2.7.1.197;
CC   -!- ACTIVITY REGULATION: The regulatory activity of MtlR is modulated by
CC       phosphorylation and dephosphorylation of the various MtlR domains. It
CC       becomes activated via phosphoryl group transfer from PEP, EI and HPr on
CC       the two conserved histidine residues in the PRD 2 domain, whereas
CC       phosphorylation of the EIIA-like domain on His-599 by the PTS EIIB-Mtl
CC       domain of MtlA inactivates MtlR (By similarity). {ECO:0000250}.
CC   -!- INDUCTION: Up-regulated by mannitol or glucitol.
CC       {ECO:0000269|PubMed:12897001}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene cannot grow on either
CC       mannitol or glucitol as sole carbon source.
CC       {ECO:0000269|PubMed:12897001}.
CC   -!- SIMILARITY: Belongs to the transcriptional antiterminator BglG family.
CC       {ECO:0000305}.
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DR   EMBL; AB001488; BAA19254.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12223.1; -; Genomic_DNA.
DR   PIR; A69768; A69768.
DR   RefSeq; NP_388297.1; NC_000964.3.
DR   RefSeq; WP_003246695.1; NZ_JNCM01000031.1.
DR   AlphaFoldDB; P96574; -.
DR   SMR; P96574; -.
DR   STRING; 224308.BSU04160; -.
DR   PaxDb; P96574; -.
DR   PRIDE; P96574; -.
DR   EnsemblBacteria; CAB12223; CAB12223; BSU_04160.
DR   GeneID; 938253; -.
DR   KEGG; bsu:BSU04160; -.
DR   PATRIC; fig|224308.179.peg.442; -.
DR   eggNOG; COG3711; Bacteria.
DR   InParanoid; P96574; -.
DR   OMA; YMTAREQ; -.
DR   PhylomeDB; P96574; -.
DR   BioCyc; BSUB:BSU04160-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 2.
DR   Gene3D; 3.40.930.10; -; 1.
DR   InterPro; IPR013196; HTH_11.
DR   InterPro; IPR007737; Mga_HTH.
DR   InterPro; IPR011608; PRD.
DR   InterPro; IPR036634; PRD_sf.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR   InterPro; IPR036095; PTS_EIIB-like_sf.
DR   InterPro; IPR013011; PTS_EIIB_2.
DR   InterPro; IPR003501; PTS_EIIB_2/3.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF08279; HTH_11; 1.
DR   Pfam; PF05043; Mga; 1.
DR   Pfam; PF00874; PRD; 2.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF46785; SSF46785; 2.
DR   SUPFAM; SSF52794; SSF52794; 1.
DR   SUPFAM; SSF55804; SSF55804; 1.
DR   SUPFAM; SSF63520; SSF63520; 2.
DR   PROSITE; PS51372; PRD_2; 2.
DR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Kinase; Phosphoprotein; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN           1..694
FT                   /note="Transcriptional regulator MtlR"
FT                   /id="PRO_0000376081"
FT   DOMAIN          195..300
FT                   /note="PRD 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT   DOMAIN          305..410
FT                   /note="PRD 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT   DOMAIN          413..502
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT   DOMAIN          536..683
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT   MOD_RES         230
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT   MOD_RES         289
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT   MOD_RES         342
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT   MOD_RES         399
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT   MOD_RES         419
FT                   /note="Phosphocysteine; by EIIA"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         599
FT                   /note="Phosphohistidine; by EIIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
SQ   SEQUENCE   694 AA;  78853 MW;  540D906A19318343 CRC64;
     MYMTAREQKL LKHLLLQNRY ITVTELAELM QVSTRTIHRE LKSIKPLMET VGLTLDKQPG
     KGLKAVGSPE GKQKLLTDLS YEQHEYSADE RKLLILCSLL ESQEPVKLYT LAHDLQVTNA
     TVSYDLDELE KWISPFGLTL IRKRGFGIQL IGPENAKRKI VGNLIVNRLD IQMFLEAVEL
     NIKGKTDSSE KMFGVVSKGE LLKMERILFQ LKEKIAFSLS DSSYIALVVH LTYAIERIKL
     GETITMEQNE LEELMNAKEY SSALEIAGEL ERAFGVTIPE AEVGYITIHL RSANRKYKTE
     YKAQEIELET ALQTKRLIAF ISDKIRMDLT KNYSLYEGLI AHLEPAVSRI KENIEIYNPM
     KEQIKRDYFL LYMAIEEGVE KYFPGMSFSD DEIAFIVLHF GSALEIKKEE AKVKALVVCS
     SGIGSSKMLA SRLKKELPEI ESFDMSSLIE LKGKDVQAYD MIVSTVPIPY ENIDYIMVSP
     LLNEEDANQV KQYIKRKIPL ILNKKRSSKE EAQQADVPDM LEAAESIGRY MEVIQDVLRH
     FTLAQLKTNP DHSMLLLELF QQLKKDGLIR DPEKAAVCLA EREKQGGLGI PGTNMALYHL
     KNDEIVLPFF KMFDLSTPYE VDGMDGNTLR MTRILVMMAP GSLSAEGSEI LSAISSAIIE
     SGESMAGFQE EGGQELYQRL NRIFFTWMKE KNIL