LICR_BACSU
ID LICR_BACSU Reviewed; 641 AA.
AC P46321;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable licABCH operon regulator;
DE Includes:
DE RecName: Full=Putative phosphotransferase enzyme IIB component;
DE EC=2.7.1.-;
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=licR; Synonyms=celR; OrderedLocusNames=BSU38600;
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=8990303; DOI=10.1128/jb.179.2.496-506.1997;
RA Tobisch S., Glaser P., Krueger S., Hecker M.;
RT "Identification and characterization of a new beta-glucoside utilization
RT system in Bacillus subtilis.";
RL J. Bacteriol. 179:496-506(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=8969509; DOI=10.1099/13500872-142-11-3113;
RA Yoshida K., Shindo K., Sano H., Seki S., Fujimura M., Yanai N., Miwa Y.,
RA Fujita Y.;
RT "Sequencing of a 65 kb region of the Bacillus subtilis genome containing
RT the lic and cel loci, and creation of a 177 kb contig covering the gnt-
RT sacXY region.";
RL Microbiology 142:3113-3123(1996).
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 MUTAGENESIS OF HIS-219; HIS-278; HIS-333; HIS-392 AND HIS-559.
RX PubMed=10438772; DOI=10.1128/jb.181.16.4995-5003.1999;
RA Tobisch S., Stuelke J., Hecker M.;
RT "Regulation of the lic operon of Bacillus subtilis and characterization of
RT potential phosphorylation sites of the LicR regulator protein by site-
RT directed mutagenesis.";
RL J. Bacteriol. 181:4995-5003(1999).
CC -!- FUNCTION: Positive regulator of the licABCH operon.
CC -!- ACTIVITY REGULATION: The regulatory activity of LicR is modulated by
CC phosphorylation and dephosphorylation of the various LicR 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-559 by the PTS EIIB
CC component LicB inactivates LicR (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transcriptional antiterminator BglG family.
CC {ECO:0000305}.
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DR EMBL; Z49992; CAA90284.1; -; Genomic_DNA.
DR EMBL; D83026; BAA11742.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15886.1; -; Genomic_DNA.
DR PIR; H69651; H69651.
DR RefSeq; NP_391739.1; NC_000964.3.
DR RefSeq; WP_003243034.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P46321; -.
DR SMR; P46321; -.
DR STRING; 224308.BSU38600; -.
DR PaxDb; P46321; -.
DR PRIDE; P46321; -.
DR DNASU; 937383; -.
DR EnsemblBacteria; CAB15886; CAB15886; BSU_38600.
DR GeneID; 937383; -.
DR KEGG; bsu:BSU38600; -.
DR PATRIC; fig|224308.179.peg.4179; -.
DR eggNOG; COG1762; Bacteria.
DR eggNOG; COG3711; Bacteria.
DR InParanoid; P46321; -.
DR OMA; VSSWGKY; -.
DR PhylomeDB; P46321; -.
DR BioCyc; BSUB:BSU38600-MON; -.
DR Proteomes; UP000001570; Chromosome.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
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 CDD; cd00211; PTS_IIA_fru; 1.
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; 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 SUPFAM; SSF46785; SSF46785; 1.
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 1: Evidence at protein level;
KW Activator; Kinase; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..641
FT /note="Probable licABCH operon regulator"
FT /id="PRO_0000204245"
FT DOMAIN 184..289
FT /note="PRD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT DOMAIN 296..403
FT /note="PRD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT DOMAIN 407..498
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT DOMAIN 499..638
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT MOD_RES 219
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT MOD_RES 278
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT MOD_RES 333
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT MOD_RES 392
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT MOD_RES 413
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255"
FT MOD_RES 559
FT /note="Phosphohistidine; by EIIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT MUTAGEN 219
FT /note="H->A: Residual activity."
FT /evidence="ECO:0000269|PubMed:10438772"
FT MUTAGEN 219
FT /note="H->D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10438772"
FT MUTAGEN 278
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10438772"
FT MUTAGEN 278
FT /note="H->E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10438772"
FT MUTAGEN 333
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10438772"
FT MUTAGEN 392
FT /note="H->E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10438772"
FT MUTAGEN 392
FT /note="H->I: Residual activity."
FT /evidence="ECO:0000269|PubMed:10438772"
FT MUTAGEN 559
FT /note="H->G: Increase in activity."
FT /evidence="ECO:0000269|PubMed:10438772"
SQ SEQUENCE 641 AA; 73315 MW; FCEF83BFC72A0168 CRC64;
MLHGRLRDIL RLLMAAEAPV TSSFFAAQLN VTTRTVRNDI KELQGVLSGH GAFVQSVRGS
GYKLRIDDEQ VFRTLLQDEF QQKKGLPVLP EERMAYLMKR LLLADHYLKL DELAEELFIS
KSTLQTDLKE VKKRLLPYRI VMETRPNYGF KLRGDEVQMR YCMAEYIVDE RETEIDVLNE
KADILPKEEI EIIRSAILKK MKNDRIPLSN MGLNNLIIHI AIACKRIRTE NYVSLFPKDM
DHILHQKEYQ AAEAIVKELE SKLSVTFPKD ETAYITMHLL GTKRMTQSQC GEDTFSIEEE
TDQLTLAMIK AVDRELKLGI LHDKELKIGL ALHMKPAISR NRYGMNLRNP MLAAIKEHYP
LAFEAGIIAG IVIKEQTGIE IHENEIGYLA LHFGAAIERK KTESPPKRCI IVCASGAGSA
QLLREKLRSH FGKRLDILGT AEYYSLDQMS YESIDFVIST IPIKKELPVP VLKVNTILGG
TDFTKIESIL SDEKEKANRY LKKELVFFQE DLRSKEEVIQ FLGQKVVECG FADEEIIDSI
FEREDMSPTC FGNLVAIPHP LVPQTKTTFW AVCTLKKPID WESQRVQFVC LLCVEKENKA
DLQSMYKLLG SILDDPAAMN QLIKCRSYQE LSDVFDQKML S
