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Probable licABCH operon regulator [Includes: Putative phosphotransferase enzyme IIB component (EC 2.7.1.-) (Putative PTS system EIIB component); Putative phosphotransferase enzyme IIA component (Putative PTS system EIIA component)]

 LICR_BACSU              Reviewed;         641 AA.
P46321;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
25-APR-2018, entry version 130.
RecName: Full=Probable licABCH operon regulator;
Includes:
RecName: Full=Putative phosphotransferase enzyme IIB component;
EC=2.7.1.-;
AltName: Full=Putative PTS system EIIB component;
Includes:
RecName: Full=Putative phosphotransferase enzyme IIA component;
AltName: Full=Putative PTS system EIIA component;
Name=licR; Synonyms=celR; OrderedLocusNames=BSU38600;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=8990303; DOI=10.1128/jb.179.2.496-506.1997;
Tobisch S., Glaser P., Krueger S., Hecker M.;
"Identification and characterization of a new beta-glucoside
utilization system in Bacillus subtilis.";
J. Bacteriol. 179:496-506(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / BGSC1A1;
PubMed=8969509; DOI=10.1099/13500872-142-11-3113;
Yoshida K., Shindo K., Sano H., Seki S., Fujimura M., Yanai N.,
Miwa Y., Fujita Y.;
"Sequencing of a 65 kb region of the Bacillus subtilis genome
containing the lic and cel loci, and creation of a 177 kb contig
covering the gnt-sacXY region.";
Microbiology 142:3113-3123(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[4]
MUTAGENESIS OF HIS-219; HIS-278; HIS-333; HIS-392 AND HIS-559.
PubMed=10438772;
Tobisch S., Stuelke J., Hecker M.;
"Regulation of the lic operon of Bacillus subtilis and
characterization of potential phosphorylation sites of the LicR
regulator protein by site-directed mutagenesis.";
J. Bacteriol. 181:4995-5003(1999).
-!- FUNCTION: Positive regulator of the licABCH operon.
-!- ENZYME REGULATION: The regulatory activity of LicR is modulated by
phosphorylation and dephosphorylation of the various LicR domains.
It becomes activated via phosphoryl group transfer from PEP, EI
and HPr on the two conserved histidine residues in the PRD 2
domain, whereas phosphorylation of the EIIA-like domain on His-559
by the PTS EIIB component LicB inactivates LicR (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the transcriptional antiterminator BglG
family. {ECO:0000305}.
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EMBL; Z49992; CAA90284.1; -; Genomic_DNA.
EMBL; D83026; BAA11742.1; -; Genomic_DNA.
EMBL; AL009126; CAB15886.1; -; Genomic_DNA.
PIR; H69651; H69651.
RefSeq; NP_391739.1; NC_000964.3.
RefSeq; WP_003243034.1; NZ_JNCM01000034.1.
ProteinModelPortal; P46321; -.
SMR; P46321; -.
STRING; 224308.Bsubs1_010100020836; -.
PaxDb; P46321; -.
PRIDE; P46321; -.
DNASU; 937383; -.
EnsemblBacteria; CAB15886; CAB15886; BSU38600.
GeneID; 937383; -.
KEGG; bsu:BSU38600; -.
PATRIC; fig|224308.179.peg.4179; -.
eggNOG; ENOG4105EMD; Bacteria.
eggNOG; COG1762; LUCA.
eggNOG; COG3711; LUCA.
HOGENOM; HOG000083911; -.
InParanoid; P46321; -.
KO; K03491; -.
OMA; ETAYITM; -.
PhylomeDB; P46321; -.
BioCyc; BSUB:BSU38600-MONOMER; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.10.10; -; 2.
Gene3D; 3.40.930.10; -; 1.
InterPro; IPR013196; HTH_11.
InterPro; IPR007737; Mga_HTH.
InterPro; IPR011608; PRD.
InterPro; IPR036634; PRD_sf.
InterPro; IPR016152; PTrfase/Anion_transptr.
InterPro; IPR002178; PTS_EIIA_type-2_dom.
InterPro; IPR036095; PTS_EIIB-like_sf.
InterPro; IPR013011; PTS_EIIB_2.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF08279; HTH_11; 1.
Pfam; PF05043; Mga; 1.
Pfam; PF00874; PRD; 2.
Pfam; PF00359; PTS_EIIA_2; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF52794; SSF52794; 1.
SUPFAM; SSF55804; SSF55804; 1.
SUPFAM; SSF63520; SSF63520; 2.
PROSITE; PS51372; PRD_2; 2.
PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
1: Evidence at protein level;
Activator; Complete proteome; Kinase; Phosphoprotein;
Reference proteome; Repeat; RNA-binding; Transcription;
Transcription regulation; Transferase.
CHAIN 1 641 Probable licABCH operon regulator.
/FTId=PRO_0000204245.
DOMAIN 184 289 PRD 1. {ECO:0000255|PROSITE-
ProRule:PRU00704}.
DOMAIN 296 403 PRD 2. {ECO:0000255|PROSITE-
ProRule:PRU00704}.
DOMAIN 407 498 PTS EIIB type-2. {ECO:0000255|PROSITE-
ProRule:PRU00422}.
DOMAIN 499 638 PTS EIIA type-2. {ECO:0000255|PROSITE-
ProRule:PRU00417}.
MOD_RES 219 219 Phosphohistidine; by HPr.
{ECO:0000255|PROSITE-ProRule:PRU00704}.
MOD_RES 278 278 Phosphohistidine; by HPr.
{ECO:0000255|PROSITE-ProRule:PRU00704}.
MOD_RES 333 333 Phosphohistidine; by HPr.
{ECO:0000255|PROSITE-ProRule:PRU00704}.
MOD_RES 392 392 Phosphohistidine; by HPr.
{ECO:0000255|PROSITE-ProRule:PRU00704}.
MOD_RES 413 413 Phosphocysteine; by EIIA. {ECO:0000255}.
MOD_RES 559 559 Phosphohistidine; by EIIB.
{ECO:0000255|PROSITE-ProRule:PRU00704}.
MUTAGEN 219 219 H->A: Residual activity.
{ECO:0000269|PubMed:10438772}.
MUTAGEN 219 219 H->D: Loss of activity.
{ECO:0000269|PubMed:10438772}.
MUTAGEN 278 278 H->A: Loss of activity.
{ECO:0000269|PubMed:10438772}.
MUTAGEN 278 278 H->E: Loss of activity.
{ECO:0000269|PubMed:10438772}.
MUTAGEN 333 333 H->A: Loss of activity.
{ECO:0000269|PubMed:10438772}.
MUTAGEN 392 392 H->E: Loss of activity.
{ECO:0000269|PubMed:10438772}.
MUTAGEN 392 392 H->I: Residual activity.
{ECO:0000269|PubMed:10438772}.
MUTAGEN 559 559 H->G: Increase in activity.
{ECO:0000269|PubMed:10438772}.
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


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