Detail Information for IndEnz0011000125
IED ID IndEnz0011000125
Enzyme Type ID glucanase000125
Protein Name Transcription antiterminator LicT
Gene Name licT BSU39080 N15A
Organism Bacillus subtilis (strain 168)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168)
Enzyme Sequence MKIAKVINNNVISVVNEQGKELVVMGRGLAFQKKSGDDVDEARIEKVFTLDNKDVSEKFKTLLYDIPIECMEVSEEIISYAKLQLGKKLNDSIYVSLTDHINFAIQRNQKGLDIKNALLWETKRLYKDEFAIGKEALVMVKNKTGVSLPEDEAGFIALHIVNAELNEEMPNIINITKVMQEILSIVKYHFKIEFNEESLHYYRFVTHLKFFAQRLFNGTHMESQDDFLLDTVKEKYHRAYECTKKIQTYIEREYEHKLTSDELLYLTIHIERVVKQA
Enzyme Length 277
Uniprot Accession Number P39805
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Mediates positive regulation of the glucanase operon (licST) by functioning as an antiterminator factor of transcription. Prevents termination at terminator lic-t.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (5); Chain (1); Domain (2); Helix (13); Sequence conflict (1)
Keywords 3D-structure;Activator;Phosphoprotein;RNA-binding;Reference proteome;Repeat;Transcription;Transcription regulation
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: Phosphorylated. {ECO:0000250}.
Signal Peptide
Structure 3D X-ray crystallography (2); NMR spectroscopy (2)
Cross Reference PDB 1H99; 1L1C; 1TLV; 6TWR;
Mapped Pubmed ID 11447120; 11953318; 15699035; 33781896;
Motif
Gene Encoded By
Mass 32,317
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda