| IED ID | IndEnz0002011035 |
| Enzyme Type ID | protease011035 |
| Protein Name |
tRNA nuclease WapA EC 3.1.-.- Cell wall-associated polypeptide CWBP200 CWBP200 RNase WapA Toxin WapA Wall-associated protein |
| Gene Name | wapA BSU39230 N17G |
| 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 | MKKRKRRNFKRFIAAFLVLALMISLVPADVLAKSTEEENGNRIAADDPEETLQKEQTEEAVPFDPKDINKEGEITSERTENTKLYYEGDGVYKQEVYLDPIHTKETPDADWEDISPELKESTSKQVETENAILNSDFQKQMKNGLYATFEHNDHKVTYSLAEAKGPNKTSLTPKDTSADYKTDSNEIVYPDVFPNIDLQTFTFNENIKEDLVLHQYNGYNTFTFQLKTDLQAKEQEDGSIDFSDEKGKVVFSVPKPFMTDSKLDELSGEVERSDKVSYKLEKNEEGYLLHLTADENWLKDPERVYPVSIDPSTSLSVSSDTFVMSAYPTTNYSASSQKWDANLKAYVLKTGYYDKTTGTNYAFMKFNNLKPIQNMTVTKATLKTYVAHSYYGTKATGLWLDTVNSNYDNAKVTWNTKPASKNIGKADVHKGQWASYDVTAAVKSWNSGGANYGFKLHTNGNGKEYWKKLISSANSANKPYIEVTYTIPKGNTPTIKAYHNGDSTGYFDISWKKVEGAKGYKVWIYNGKEYQAISAGNVTSWSTKGKKIWPTSAEIASKRYKLHLDGKDGAELALDPSPVYKNSGGSYATSKNYWIGVSAIFDQGEGAMSAPAKPVIPNVGKAQAPSAKGYNNGNATGYFDLSWKAVSGATGYKVQVFNGKGFETLDLGNQTSWTTKGKKIWPTSAEIKAGKYALHLKDGSGAELPINPGPTYKNAGGDGAKRNYSFKIIAYNKDGEAIASPAATPALPDIARPKNVTGYLYTNTKSSQTGYVNLIWEKVQNAKGYKVNIYNGKEYQSFDVGDADHWTTQNKNIWPTSEEIKAGSYKLHTDGKGGELALDPSPVYNNANGNYKGKKNYSFTLVAYDANGETIPTAPFNPTFHEGAEFLGTEEYWSIIDIPSGQLNGATGNVIVNEEDLSIDGRGPGLGLSRTYNSLDSSDHLFGQGWYADAETSVISTDGGAMYIDEDATTHRFTKKADGTYQPPTGVYLELTETADQFILKTKDQTNAYFNKKGGKLQKVVDGHNNATVYTYNDKNQLTAITDASGRKLTFTYDENGHVTSITGPKNKKVTYSYENDLLKKVTDTDGTVTSYDYDSEGRLVKQYSANSTEAKPVFTEYQYSGHRLEKAINAKKETYVYSYDADKKTLLMTQPNGRKVQYGYNEAGNPIQVIDDAEGLKITTNTKYEGNNVVEDVDPNDVGTGKATESYQYDKDGNVTSVKDAYGTETYEYNKNNDVTKMKDTEGNVTDIAYDGLDAVSETDQSGKSSSAAVYDKYGNQIQSSKDLSASTNILKDGSFEAQKSGWNLTASKDSGKISVIADKSGVLSGSKALEVLSQSTSAGTDHGYSSATQTVELEPNTTYTLSGKIKTDLAKSRAYFNIDLRDKDQKRIQWIHNEYSALAGKNDWTKRQITFTTPANAGKAVVYMEVDHKDKDGKGKAWFDEVQLEKGEVSSSYNPVQNSSFTSATENWNVSGASVDSEEGFNDDVSLKAARTSASQAGSVTKQTVVLGQSANDKPVYLTLTGMSKASSVKFTDEKDYSLQANVTYADGSTGIYNAKFPSGTQEWNRAAVVIPKTKPINKVDISILFQKSATGTVWFDDIRLIEGSLLTKSTYDSNGNYVTKEEDELGYATSTDYDETGKKTSETDAKGEKTTYTYDQADQLTNMTLSNGTSILHSYDKEGNEVSKTIRAGADQTYKFEYDVMGKLVKTTDPLGNVLASEYDANSNLTKTISPNGNEVSLSYDGTDRVKSKSYNGTEKYIFTYDKNGNETSVVNKEQNTTKKRTFDNKNRLTELTDRGGSQTWTYPSDSDKLKTFSWIHGDQKGTNQFTYNKLDQMIEMKDSTSSYSFDYDENGNVQTFITGNGGGTSFSYDERNLVSSLHIGDKNGGDILTESYEYDANGNRTTINSSASGKVQYEYGKLNQLVKETHEDGTVIEYTYDGFGNRKTVTTIKDGSSKTVNASFNIMNQLTKVNDESISYDKNGNRTSDGKFTYTWDAEDNLTAVTKKGEDKPFATYKYDEKGNRIQKTVNGKVTNYFYDGDSLNVLYETDADNNVTKSYTYGDSGQLLSYTENGKKYFYHYNAHGDIIAISDSTGKTVAKYQYDAWGNPTKTEASDEVKDNRYRYAGYQYDEETGLYYLMARYYEPRNGVFLSLDPDPGSDGDSLDQNGYAYGNNNPVMNVDPDGHWVWLVVNAGFAAYDGYKAYKSGKGWKGAAWAAASNFGPGKIFKGASRAYKFTKKAVKITGHTRHGLNQSIGRNGGRGVNLRAKLNAVRSPKKVIKQPNGATKYVGKKATVVLNKRGKVITAYGSSRAKGSKHVFHTHGKGNKSKRRR |
| Enzyme Length | 2334 |
| Uniprot Accession Number | Q07833 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Detected in exponentially growing cells as many processing products, protein disappears upon entry into stationary phase with the concomitant appearance of smaller products. The large products persist in the absence of the extracellular serine protease Epr (PubMed:11987133). {ECO:0000269|PubMed:11987133}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.1.-.- |
| Enzyme Function | FUNCTION: Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. A site-specific general tRNA nuclease, the C-terminus (residues 2201-2334) removes 2 or 4 nucleotides from the 3' end of at least 4 tRNAs (upon expression in E.coli), possibly endonucleolytically. The nuclease activity is neutralized by expression of the cognate immunity protein WapI from the same strain, but not its homolog from 2 other B.subtilis strains. The C-terminus cannot be expressed on its own in E.coli, however it can be cloned in the presence of its cognate immunity protein gene. Cell contact is necessary for growth inhibition. {ECO:0000269|PubMed:23572593}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Region (4); Repeat (39); Sequence conflict (3); Signal peptide (1) |
| Keywords | Cell wall;Direct protein sequencing;Endonuclease;Hydrolase;Nuclease;Reference proteome;Repeat;Secreted;Signal;Toxin;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:10658653, ECO:0000269|PubMed:11987133}. Note=Released into the medium. |
| Modified Residue | |
| Post Translational Modification | PTM: Identified in the extracellular proteome as many processing products ranging from over 85 kDa to about 30 kDa. One of these probably starts on Ser-1726. Two forms are known as CWBP62 and CWBP105 (PubMed:11987133). {ECO:0000269|PubMed:11987133}. |
| Signal Peptide | SIGNAL 1..28; /note=Or 32; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 25374563; |
| Motif | |
| Gene Encoded By | |
| Mass | 258,162 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |