| Definition | Clostridium botulinum A2 str. Kyoto chromosome, complete genome. |
|---|---|
| Accession | NC_012563 |
| Length | 4,155,278 |
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The map label for this gene is yjbJ [H]
Identifier: 226950700
GI number: 226950700
Start: 3722285
End: 3723001
Strand: Reverse
Name: yjbJ [H]
Synonym: CLM_3708
Alternate gene names: 226950700
Gene position: 3723001-3722285 (Counterclockwise)
Preceding gene: 226950701
Following gene: 226950699
Centisome position: 89.6
GC content: 33.05
Gene sequence:
>717_bases ATGAACGATAATGTTAAATATATGTTTAATATTGGTGGTGGATTTATGAAAGTGAACAGTAGTGAAATGGTATTACAACA GATGCTACAAATGCAATTGATGGGACAGATAATGAAGTCATCCTTTGGAGATTCATCAAGTTTTCAAATAGTTTTAGATA GTTTGTTAAAGGCCATGGAAAATAAGGATATTAATGCTTCAAATGATATATTATCATTAGACAGTGCAGCAAATAGTGGA AATAAATATTATGGAGCAGGACAAAGATTAGAAGATGCGAGAAGAGAAATAAATAATATAAAATCTGAAGTTAGAACTGG TAATATAACTATAGATAGCGCTGTAGAAAAAGCTTCAAGAAAATATGGTATAGACAAAGAACTTCTAATGGCAGTTATAA AGCAAGAATCGGATTTCAATCCTAATTGCGTATCAAGTGCAGGGGCAAAGGGGTTAATGCAGCTTATGCCAGGTACTGCT AGAGAAGTAGGAGTTACAAATCCCTTCGATATAGAACAAAATATAGATGGGGGAACAAAATATTTAAAGAAAATGCTAGA TATGCATGGAAACGTAAAAGAGTTAGCTTTGGCAGCATATAACGCAGGTCCTGGAACCCTCCAGTGGAGAGGTGTGAAAA GCCCTTCAGATATAAATAGATTGCCAAGTGAAACAAGAAATTATGTAAAAAATATAATGAAAAATTATGGAGTATAA
Upstream 100 bases:
>100_bases GGGGAATATGAAGTATTAGTTTTATCCAAAAGTAGCTTTTTAAAGTGTGCTTATGAAGATTATGATATATTTAAATTTAA AGTGTAAATAAAGTAGAAAG
Downstream 100 bases:
>100_bases AAAGGAAAGTGCCCTGCACTTTCCTTTAAATTTGTTATAATGGTAATACTAATAATAGAATAATCAAAACTAGGAGGAAT TTCATGGAACGTTTAGATAA
Product: transglycosylase, SLT family
Products: 1,6-Anhydrobond [C]
Alternate protein names: NA
Number of amino acids: Translated: 238; Mature: 238
Protein sequence:
>238_residues MNDNVKYMFNIGGGFMKVNSSEMVLQQMLQMQLMGQIMKSSFGDSSSFQIVLDSLLKAMENKDINASNDILSLDSAANSG NKYYGAGQRLEDARREINNIKSEVRTGNITIDSAVEKASRKYGIDKELLMAVIKQESDFNPNCVSSAGAKGLMQLMPGTA REVGVTNPFDIEQNIDGGTKYLKKMLDMHGNVKELALAAYNAGPGTLQWRGVKSPSDINRLPSETRNYVKNIMKNYGV
Sequences:
>Translated_238_residues MNDNVKYMFNIGGGFMKVNSSEMVLQQMLQMQLMGQIMKSSFGDSSSFQIVLDSLLKAMENKDINASNDILSLDSAANSG NKYYGAGQRLEDARREINNIKSEVRTGNITIDSAVEKASRKYGIDKELLMAVIKQESDFNPNCVSSAGAKGLMQLMPGTA REVGVTNPFDIEQNIDGGTKYLKKMLDMHGNVKELALAAYNAGPGTLQWRGVKSPSDINRLPSETRNYVKNIMKNYGV >Mature_238_residues MNDNVKYMFNIGGGFMKVNSSEMVLQQMLQMQLMGQIMKSSFGDSSSFQIVLDSLLKAMENKDINASNDILSLDSAANSG NKYYGAGQRLEDARREINNIKSEVRTGNITIDSAVEKASRKYGIDKELLMAVIKQESDFNPNCVSSAGAKGLMQLMPGTA REVGVTNPFDIEQNIDGGTKYLKKMLDMHGNVKELALAAYNAGPGTLQWRGVKSPSDINRLPSETRNYVKNIMKNYGV
Specific function: Murein-Degrading Enzyme. Catalyzes The Cleavage Of The Glycosidic Bonds Between N-Acetylmuramic Acid And N- Acetylglucosamine Residues In Peptidoglycan. May Play A Role In Recycling Of Muropeptides During Cell Elongation And/Or Cell Division. [C]
COG id: COG0741
COG function: function code M; Soluble lytic murein transglycosylase and related regulatory proteins (some contain LysM/invasin domains)
Gene ontology:
Cell location: Periplasmic Protein. Tightly Associated With The Murein Sacculus [C]
Metaboloic importance: Non_Essential [C]
Operon status: Not Known
Operon components: None
Similarity: Belongs to the transglycosylase slt family [H]
Homologues:
Organism=Escherichia coli, GI87082441, Length=127, Percent_Identity=40.1574803149606, Blast_Score=85, Evalue=5e-18, Organism=Escherichia coli, GI87082191, Length=111, Percent_Identity=36.9369369369369, Blast_Score=67, Evalue=1e-12,
Paralogues:
None
Copy number: NA
Swissprot (AC and ID): NA
Other databases:
- InterPro: IPR008258 - InterPro: IPR000189 [H]
Pfam domain/function: PF01464 SLT [H]
EC number: 3.2.1.- [C]
Molecular weight: Translated: 26212; Mature: 26212
Theoretical pI: Translated: 8.86; Mature: 8.86
Prosite motif: PS00922 TRANSGLYCOSYLASE
Important sites: NA
Signals:
None
Transmembrane regions:
None
Cys/Met content:
0.4 %Cys (Translated Protein) 6.3 %Met (Translated Protein) 6.7 %Cys+Met (Translated Protein) 0.4 %Cys (Mature Protein) 6.3 %Met (Mature Protein) 6.7 %Cys+Met (Mature Protein)
Secondary structure:
>Translated Secondary Structure MNDNVKYMFNIGGGFMKVNSSEMVLQQMLQMQLMGQIMKSSFGDSSSFQIVLDSLLKAME CCCCEEEEEEECCCEEEECCHHHHHHHHHHHHHHHHHHHHHCCCCCHHHHHHHHHHHHHH NKDINASNDILSLDSAANSGNKYYGAGQRLEDARREINNIKSEVRTGNITIDSAVEKASR CCCCCCCCCEEECCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHHHCCCEEHHHHHHHHHH KYGIDKELLMAVIKQESDFNPNCVSSAGAKGLMQLMPGTAREVGVTNPFDIEQNIDGGTK HCCCCHHHHHHHHHHCCCCCCCHHHHHHHHHHHHHCCCCCHHCCCCCCCCCCCCCCHHHH YLKKMLDMHGNVKELALAAYNAGPGTLQWRGVKSPSDINRLPSETRNYVKNIMKNYGV HHHHHHHHCCCHHHHHHHHCCCCCCCEEECCCCCCHHHHHCHHHHHHHHHHHHHHCCC >Mature Secondary Structure MNDNVKYMFNIGGGFMKVNSSEMVLQQMLQMQLMGQIMKSSFGDSSSFQIVLDSLLKAME CCCCEEEEEEECCCEEEECCHHHHHHHHHHHHHHHHHHHHHCCCCCHHHHHHHHHHHHHH NKDINASNDILSLDSAANSGNKYYGAGQRLEDARREINNIKSEVRTGNITIDSAVEKASR CCCCCCCCCEEECCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHHHCCCEEHHHHHHHHHH KYGIDKELLMAVIKQESDFNPNCVSSAGAKGLMQLMPGTAREVGVTNPFDIEQNIDGGTK HCCCCHHHHHHHHHHCCCCCCCHHHHHHHHHHHHHCCCCCHHCCCCCCCCCCCCCCHHHH YLKKMLDMHGNVKELALAAYNAGPGTLQWRGVKSPSDINRLPSETRNYVKNIMKNYGV HHHHHHHHCCCHHHHHHHHCCCCCCCEEECCCCCCHHHHHCHHHHHHHHHHHHHHCCC
PDB accession: NA
Resolution: NA
Structure class: Unstructured
Cofactors: NA
Metal ions: NA
Kcat value (1/min): NA
Specific activity: NA
Km value (mM): NA
Substrates: Muramic Acid Residue (N-Acetylmuramic Acid And N-Acetylglucosamine Residues) [C]
Specific reaction: Cleavage Of The Beta-1,4-Glycosidic Bond Between N-Acetylmuramic Acid And N-Acetylglucosamine Residues, Thereby Conserving The Energy In A Newly Synthesized 1,6-Anhydrobond In The Muramic Acid Residue. [C]
General reaction: Cleavage Of The Beta-1,4-Glycosidic Bond [C]
Inhibitor: NA
Structure determination priority: 10.0
TargetDB status: NA
Availability: NA
References: 9384377 [H]