Definition | Clostridium botulinum A str. ATCC 3502, complete genome. |
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Accession | NC_009495 |
Length | 3,886,916 |
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The map label for this gene is sleB [H]
Identifier: 148379303
GI number: 148379303
Start: 1444855
End: 1445634
Strand: Reverse
Name: sleB [H]
Synonym: CBO1324
Alternate gene names: 148379303
Gene position: 1445634-1444855 (Counterclockwise)
Preceding gene: 148379306
Following gene: 148379302
Centisome position: 37.19
GC content: 32.69
Gene sequence:
>780_bases ATGACAAAGCACAAATCATTAAAAACACTCTTAGCTACACTAACTTTTTGTGTAGGTTTATCTAGTCCAGTCTTTGCTGC AGATTACAGGGTAAGTTCTGGTGATTCTCTTTACAAGATAGGTCAATTATTCAATGTATCTTCAGACACTATTATAAAAA ACAATAATCTTAAGGAAAGCACAATTCATCCTGGACAAGTTCTAAACATTCCTTGCAATACTTATACTGTAAAAAGTGGA GATAGTCTATTTTTAATTTCTAAAGCGCAGGGCATAAGTTTATACAATTTAAGAAAAGCAAATAATAAATTGGATGACAC AATTTATCCTGGACAAGTTTTGAATTTACCTGGAAAAACTTCTAGTAATACTAGTCCAGCACCAGCTCCAACTACACCAA AGCCTATAGTGAATTATACAGAATCAGATTTAGACCTTTTAGCTAGACTTATAACAGCTGAAGCTCAAAGTGAACCCTAT AGCGCTCAAGTAGCTGTGGCGTCTGTAGTTATAAACAGAATAAAAAGTTCTCAATTTCCAAACAGTATTTCATCTGTAAT TTATCAAAAAAGTGATGGATACTATCAATTTACACCTGTATTAAATGGTTGGATAAATAAACCTGCTACAGAAACATCAA AAAAAGCTGCTAAAGAAGCTTTATATGGATCTGACCCAAGCAAAGGTGCACTATATTATTTTGATAATACTGCCACTAAT AAATGGTTATGGTCCAAGCCTATAACAGCTAGAATTGGTAACATGGTTTATGTTAAATAA
Upstream 100 bases:
>100_bases AAGTACCGGGGATACTCTTGGGGTGAATCTCTTAGGAATAGGGTACCTCTAACCCGAACCCGTCAACTAACCTGGGAGGC AATATGGAGGGATTTAACTA
Downstream 100 bases:
>100_bases TAATATTATTATTTAAGGGCCACTATCAAGATTTAAAATATTGTTATAAATAACAAACCAACAATAAATAAAAATTTTTA ATAAACAACATACTTAAAAT
Product: putative cell wall hydrolase
Products: 1,6-Anhydrobond In The Muramic Acid Residue [C]
Alternate protein names: SCLE; Germination-specific amidase [H]
Number of amino acids: Translated: 259; Mature: 258
Protein sequence:
>259_residues MTKHKSLKTLLATLTFCVGLSSPVFAADYRVSSGDSLYKIGQLFNVSSDTIIKNNNLKESTIHPGQVLNIPCNTYTVKSG DSLFLISKAQGISLYNLRKANNKLDDTIYPGQVLNLPGKTSSNTSPAPAPTTPKPIVNYTESDLDLLARLITAEAQSEPY SAQVAVASVVINRIKSSQFPNSISSVIYQKSDGYYQFTPVLNGWINKPATETSKKAAKEALYGSDPSKGALYYFDNTATN KWLWSKPITARIGNMVYVK
Sequences:
>Translated_259_residues MTKHKSLKTLLATLTFCVGLSSPVFAADYRVSSGDSLYKIGQLFNVSSDTIIKNNNLKESTIHPGQVLNIPCNTYTVKSG DSLFLISKAQGISLYNLRKANNKLDDTIYPGQVLNLPGKTSSNTSPAPAPTTPKPIVNYTESDLDLLARLITAEAQSEPY SAQVAVASVVINRIKSSQFPNSISSVIYQKSDGYYQFTPVLNGWINKPATETSKKAAKEALYGSDPSKGALYYFDNTATN KWLWSKPITARIGNMVYVK >Mature_258_residues TKHKSLKTLLATLTFCVGLSSPVFAADYRVSSGDSLYKIGQLFNVSSDTIIKNNNLKESTIHPGQVLNIPCNTYTVKSGD SLFLISKAQGISLYNLRKANNKLDDTIYPGQVLNLPGKTSSNTSPAPAPTTPKPIVNYTESDLDLLARLITAEAQSEPYS AQVAVASVVINRIKSSQFPNSISSVIYQKSDGYYQFTPVLNGWINKPATETSKKAAKEALYGSDPSKGALYYFDNTATNK WLWSKPITARIGNMVYVK
Specific function: Probable N-acetylmuramyl-L-alanine amidase. Required for spore cortex hydrolysis during germination. May form a complex with some hydrophobic spore component, leading to a stabilization of the enzyme in a spore-bound form [H]
COG id: COG3773
COG function: function code M; Cell wall hydrolyses involved in spore germination
Gene ontology:
Cell location: Forespore. Note=Expressed in the forespore and then transported across the inner forespore membrane and deposited on the outside of the cortex [H]
Metaboloic importance: Unknown [C]
Operon status: Not Known
Operon components: None
Similarity: Belongs to the sleB family [H]
Homologues:
None
Paralogues:
None
Copy number: 10-20 Molecules/Cell [C]
Swissprot (AC and ID): NA
Other databases:
- InterPro: IPR011105 - InterPro: IPR002477 - InterPro: IPR014224 [H]
Pfam domain/function: PF07486 Hydrolase_2; PF01471 PG_binding_1 [H]
EC number: 3.2.1.- [C]
Molecular weight: Translated: 28275; Mature: 28144
Theoretical pI: Translated: 9.84; Mature: 9.84
Prosite motif: NA
Important sites: NA
Signals:
None
Transmembrane regions:
None
Cys/Met content:
0.8 %Cys (Translated Protein) 0.8 %Met (Translated Protein) 1.5 %Cys+Met (Translated Protein) 0.8 %Cys (Mature Protein) 0.4 %Met (Mature Protein) 1.2 %Cys+Met (Mature Protein)
Secondary structure:
>Translated Secondary Structure MTKHKSLKTLLATLTFCVGLSSPVFAADYRVSSGDSLYKIGQLFNVSSDTIIKNNNLKES CCCHHHHHHHHHHHHHHHCCCCCCEEECEEECCCCCHHHHHHHHCCCCCCEEECCCCCCC TIHPGQVLNIPCNTYTVKSGDSLFLISKAQGISLYNLRKANNKLDDTIYPGQVLNLPGKT CCCCCCEEEECCCEEEECCCCEEEEEECCCCCEEEEEHHCCCCCCCCCCCCEEEECCCCC SSNTSPAPAPTTPKPIVNYTESDLDLLARLITAEAQSEPYSAQVAVASVVINRIKSSQFP CCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHCCCCCCHHHHHHHHHHHHHHHCCCCC NSISSVIYQKSDGYYQFTPVLNGWINKPATETSKKAAKEALYGSDPSKGALYYFDNTATN HHHHHHHEECCCCCEEEECHHHHHCCCCCCHHHHHHHHHHHCCCCCCCCEEEEEECCCCC KWLWSKPITARIGNMVYVK CEEECCCHHHHHCCEEEEC >Mature Secondary Structure TKHKSLKTLLATLTFCVGLSSPVFAADYRVSSGDSLYKIGQLFNVSSDTIIKNNNLKES CCHHHHHHHHHHHHHHHCCCCCCEEECEEECCCCCHHHHHHHHCCCCCCEEECCCCCCC TIHPGQVLNIPCNTYTVKSGDSLFLISKAQGISLYNLRKANNKLDDTIYPGQVLNLPGKT CCCCCCEEEECCCEEEECCCCEEEEEECCCCCEEEEEHHCCCCCCCCCCCCEEEECCCCC SSNTSPAPAPTTPKPIVNYTESDLDLLARLITAEAQSEPYSAQVAVASVVINRIKSSQFP CCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHCCCCCCHHHHHHHHHHHHHHHCCCCC NSISSVIYQKSDGYYQFTPVLNGWINKPATETSKKAAKEALYGSDPSKGALYYFDNTATN HHHHHHHEECCCCCEEEECHHHHHCCCCCCHHHHHHHHHHHCCCCCCCCEEEEEECCCCC KWLWSKPITARIGNMVYVK CEEECCCHHHHHCCEEEEC
PDB accession: NA
Resolution: NA
Structure class: Alpha Beta
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: 7.0
TargetDB status: NA
Availability: NA
References: 8752358; 8081503; 10197998 [H]