The gene/protein map for NC_009698 is currently unavailable.
Definition Clostridium botulinum A str. Hall, complete genome.
Accession NC_009698
Length 3,760,560

Click here to switch to the map view.

The map label for this gene is yomI [H]

Identifier: 153936288

GI number: 153936288

Start: 3072570

End: 3073094

Strand: Reverse

Name: yomI [H]

Synonym: CLC_2909

Alternate gene names: 153936288

Gene position: 3073094-3072570 (Counterclockwise)

Preceding gene: 153936121

Following gene: 153937201

Centisome position: 81.72

GC content: 26.1

Gene sequence:

>525_bases
TTGATTTTAATATTAACAATTATGTTATTAATAAATATAACAACTATAGCAAAATATATTTTCCCTATAAAATATAGAGA
TTATATAGATATGTATGCTAATGAACATAAATTAGATCCTTACTTTGTAGCAGCAGTTATAAAAACTGAAAGTAATTTTA
AAAAAGATGCTGCCTCTAAAAAAAATGCACAGGGACTTATGCAAATAACTCCAGAAACAGGAGAATGGGTAGCAGAAAAA
ATGGGAATGAAAGATTTTAATATTGATGATTTAAAAGATCCAGAAACTAATATAAAAATGGGATGTTGGTATTTAAATAA
TTTAAAAGAAGAATTTGATGGTAATATGGATCTTGTATTAGCTGCATATAATGGTGGTAGGGGAAATGTTCAGAAGTGGT
TAAAAGACTCAGAGCATTCAAAAGACGGTGAAAGTCTTCATTATATACCTTTTAAGGAAACAGACAAATATGTAAAAAAG
GTAAAGGCCATATATAATATATATAGATTTTTATATAAAAGTTAA

Upstream 100 bases:

>100_bases
AATTAGATAAGATTTTTATGGAAGTAATGATTAAAGCAAGGCAGAAGGGGGGAGTGCTCTAATATTAGGGCAAAAAAAAG
TGAAGTTTTTAAGAAGACTT

Downstream 100 bases:

>100_bases
ATAATAATTTAATAAGTTTATTGACAATAATATAAAAATATTATAATATAACTATAACTTATTTGTTCTATTAAAATTTA
TGTACCGAAATTTAGCAGGT

Product: transglycosylase SLT domain-containing protein

Products: 1,6-Anhydrobond [C]

Alternate protein names: NA

Number of amino acids: Translated: 174; Mature: 174

Protein sequence:

>174_residues
MILILTIMLLINITTIAKYIFPIKYRDYIDMYANEHKLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPETGEWVAEK
MGMKDFNIDDLKDPETNIKMGCWYLNNLKEEFDGNMDLVLAAYNGGRGNVQKWLKDSEHSKDGESLHYIPFKETDKYVKK
VKAIYNIYRFLYKS

Sequences:

>Translated_174_residues
MILILTIMLLINITTIAKYIFPIKYRDYIDMYANEHKLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPETGEWVAEK
MGMKDFNIDDLKDPETNIKMGCWYLNNLKEEFDGNMDLVLAAYNGGRGNVQKWLKDSEHSKDGESLHYIPFKETDKYVKK
VKAIYNIYRFLYKS
>Mature_174_residues
MILILTIMLLINITTIAKYIFPIKYRDYIDMYANEHKLDPYFVAAVIKTESNFKKDAASKKNAQGLMQITPETGEWVAEK
MGMKDFNIDDLKDPETNIKMGCWYLNNLKEEFDGNMDLVLAAYNGGRGNVQKWLKDSEHSKDGESLHYIPFKETDKYVKK
VKAIYNIYRFLYKS

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: Contains 10 TPR repeats [H]

Homologues:

Organism=Escherichia coli, GI87082441, Length=153, Percent_Identity=33.9869281045752, Blast_Score=86, Evalue=2e-18,

Paralogues:

None

Copy number: NA

Swissprot (AC and ID): NA

Other databases:

- InterPro:   IPR011055
- InterPro:   IPR008258
- InterPro:   IPR016047
- InterPro:   IPR010090
- InterPro:   IPR000189 [H]

Pfam domain/function: PF01551 Peptidase_M23; PF10145 PhageMin_Tail; PF01464 SLT [H]

EC number: 3.2.1.- [C]

Molecular weight: Translated: 20289; Mature: 20289

Theoretical pI: Translated: 8.34; Mature: 8.34

Prosite motif: NA

Important sites: NA

Signals:

None

Transmembrane regions:

None

Cys/Met content:

0.6 %Cys     (Translated Protein)
4.6 %Met     (Translated Protein)
5.2 %Cys+Met (Translated Protein)
0.6 %Cys     (Mature Protein)
4.6 %Met     (Mature Protein)
5.2 %Cys+Met (Mature Protein)

Secondary structure:

>Translated Secondary Structure
MILILTIMLLINITTIAKYIFPIKYRDYIDMYANEHKLDPYFVAAVIKTESNFKKDAASK
CHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHCCCCCCCCEEEEEEEECCCCHHHHHCCC
KNAQGLMQITPETGEWVAEKMGMKDFNIDDLKDPETNIKMGCWYLNNLKEEFDGNMDLVL
CCCCCEEEECCCHHHHHHHHCCCCCCCCCCCCCCCCCEEEEHHHHHHHHHHHCCCEEEEE
AAYNGGRGNVQKWLKDSEHSKDGESLHYIPFKETDKYVKKVKAIYNIYRFLYKS
EEECCCCCCHHHHHHCCCCCCCCCEEEECCCHHHHHHHHHHHHHHHHHHHHHCC
>Mature Secondary Structure
MILILTIMLLINITTIAKYIFPIKYRDYIDMYANEHKLDPYFVAAVIKTESNFKKDAASK
CHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHCCCCCCCCEEEEEEEECCCCHHHHHCCC
KNAQGLMQITPETGEWVAEKMGMKDFNIDDLKDPETNIKMGCWYLNNLKEEFDGNMDLVL
CCCCCEEEECCCHHHHHHHHCCCCCCCCCCCCCCCCCEEEEHHHHHHHHHHHCCCEEEEE
AAYNGGRGNVQKWLKDSEHSKDGESLHYIPFKETDKYVKKVKAIYNIYRFLYKS
EEECCCCCCHHHHHHCCCCCCCCCEEEECCCHHHHHHHHHHHHHHHHHHHHHCC

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: 10.0

TargetDB status: NA

Availability: NA

References: 9384377 [H]