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]