Definition | Shewanella baltica OS195 chromosome, complete genome. |
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Accession | NC_009997 |
Length | 5,347,283 |
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The map label for this gene is yomI [H]
Identifier: 160877480
GI number: 160877480
Start: 5174441
End: 5175196
Strand: Reverse
Name: yomI [H]
Synonym: Sbal195_4378
Alternate gene names: 160877480
Gene position: 5175196-5174441 (Counterclockwise)
Preceding gene: 160877481
Following gene: 160877477
Centisome position: 96.78
GC content: 49.47
Gene sequence:
>756_bases ATGTTGCTCACTCGCTCAGCACCGACTCGTACACAGATGACTGCGGCCTTTTTATCGCCTCGCCGCCTTGTCGTGTTGGG TCTGTGTTTATGGCTGATATCGAGTCTGATGATGAGTGTAAAAGCGGAGGAGGCGAGCGTTAAAGCTAAGCCGCGTATCG TTGCCAGATATTCAGAGAGCGGCATAGTCAGCCGTGAAGGCTTAGAAAAACTCAAGATTTATCAATACCAACAAGCCAAT GGCGTGACTGTATTTACCGACAAAGCCCCTGCCAATAATCCATATCAAATTCTGTTGTATGACTGTTTTGCCTGCCGCCC CGACTCGACTATAGATTGGAATGGTATCCGTTTATTTACCGCCAATTACGATGCCCTGATCACCCGTGCTGCCCATAAAC ATCAACTCGACCCCGCCTTGATCCGCGCCGTGATCCACGCAGAATCAGCCTTCAATGCGCGTGCATTGTCGCGTACTGGC GCGATGGGATTAATGCAATTAATGCCTGAAACGGCTAAAGAAATGGGTGTGGCAAACGCGTTTTTACCCGAAGAAAATAT CTTAGGTGGCAGTAAGTATCTGGCGCAAATGCTAAAACAGTTTAACGGGGATGTGGCCTTGGCCTGCGCGGCCTACAATG CGGGGCCGACAACTGTGGTGCAGTACAATGGCATTCCACCCTATCCTGAAACCCAAGCTTATGTTGAGCGGGTGAAAATT TTATTAAAGCGTTATCGCGAGCAGAAGGGCGTTTAG
Upstream 100 bases:
>100_bases GCGCGACCTTTTCAGCAGAATTTAGTCAGATAAACCGAGAGATGAAGCAACTCTTTGCTATTATTGAAGTACTTAAACTT AATCAGCACACGGGACTTTG
Downstream 100 bases:
>100_bases CTGTAGGCTTTGTGAACTTAAATCAAGCGGCGAAAACCTGAGATCATCGCCGCCATTTGAGTCGAAGGTTATTCGCCGAC TTCCCATTTTACTGTGATAT
Product: lytic transglycosylase
Products: 1,6-Anhydrobond [C]
Alternate protein names: NA
Number of amino acids: Translated: 251; Mature: 251
Protein sequence:
>251_residues MLLTRSAPTRTQMTAAFLSPRRLVVLGLCLWLISSLMMSVKAEEASVKAKPRIVARYSESGIVSREGLEKLKIYQYQQAN GVTVFTDKAPANNPYQILLYDCFACRPDSTIDWNGIRLFTANYDALITRAAHKHQLDPALIRAVIHAESAFNARALSRTG AMGLMQLMPETAKEMGVANAFLPEENILGGSKYLAQMLKQFNGDVALACAAYNAGPTTVVQYNGIPPYPETQAYVERVKI LLKRYREQKGV
Sequences:
>Translated_251_residues MLLTRSAPTRTQMTAAFLSPRRLVVLGLCLWLISSLMMSVKAEEASVKAKPRIVARYSESGIVSREGLEKLKIYQYQQAN GVTVFTDKAPANNPYQILLYDCFACRPDSTIDWNGIRLFTANYDALITRAAHKHQLDPALIRAVIHAESAFNARALSRTG AMGLMQLMPETAKEMGVANAFLPEENILGGSKYLAQMLKQFNGDVALACAAYNAGPTTVVQYNGIPPYPETQAYVERVKI LLKRYREQKGV >Mature_251_residues MLLTRSAPTRTQMTAAFLSPRRLVVLGLCLWLISSLMMSVKAEEASVKAKPRIVARYSESGIVSREGLEKLKIYQYQQAN GVTVFTDKAPANNPYQILLYDCFACRPDSTIDWNGIRLFTANYDALITRAAHKHQLDPALIRAVIHAESAFNARALSRTG AMGLMQLMPETAKEMGVANAFLPEENILGGSKYLAQMLKQFNGDVALACAAYNAGPTTVVQYNGIPPYPETQAYVERVKI LLKRYREQKGV
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:
None
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: 27822; Mature: 27822
Theoretical pI: Translated: 9.69; Mature: 9.69
Prosite motif: PS00922 TRANSGLYCOSYLASE
Important sites: NA
Signals:
None
Transmembrane regions:
None
Cys/Met content:
1.6 %Cys (Translated Protein) 3.6 %Met (Translated Protein) 5.2 %Cys+Met (Translated Protein) 1.6 %Cys (Mature Protein) 3.6 %Met (Mature Protein) 5.2 %Cys+Met (Mature Protein)
Secondary structure:
>Translated Secondary Structure MLLTRSAPTRTQMTAAFLSPRRLVVLGLCLWLISSLMMSVKAEEASVKAKPRIVARYSES CCCCCCCCCHHHHHHHHHCCHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCEEEEEECCC GIVSREGLEKLKIYQYQQANGVTVFTDKAPANNPYQILLYDCFACRPDSTIDWNGIRLFT CCCCHHHHHHHHHEEEECCCCEEEEECCCCCCCCCEEEEEEEECCCCCCCCCCCCEEEEE ANYDALITRAAHKHQLDPALIRAVIHAESAFNARALSRTGAMGLMQLMPETAKEMGVANA ECHHHHHHHHHHHHCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCCHHH FLPEENILGGSKYLAQMLKQFNGDVALACAAYNAGPTTVVQYNGIPPYPETQAYVERVKI CCCCCCCCCCHHHHHHHHHHHCCCEEEEEEEECCCCCEEEEECCCCCCCCHHHHHHHHHH LLKRYREQKGV HHHHHHHHCCC >Mature Secondary Structure MLLTRSAPTRTQMTAAFLSPRRLVVLGLCLWLISSLMMSVKAEEASVKAKPRIVARYSES CCCCCCCCCHHHHHHHHHCCHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCEEEEEECCC GIVSREGLEKLKIYQYQQANGVTVFTDKAPANNPYQILLYDCFACRPDSTIDWNGIRLFT CCCCHHHHHHHHHEEEECCCCEEEEECCCCCCCCCEEEEEEEECCCCCCCCCCCCEEEEE ANYDALITRAAHKHQLDPALIRAVIHAESAFNARALSRTGAMGLMQLMPETAKEMGVANA ECHHHHHHHHHHHHCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCCHHH FLPEENILGGSKYLAQMLKQFNGDVALACAAYNAGPTTVVQYNGIPPYPETQAYVERVKI CCCCCCCCCCHHHHHHHHHHHCCCEEEEEEEECCCCCEEEEECCCCCCCCHHHHHHHHHH LLKRYREQKGV HHHHHHHHCCC
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]