The gene/protein map for NC_009997 is currently unavailable.
Definition Shewanella baltica OS195 chromosome, complete genome.
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]