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The map label for this gene is yomI [H]

Identifier: 119944148

GI number: 119944148

Start: 469549

End: 470196

Strand: Reverse

Name: yomI [H]

Synonym: Ping_0367

Alternate gene names: 119944148

Gene position: 470196-469549 (Counterclockwise)

Preceding gene: 119944149

Following gene: 119944137

Centisome position: 10.31

GC content: 39.66

Gene sequence:

>648_bases
ATGAAACAACTCAAGTACATTCAAAAATGGAAAATTTTACTGTCGTTATTGGTTAGTTTACTGCTGACGAATAATGTCTG
TGCTGATGTTTATAGAATGATTGATAAAGAGGGTAATCAACATTTTGCTGAACGTAAAGTTGATTCAACTTACCACTTGA
TATTAAAAAGTGATTCTAATACAAGTTCAAACTCGTTCAATACCCAGAAACGTAAAAATGTGACTGTTGTTAGGGTACCA
AGGAACAAAACACTGCAAAAAAAATACCACCCTCTTATTCTTCAAGCGGCAAATCTATATCACCTGGAGCCATCATTTAT
TCATGCGGTGATCACAGCAGAATCCAGCTATCAGTATAATGCAGTTTCATCCGCTGGTGCGCAGGGTTTGATGCAGTTGA
TGCCGGAGACGGCGCTGCGTTTTGGTGTCAATGATCCTTTTGATCCCAAGCAGAGTATTCACGCCGGCACAGAATACCTG
TATACACTGCTGCAGGAGTTTAAAAGTAAAGAGCTCGCGTTAGCGGCATACAATGCAGGAGAGGGCACAGTAAGACGTTA
TAATAAAACAATTCCGCCCTACCCCGAGACTGAACACTATATTAATAAAGTAATGGGATTTTATTGGTATTACCGCAATA
GCCTCTAA

Upstream 100 bases:

>100_bases
AGCGCAAGCTTCACCAGTTAATGTCAACGAAGAAAAAAAGATAACTGAACAATAATAACTGAACAATAATAACTGAACAA
TAAAAGAGTCATCACTCCTT

Downstream 100 bases:

>100_bases
AGCCCCATTCTTTATTAAAGCGGTCCATAAGCTTAAATTTTATCCCTTTAGGCTAAAACTAATTGGCTTACGCGTTTTTT
TGACCGCTTTACTCTTTTCA

Product: lytic transglycosylase, catalytic

Products: 1,6-Anhydrobond [C]

Alternate protein names: NA

Number of amino acids: Translated: 215; Mature: 215

Protein sequence:

>215_residues
MKQLKYIQKWKILLSLLVSLLLTNNVCADVYRMIDKEGNQHFAERKVDSTYHLILKSDSNTSSNSFNTQKRKNVTVVRVP
RNKTLQKKYHPLILQAANLYHLEPSFIHAVITAESSYQYNAVSSAGAQGLMQLMPETALRFGVNDPFDPKQSIHAGTEYL
YTLLQEFKSKELALAAYNAGEGTVRRYNKTIPPYPETEHYINKVMGFYWYYRNSL

Sequences:

>Translated_215_residues
MKQLKYIQKWKILLSLLVSLLLTNNVCADVYRMIDKEGNQHFAERKVDSTYHLILKSDSNTSSNSFNTQKRKNVTVVRVP
RNKTLQKKYHPLILQAANLYHLEPSFIHAVITAESSYQYNAVSSAGAQGLMQLMPETALRFGVNDPFDPKQSIHAGTEYL
YTLLQEFKSKELALAAYNAGEGTVRRYNKTIPPYPETEHYINKVMGFYWYYRNSL
>Mature_215_residues
MKQLKYIQKWKILLSLLVSLLLTNNVCADVYRMIDKEGNQHFAERKVDSTYHLILKSDSNTSSNSFNTQKRKNVTVVRVP
RNKTLQKKYHPLILQAANLYHLEPSFIHAVITAESSYQYNAVSSAGAQGLMQLMPETALRFGVNDPFDPKQSIHAGTEYL
YTLLQEFKSKELALAAYNAGEGTVRRYNKTIPPYPETEHYINKVMGFYWYYRNSL

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=131, Percent_Identity=32.824427480916, Blast_Score=60, Evalue=7e-11,

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: 24808; Mature: 24808

Theoretical pI: Translated: 9.82; Mature: 9.82

Prosite motif: NA

Important sites: NA

Signals:

None

Transmembrane regions:

None

Cys/Met content:

0.5 %Cys     (Translated Protein)
2.3 %Met     (Translated Protein)
2.8 %Cys+Met (Translated Protein)
0.5 %Cys     (Mature Protein)
2.3 %Met     (Mature Protein)
2.8 %Cys+Met (Mature Protein)

Secondary structure:

>Translated Secondary Structure
MKQLKYIQKWKILLSLLVSLLLTNNVCADVYRMIDKEGNQHFAERKVDSTYHLILKSDSN
CCHHHHHHHHHHHHHHHHHHHHCCHHHHHHHHHHHCCCCHHHHHHHCCCEEEEEEECCCC
TSSNSFNTQKRKNVTVVRVPRNKTLQKKYHPLILQAANLYHLEPSFIHAVITAESSYQYN
CCCCCCCCHHHCCEEEEECCCCCCHHHHHCHHHEECCCEEECCHHHEEEEEECCCCCCCC
AVSSAGAQGLMQLMPETALRFGVNDPFDPKQSIHAGTEYLYTLLQEFKSKELALAAYNAG
HHHHHHHHHHHHHHHHHHHHCCCCCCCCCHHHHHHHHHHHHHHHHHHCCCCEEEEEECCC
EGTVRRYNKTIPPYPETEHYINKVMGFYWYYRNSL
CCHHHHHCCCCCCCCCHHHHHHHHHHHHHHHHCCC
>Mature Secondary Structure
MKQLKYIQKWKILLSLLVSLLLTNNVCADVYRMIDKEGNQHFAERKVDSTYHLILKSDSN
CCHHHHHHHHHHHHHHHHHHHHCCHHHHHHHHHHHCCCCHHHHHHHCCCEEEEEEECCCC
TSSNSFNTQKRKNVTVVRVPRNKTLQKKYHPLILQAANLYHLEPSFIHAVITAESSYQYN
CCCCCCCCHHHCCEEEEECCCCCCHHHHHCHHHEECCCEEECCHHHEEEEEECCCCCCCC
AVSSAGAQGLMQLMPETALRFGVNDPFDPKQSIHAGTEYLYTLLQEFKSKELALAAYNAG
HHHHHHHHHHHHHHHHHHHHCCCCCCCCCHHHHHHHHHHHHHHHHHHCCCCEEEEEECCC
EGTVRRYNKTIPPYPETEHYINKVMGFYWYYRNSL
CCHHHHHCCCCCCCCCHHHHHHHHHHHHHHHHCCC

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]