| Definition | Acinetobacter baumannii AB0057, complete genome. |
|---|---|
| Accession | NC_011586 |
| Length | 4,050,513 |
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The map label for this gene is yjbJ [H]
Identifier: 213158342
GI number: 213158342
Start: 3167250
End: 3168026
Strand: Direct
Name: yjbJ [H]
Synonym: AB57_3072
Alternate gene names: 213158342
Gene position: 3167250-3168026 (Clockwise)
Preceding gene: 213158339
Following gene: 213158343
Centisome position: 78.19
GC content: 43.11
Gene sequence:
>777_bases ATGTACATTTACCAAGACAAAAACGGCAGTACTTTACTGACTAACCGTAAAAGTTATGACCATTTACTCAAAAAAGTAAA AGTCACCTACTACCCGGATAGTAATATTCATAGTTATAGCAACTGGGGGACTTCAGAGGCTTCGGTTCTACCAAGCTATA GCAAAAACAAAAATGCTTTTGACCATATTATTAAGCAGGCAGCACAACAGCACGGCGTTTCGGAAGGATTAATCAAAGCC GTTATGCATACCGAGTCTGGCTTTAATGTAAATGCCCGCTCCCCGGTTGGCGCCCAAGGTTTAATGCAGCTTATGCCGGC TACTGCTCGTCGTTTTAACGTATCTAACGCTTATGATCCTCAGCAAAATATCTTCGCTGGTGCTAAATATTTAAGTTGGT TGCTCAAACGTTTTAACGGCAATACGCAAATGGCGCTTGCCGCTTATAATGCAGGAGAAGGAAACGTCGATAAATATGGC GGTATTCCGCCATTCCGTGAAACCCAAGATTATGTTCGCCGAGTCACTAGCCGCTACCAAAACTTATATTCTTCTGGTGT AGGCCTTTCTTCTTTTAGCAATTCGAGTATTTCTGCCCAAGCGATAAACCAACCAGCCATACCGCACAGTACTTCGACGC AAGTCTCTGCTCAGCCTATTAAGTATTCTTCTTCACGCCAAATCGTTACATTGCCAGATGGTACATATACAGACGCACCT ACGGGAACTTATGTCACCAATAATGCAACTGCTATTGCACACATCCGGATTGAGTAA
Upstream 100 bases:
>100_bases TGAATAACATAAAATGAAAAATTCGGTTCAATATCTTTTTTCTTGTTTACTGGGGATGACCACTTTTTCGGTAGGTATAA CGCCGACTTCAGCAGGTCAG
Downstream 100 bases:
>100_bases GCTTAAAAAGCCTCATATCTTACGGTTACTTATTTAGCGGGCCCTATTGTCAAAAAATTGTAATGATCTATTACTCCCAC TTTCGTGTTCAGAGGGGCCT
Product: lytic transglycosylase, catalytic
Products: 1,6-Anhydrobond [C]
Alternate protein names: NA
Number of amino acids: Translated: 258; Mature: 258
Protein sequence:
>258_residues MYIYQDKNGSTLLTNRKSYDHLLKKVKVTYYPDSNIHSYSNWGTSEASVLPSYSKNKNAFDHIIKQAAQQHGVSEGLIKA VMHTESGFNVNARSPVGAQGLMQLMPATARRFNVSNAYDPQQNIFAGAKYLSWLLKRFNGNTQMALAAYNAGEGNVDKYG GIPPFRETQDYVRRVTSRYQNLYSSGVGLSSFSNSSISAQAINQPAIPHSTSTQVSAQPIKYSSSRQIVTLPDGTYTDAP TGTYVTNNATAIAHIRIE
Sequences:
>Translated_258_residues MYIYQDKNGSTLLTNRKSYDHLLKKVKVTYYPDSNIHSYSNWGTSEASVLPSYSKNKNAFDHIIKQAAQQHGVSEGLIKA VMHTESGFNVNARSPVGAQGLMQLMPATARRFNVSNAYDPQQNIFAGAKYLSWLLKRFNGNTQMALAAYNAGEGNVDKYG GIPPFRETQDYVRRVTSRYQNLYSSGVGLSSFSNSSISAQAINQPAIPHSTSTQVSAQPIKYSSSRQIVTLPDGTYTDAP TGTYVTNNATAIAHIRIE >Mature_258_residues MYIYQDKNGSTLLTNRKSYDHLLKKVKVTYYPDSNIHSYSNWGTSEASVLPSYSKNKNAFDHIIKQAAQQHGVSEGLIKA VMHTESGFNVNARSPVGAQGLMQLMPATARRFNVSNAYDPQQNIFAGAKYLSWLLKRFNGNTQMALAAYNAGEGNVDKYG GIPPFRETQDYVRRVTSRYQNLYSSGVGLSSFSNSSISAQAINQPAIPHSTSTQVSAQPIKYSSSRQIVTLPDGTYTDAP TGTYVTNNATAIAHIRIE
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=142, Percent_Identity=31.6901408450704, Blast_Score=68, Evalue=5e-13,
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: 28406; Mature: 28406
Theoretical pI: Translated: 9.90; Mature: 9.90
Prosite motif: NA
Important sites: NA
Signals:
None
Transmembrane regions:
None
Cys/Met content:
0.0 %Cys (Translated Protein) 1.9 %Met (Translated Protein) 1.9 %Cys+Met (Translated Protein) 0.0 %Cys (Mature Protein) 1.9 %Met (Mature Protein) 1.9 %Cys+Met (Mature Protein)
Secondary structure:
>Translated Secondary Structure MYIYQDKNGSTLLTNRKSYDHLLKKVKVTYYPDSNIHSYSNWGTSEASVLPSYSKNKNAF CEEEECCCCCEEEECCHHHHHHHHHEEEEECCCCCCCCCCCCCCCCHHCCCCCCCCCHHH DHIIKQAAQQHGVSEGLIKAVMHTESGFNVNARSPVGAQGLMQLMPATARRFNVSNAYDP HHHHHHHHHHCCCHHHHHHHHHHCCCCCCCCCCCCCCHHHHHHHHHHHHHHCCCCCCCCC QQNIFAGAKYLSWLLKRFNGNTQMALAAYNAGEGNVDKYGGIPPFRETQDYVRRVTSRYQ HHHHHHHHHHHHHHHHHHCCCCEEEEEEECCCCCCCCCCCCCCCCHHHHHHHHHHHHHHH NLYSSGVGLSSFSNSSISAQAINQPAIPHSTSTQVSAQPIKYSSSRQIVTLPDGTYTDAP HHHHCCCCCCCCCCCCCCHHHCCCCCCCCCCCCCCCCCCEEECCCCEEEECCCCCCCCCC TGTYVTNNATAIAHIRIE CCCEEECCCEEEEEEEEC >Mature Secondary Structure MYIYQDKNGSTLLTNRKSYDHLLKKVKVTYYPDSNIHSYSNWGTSEASVLPSYSKNKNAF CEEEECCCCCEEEECCHHHHHHHHHEEEEECCCCCCCCCCCCCCCCHHCCCCCCCCCHHH DHIIKQAAQQHGVSEGLIKAVMHTESGFNVNARSPVGAQGLMQLMPATARRFNVSNAYDP HHHHHHHHHHCCCHHHHHHHHHHCCCCCCCCCCCCCCHHHHHHHHHHHHHHCCCCCCCCC QQNIFAGAKYLSWLLKRFNGNTQMALAAYNAGEGNVDKYGGIPPFRETQDYVRRVTSRYQ HHHHHHHHHHHHHHHHHHCCCCEEEEEEECCCCCCCCCCCCCCCCHHHHHHHHHHHHHHH NLYSSGVGLSSFSNSSISAQAINQPAIPHSTSTQVSAQPIKYSSSRQIVTLPDGTYTDAP HHHHCCCCCCCCCCCCCCHHHCCCCCCCCCCCCCCCCCCEEECCCCEEEECCCCCCCCCC TGTYVTNNATAIAHIRIE CCCEEECCCEEEEEEEEC
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]