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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0523 IGR0524 IGR0525 IGR0526 gcr, - NG0627 gyrA, - NG0629 mfd, - NG0623 tpn, - NG0628 mltB, - NG0626 acdV, - NG0624 gcr, - NG0627 gyrA, - NG0629 mfd, - NG0623 tpn, - NG0628 mltB, - NG0626 acdV, - NG0624 Type: direct, Name:  - 133 gcr, - NG0627 gyrA, - NG0629 mfd, - NG0623 tpn, - NG0628 mltB, - NG0626 acdV, - NG0624 NG0625 NG0625
* Calculated from Protein Sequence

Gene ID: NG0626

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
mltB  

Definition:
membrane-bound lytic murein transglycosylase B, MltB

Gene Start:
614121

Gene Stop:
615209

Gene Length:
1089

Molecular Weight*:
39809

pI*:
8.60

Net Charge*:
3.13

EC:
3.2.1.-  4.2.1.96  

Functional Class:
Cell envelope; Murein sacculus and peptidoglycan  

Pathway: pathway table
Aminosugars metabolism
Nucleotide sugars metabolism

Secondary Evidence:
Dijkstra,A.J., Hermann,F. and Keck,W. Cloning and controlled overexpression of the gene encoding the 35 kDa soluble lytic transglycosylase from Escherichia coli. FEBS Lett. 366(2/3): 115-118 (1995)

Ehlert,K., Holtje,J.V. and Templin,M.F. Cloning and expression of a murein hydrolase lipoprotein from Escherichia coli. Mol. Microbiol. 16 (4): 761-768 (1995) [Medline: 96065704].

Dijkstra,A.J., Hermann,F. and Keck,W. Cloning and controlled overexpression of the gene encoding the 35 kDa soluble lytic transglycosylase from Escherichia coli. FEBS Lett. 366 (2-3): 115-118 (1995) [Medline: 95309413].

van Asselt,E.J. and Dijkstra,B.W. Binding of calcium in the EF-hand of Escherichia coli lytic transglycosylase Slt35 is important for stability. FEBS Lett. 458 (3): 429-435 (1999) [Medline: 20035731].

van Asselt,E.J., Dijkstra,A.J., Kalk,K.H., Takacs,B., Keck,W. and Dijkstra,B.W. Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals a lysozyme-like catalytic domain with an EF-hand. Structure 7, 1167-1180 (1999)

van Asselt,E.J., Kalk,K.H. and Dijkstra,B.W. Crystallographic studies of the interactions of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan. Biochemistry 39 (8): 1924-1934 (2000) [Medline: 20149813].

Comment:
From GenBANK (gi:730034): This is a murein-degrading enzyme. It catalyzes the cleavage of the glycosidic bonds between n-acetylmuramic acid and n-acetylglucosamine residues in peptidoglycan and may play a role in recycling of muropeptides during cell elongation and/or cell division. Catalytic activity: 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. This monomer is attached to the outer membrane by a lipid anchor and exposed to the periplasmic side.

See also NG0608, MltD.

Oklahoma ID: NGO.626

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to membrane-bound lytic transglycosylases; e.g. residues 60-358 are 40% similar to AF147448 of Pseudomonas aeruginosa.

Residues 1-363 are 95% similar to NMB1279, a membrane-bound lytic murein transglycosylase B, and residues 40-363 are 95% similar to NMA1488, a murein hydrolase, both proteins of N.meningitidis (11283076, 11283074).

COGS Summary:  COGS Search
No hits to the COGs database.

Blocks Summary:  Blocks Search
No significant hits to the Blocks database.

ProDom Summary:  Protein Domain Search
Residues 129-358 are 41% similar to a (LYTIC TRANSGLYCOSYLASE MEMBRANE-BOUND MUREIN B PRECURSOR) protein domain (PD024806) which is seen in MLTB_ECOLI.



Paralogs:  Local Blast Search


NG0626 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
No significant hits to the Pfam 11.0 database

Structural Feature(s):
Feature Type  Start  Stop
may be a lipoprotein  
  
gram negative signal  
1  
23
non-globular  
24  
96

PDB Hit:
pdb|1D0K|1D0K-A THE ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE 190.0 2e-49
pdb|1LTM|1LTM ACCELERATED X-RAY STRUCTURE ELUCIDATION OF A 36 190.0 2e-49
pdb|1D0K|1D0K-A THE ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE 192.0 1e-49
pdb|1LTM|1LTM ACCEL

Gene Protein Sequence:
MEKRKILPLAICLAALSACTAMEARTPRANEAQAPRADEMKKESRPAFDA
AAVPVSDSGFAANANVRRFVDDEVGKGDFSQAEWQDFFDKAAYKADIVKI
MHRPSTSRPWYVFRTGNSGRAKFHGARRFYAENRAVIDDVAQKYGVPAEL
IVAIIGIETNYGKNTGSFRVADALATLGFDYPRRAGFFQKELVELLKLAK
EEGGDVFAFKGSYAGAMGMPQFMPSSYRKWAVDYDGDGHRDIWGNVGDVA
ASVANYMKQHGWRTGGKMLVSATLAPGADVQAIIGEKTALTRTVADLKAY
GIIPGETLADDEKAVLFKLETAPGVFEYYLGLNNFYTVWQYNHSRMYVTA
VRDIANSLGGPGL

Gene Nucleotide Sequence:  Sequence Viewer
ATGGAAAAGAGAAAAATACTGCCGCTGGCAATTTGTTTGGCGGCTTTGTC
TGCCTGTACGGCGATGGAGGCCCGCACACCCCGGGCAAATGAAGCCCAAG
CCCCCCGCGCGGATGAAATGAAAAAAGAAAGCCGCCCCGCGTTTGACGCG
GCAGCCGTACCGGTATCCGACAGCGGGTTTGCCGCCAATGCAAATGTCCG
CCGTTTTGTGGACGATGAAGTCGGGAAAGGGGATTTTTCCCAGGCGGAAT
GGCAGGATTTTTTTGACAAAGCGGCTTACAAGGCGGACATCGTCAAGATT
ATGCACCGACCCTCCACATCGCGTCCGTGGTATGTGTTCCGCACGGGAAA
TTCGGGCAGGGCGAAATTTCACGGCGCGCGCAGGTTTTATGCGGAAAACC
GCGCGGTTATCGATGATGTGGCGCAAAAATACGGCGTGCCTGCCGAGCTT
ATCGTGGCGATTATCGGGATTGAAACGAATTACGGCAAAAATACGGGCAG
TTTCCGTGTGGCGGACGCATTGGCGACTTTAGGCTTTGATTATCCCCGCC
GCGCCGGGTTTTTCCAAAAAGAATTGGTCGAGCTTTTAAAGCTGGCAAAA
GAAGAAGGCGGTGATGTTTTCGCCTTTAAGGGCAGCTATGCGGGTGCAAT
GGGTATGCCGCAATTTATGCCTTCGAGCTACCGGAAATGGGCGGTGGATT
ATGACGGGGACGGACATCGGGATATATGGGGCAACGTCGGTGATGTCGCG
GCATCGGTTGCCAATTATATGAAGCAGCACGGTTGGCGCACGGGCGGTAA
AATGTTGGTGTCGGCGACGTTGGCGCCGGGTGCGGATGTTCAGGCAATCA
TTGGCGAAAAAACCGCCCTGACGCGGACGGTGGCGGATTTGAAGGCGTAC
GGCATCATCCCCGGGGAAACGCTCGCAGATGATGAAAAGGCGGTTTTGTT
CAAACTGGAAACCGCACCCGGCGTGTTTGAATATTATTTGGGCTTGAACA
ATTTTTATACGGTATGGCAGTACAACCACAGCCGGATGTATGTAACGGCG
GTCAGGGACATTGCCAATTCGCTCGGCGGCCCGGGATTG


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