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Escherichia coli K-12 substr. MG1655 Enzyme: membrane-bound lytic murein transglycosylase D



Gene: mltD Accession Numbers: EG10246 (EcoCyc), b0211, ECK0211

Synonyms: yafG, dniR

Regulation Summary Diagram: ?

Summary:
E. coli MltD contains an N-terminal transglycosylase domain and two lysin motif (LysM) repeats at its C-terminus and is believed to be an outer membrane bound lytic murein transglycosylase [Bateman00]. A crystal structure of the LysM-type peptidoglycan-binding domain has been determined [Bateman00].

A mutant containing deletions in mltC, mltD and mltE has a defect in cell separation, growing as short chains of cells [Heidrich02]. A mutant strain lacking all six known lytic transglycosylases (mltA mltB mltC mltD mltE slt) is unable to induce β-lactamase and is more susceptible to certain high-molecular weight antibiotics which are normally inactive against Gram-negative bacteria, such as bacitracin, gallidermin and vancomycin [Korsak05].

MltD: membrane-bound lytic murein transglycosylase D
DniR: "regulator of synthesis of the dissimilatory nitrite reductase" [Kajie91]

Review: [Vollmer08]

Locations: outer membrane, inner membrane

Map Position: [232,597 <- 233,955] (5.01 centisomes)
Length: 1359 bp / 452 aa

Molecular Weight of Polypeptide: 49.417 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0000704 , CGSC:30876 , DIP:DIP-48010N , EchoBASE:EB0242 , EcoGene:EG10246 , EcoliWiki:b0211 , ModBase:P0AEZ7 , OU-Microarray:b0211 , PortEco:mltD , PR:PRO_000023248 , Pride:P0AEZ7 , Protein Model Portal:P0AEZ7 , RefSeq:NP_414747 , RegulonDB:EG10246 , SMR:P0AEZ7 , String:511145.b0211 , Swiss-Model:P0AEZ7 , UniProt:P0AEZ7

Relationship Links: InterPro:IN-FAMILY:IPR000189 , InterPro:IN-FAMILY:IPR002482 , InterPro:IN-FAMILY:IPR008258 , InterPro:IN-FAMILY:IPR018392 , InterPro:IN-FAMILY:IPR023346 , PDB:Structure:1E0G , Pfam:IN-FAMILY:PF01464 , Pfam:IN-FAMILY:PF01476 , Prosite:IN-FAMILY:PS00922 , Prosite:IN-FAMILY:PS51257 , Smart:IN-FAMILY:SM00257

In Paralogous Gene Group: 67 (4 members)

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0051353 - positive regulation of oxidoreductase activity Inferred from experiment [Kajie91]
GO:0000270 - peptidoglycan metabolic process Inferred by computational analysis [GOA01a]
GO:0071555 - cell wall organization Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0008933 - lytic transglycosylase activity Author statement Inferred by computational analysis [GOA01a, Bateman00]
GO:0016829 - lyase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016837 - carbon-oxygen lyase activity, acting on polysaccharides Inferred by computational analysis [GOA01]
Cellular Component: GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0009279 - cell outer membrane Author statement [Vollmer08]
GO:0016020 - membrane Author statement Inferred by computational analysis [UniProtGOA11a, GOA01a, Bateman00]

MultiFun Terms: cell structure murein
metabolism biosynthesis of macromolecules (cellular constituents) murein (peptidoglycan)

Essentiality data for mltD knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Credits:
Last-Curated ? 21-Sep-2011 by Mackie A , Macquarie University


Enzymatic reaction of: murein hydrolase (membrane-bound lytic murein transglycosylase D)

Synonyms: lytic murein transglycosylase

EC Number: 4.2.2.-

a peptidoglycan dimer (generic)[periplasmic space] <=> a lipid II[periplasmic space] + GlcNAc-1,6-anhydro-MurNAc-pentapeptide[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

Reversibility of this reaction is unspecified.


Sequence Features

Feature Class Location Citations Comment
Signal-Sequence 1 -> 15
[UniProt10]
UniProt: Non-Experimental Qualifier: potential;
Lipid-Binding-Site 16
[UniProt10]
UniProt: N-palmitoyl cysteine; Non-Experimental Qualifier: potential;
Chain 16 -> 452
[UniProt09]
UniProt: Membrane-bound lytic murein transglycosylase D;
Sequence-Conflict 69 -> 72
[Kajie91, UniProt10a]
Alternate sequence: MGIP → DGNS; UniProt: (in Ref. 5);
Protein-Segment 113 -> 198
[UniProt10]
UniProt: Slt-type domain; Sequence Annotation Type: region of interest;
Active-Site 125
[UniProt10]
UniProt: Non-Experimental Qualifier: by similarity;
Sequence-Conflict 217
[Kajie91, UniProt10a]
Alternate sequence: D → A; UniProt: (in Ref. 5);
Repeat 343 -> 385
[UniProt09]
UniProt: LysM 1;
Repeat 402 -> 443
[UniProt09]
UniProt: LysM 2;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b0211 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10246; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bateman00: Bateman A, Bycroft M (2000). "The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD)." J Mol Biol 299(4);1113-9. PMID: 10843862

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Heidrich02: Heidrich C, Ursinus A, Berger J, Schwarz H, Holtje JV (2002). "Effects of multiple deletions of murein hydrolases on viability, septum cleavage, and sensitivity to large toxic molecules in Escherichia coli." J Bacteriol 184(22);6093-9. PMID: 12399477

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kajie91: Kajie S, Ideta R, Yamato I, Anraku Y (1991). "Molecular cloning and DNA sequence of dniR, a gene affecting anaerobic expression of the Escherichia coli hexaheme nitrite reductase." FEMS Microbiol Lett 67(2);205-11. PMID: 1663890

Korsak05: Korsak D, Liebscher S, Vollmer W (2005). "Susceptibility to antibiotics and beta-lactamase induction in murein hydrolase mutants of Escherichia coli." Antimicrob Agents Chemother 49(4);1404-9. PMID: 15793119

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Vollmer08: Vollmer W, Bertsche U (2008). "Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli." Biochim Biophys Acta 1778(9);1714-34. PMID: 17658458


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sat Dec 20, 2014, biocyc12.