RegulonDB RegulonDB 11.0: Gene Form
   

mltA gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

mltA tcdA metZ ppGpp anti-anti-terminator anti-terminator terminator anti-anti-terminator anti-terminator terminator metZp metZp mltAp6 mltAp6 TSS_3122 TSS_3122

Gene      
Name: mltA    Texpresso search in the literature
Synonym(s): ECK2809, G7457, b2813, mlt, ygdM
Genome position(nucleotides): 2946081 <-- 2947178
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 52.82
External database links:  
ASAP:
 ABE-0009228
ECHOBASE:
 EB2894
ECOLIHUB:
 mltA
OU-MICROARRAY:
 b2813
STRING:
 511145.b2813
COLOMBOS: mltA


Product      
Name: membrane-bound lytic murein transglycosylase A
Synonym(s): Mlt, Mlt38, MltA, YgdM
Sequence: Get amino acid sequence Fasta Format
Cellular location: inner membrane,outer membrane,periplasmic space
Molecular weight: 40.411
Isoelectric point: 9.326
Motif(s):
 
Type Positions Sequence Comment
1 -> 20 MKGRWVKYLLMGTVVAMLAA
21 -> 365 CSSKPTDRGQQYKDGKFTQPFSLVNQPDAVGAPINAGDFAEQINHIRNSSPRLYGNQSNVYNAVQEWLRAGGDTRNMRQFGIDAWQMEGADNYGNVQFTGYYTPVIQARHTRQGEFQYPIYRMPPKRGRLPSRAEIYAGALSDKYILAYSNSLMDNFIMDVQGSGYIDFGDGSPLNFFSYAGKNGHAYRSIGKVLIDRGEVKKEDMSMQAIRHWGETHSEAEVRELLEQNPSFVFFKPQSFAPVKGASAVPLVGRASVASDRSIIPPGTTLLAEVPLLDNNGKFNGQYELRLMVALDVGGAIKGQHFDIYQGIGPEAGHRAGWYNHYGRVWVLKTAPGAGNVFSG UniProt: Membrane-bound lytic murein transglycosylase A.
90 -> 257 AGGDTRNMRQFGIDAWQMEGADNYGNVQFTGYYTPVIQARHTRQGEFQYPIYRMPPKRGRLPSRAEIYAGALSDKYILAYSNSLMDNFIMDVQGSGYIDFGDGSPLNFFSYAGKNGHAYRSIGKVLIDRGEVKKEDMSMQAIRHWGETHSEAEVRELLEQNPSFVFFK
277 -> 354 SVASDRSIIPPGTTLLAEVPLLDNNGKFNGQYELRLMVALDVGGAIKGQHFDIYQGIGPEAGHRAGWYNHYGRVWVLK
317 -> 317 D D → A: reduced function

 
Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.2 - degradation of macromolecules --> 1.2.3 - proteins/peptides/glycopeptides
Gene Ontology Terms (GO)  
cellular_component GO:0009279 - cell outer membrane
GO:0019867 - outer membrane
GO:0016020 - membrane
GO:0030288 - outer membrane-bounded periplasmic space
GO:0005887 - integral component of plasma membrane
GO:0036405 - anchored component of cell outer membrane
molecular_function GO:0005515 - protein binding
GO:0016829 - lyase activity
GO:0004553 - hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008933 - lytic transglycosylase activity
biological_process GO:0000270 - peptidoglycan metabolic process
GO:0009254 - peptidoglycan turnover
GO:0009253 - peptidoglycan catabolic process
GO:0071555 - cell wall organization
Note(s): Note(s): ...[more].
Reference(s): [1] Barends TR., et al., 2005
[2] Blackburn NT., et al., 2001
[3] Engel H., et al., 1992
[4] Heidrich C., et al., 2002
[5] Korsak D., et al., 2005
[6] Rao S., et al., 2020
[7] Van Straaten KE., et al., 2004
External database links:  
ALPHAFOLD:
 P0A935
CAZY:
 GH102
DIP:
 DIP-51238N
ECOCYC:
 G7457-MONOMER
ECOLIWIKI:
 b2813
INTERPRO:
 IPR034654
INTERPRO:
 IPR036908
INTERPRO:
 IPR026044
INTERPRO:
 IPR010611
INTERPRO:
 IPR005300
PANTHER:
 PTHR30124
PDB:
 2GAE
PDB:
 2pi8
PDB:
 2pic
PDB:
 2pjj
PDB:
 2AE0
PFAM:
 PF03562
PFAM:
 PF06725
PRIDE:
 P0A935
PRODB:
 PRO_000023245
PROSITE:
 PS51257
REFSEQ:
 NP_417293
SMART:
 SM00925
SMR:
 P0A935
UNIPROT:
 P0A935


Operon      
Name: mltA         
Operon arrangement:
Transcription unit        Promoter
mltA


RNA cis-regulatory element    
Attenuation: Transcriptional


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_3122 2946548 reverse nd [RS-EPT-CBR] [8]
  promoter mltAp6 2947273 reverse nd [ICWHO] [9]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

 [ICWHO] Inferred computationally without human oversight


Reference(s)    

 [1] Barends TR., de Jong RM., van Straaten KE., Thunnissen AM., Dijkstra BW., 2005, Escherichia coli MltA: MAD phasing and refinement of a tetartohedrally twinned protein crystal structure., Acta Crystallogr D Biol Crystallogr 61(Pt 5):613-21

 [2] Blackburn NT., Clarke AJ., 2001, Identification of four families of peptidoglycan lytic transglycosylases., J Mol Evol 52(1):78-84

 [3] Engel H., Smink AJ., van Wijngaarden L., Keck W., 1992, Murein-metabolizing enzymes from Escherichia coli: existence of a second lytic transglycosylase., J Bacteriol 174(20):6394-403

 [4] 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

 [5] 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

 [6] Rao S., Bates GT., Matthews CR., Newport TD., Vickery ON., Stansfeld PJ., 2020, Characterizing Membrane Association and Periplasmic Transfer of Bacterial Lipoproteins through Molecular Dynamics Simulations., Structure 28(4):475-487.e3

 [7] Van Straaten KE., Dijkstra BW., Thunnissen AM., 2004, Purification, crystallization and preliminary X-ray analysis of the lytic transglycosylase MltA from Escherichia coli., Acta Crystallogr D Biol Crystallogr 60(Pt 4):758-60

 [8] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

 [9] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78

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