Peptidoglycan D,D-transpeptidase MrdA
Also known as: JW0630, b0635, mrdA, pbpA
Function
Catalyzes cross-linking of the peptidoglycan cell wall. Responsible for the determination of the rod shape of the cell. Is probably required for lateral peptidoglycan synthesis and maintenance of the correct diameter during lateral and centripetal growth.
Classification
- Family (Pfam)
- PF03717 PBP_dimer, PF00905 Transpeptidase
- InterPro
- Beta-lactam/transpept, Beta-lactam/transpept-like, PBP_dimer, PBP_dimer_sf, PCN-bd_Tpept, Penicillin-binding_protein_2
- Functional cluster
- Translation Initiation/Elongation GTPases
Experimental structures · PDB · 4
A predicted model is available from AlphaFold.
Gene Ontology · 10
- GO:0030288 outer membrane-bounded periplasmic space
- GO:0005886 plasma membrane
- GO:0008658 penicillin binding
- GO:0071972 peptidoglycan L,D-transpeptidase activity
- GO:0009002 serine-type D-Ala-D-Ala carboxypeptidase activity
- GO:0071555 cell wall organization
- GO:0009252 peptidoglycan biosynthetic process
- GO:0006508 proteolysis
- GO:0008360 regulation of cell shape
- GO:0046677 response to antibiotic
Drugs targeting this protein · 87
- CEFOTAXIME SODIUM inhibitor
- AMOXICILLIN inhibitor
- CEFUROXIME AXETIL inhibitor
- PENICILLIN G SODIUM inhibitor
- CEFAMANDOLE inhibitor
- CYCLACILLIN inhibitor
- MOXALACTAM DISODIUM inhibitor
- CEPHALEXIN HYDROCHLORIDE inhibitor
- CEFOPERAZONE SODIUM inhibitor
- CEFAZOLIN SODIUM inhibitor
- CEFOXITIN SODIUM inhibitor
- CEPHALEXIN inhibitor
- LORACARBEF inhibitor
- CEFPIRAMIDE SODIUM inhibitor
- AMPICILLIN SODIUM inhibitor
- CEFTAZIDIME SODIUM inhibitor
- PIPERACILLIN SODIUM inhibitor
- PENICILLIN V POTASSIUM inhibitor
- TICARCILLIN DISODIUM inhibitor
- CEFEPIME HYDROCHLORIDE inhibitor
- BACAMPICILLIN HYDROCHLORIDE inhibitor
- CEPHALOGLYCIN inhibitor
- CEFTIBUTEN DIHYDRATE inhibitor
- CARBENICILLIN INDANYL SODIUM inhibitor
- CEFONICID SODIUM inhibitor
- CEFPODOXIME PROXETIL inhibitor
- CEFACLOR inhibitor
- CEFTIZOXIME SODIUM inhibitor
- CEPHAPIRIN SODIUM inhibitor
- CEFORANIDE inhibitor
- CEFOTETAN DISODIUM inhibitor
- CEFMETAZOLE SODIUM inhibitor
- CEFTOLOZANE SULFATE inhibitor
- PENICILLIN G POTASSIUM inhibitor
- ERTAPENEM SODIUM inhibitor
- RAZUPENEM inhibitor
- FAROPENEM MEDOXOMIL inhibitor
- MEROPENEM inhibitor
- TEMOCILLIN inhibitor
- ERTAPENEM inhibitor
- CEFIXIME inhibitor
- FLOMOXEF inhibitor
- AZTREONAM inhibitor
- CEPHRADINE inhibitor
- CEFTIBUTEN inhibitor
- PHENETHICILLIN inhibitor
- CEFAMANDOLE NAFATE inhibitor
- TALAMPICILLIN inhibitor
- CEPHALOTHIN SODIUM inhibitor
- CEFADROXIL inhibitor
- AMDINOCILLIN PIVOXIL inhibitor
- CEFPODOXIME inhibitor
- MEZLOCILLIN SODIUM inhibitor
- AMPICILLIN inhibitor
- SULOPENEM inhibitor
- PENAMECILLIN inhibitor
- TEBIPENEM PIVOXIL inhibitor
- CEFUROXIME SODIUM inhibitor
- FLOXACILLIN inhibitor
- CEFTIOFUR inhibitor
- CEFODIZIME inhibitor
- PIVAMPICILLIN inhibitor
- CEFMENOXIME HYDROCHLORIDE inhibitor
- CEFSULODIN inhibitor
- CEFTAROLINE FOSAMIL ACETATE inhibitor
- AZTREONAM LYSINE inhibitor
- PENICILLIN G BENZATHINE inhibitor
- CEFIDEROCOL inhibitor
- CEFIDEROCOL SULFATE TOSYLATE inhibitor
- CEFILAVANCIN inhibitor
- CEFOTIAM HYDROCHLORIDE inhibitor
- DORIPENEM MONOHYDRATE inhibitor
- IMIPENEM inhibitor
- CEFTAZIDIME inhibitor
- CEFDITOREN PIVOXIL inhibitor
- SULOPENEM ETZADROXIL inhibitor
- DORIPENEM inhibitor
- CEFTAROLINE FOSAMIL inhibitor
- CEFTOBIPROLE inhibitor
- AMDINOCILLIN inhibitor
- CEFPROZIL, (E)- inhibitor
- FAROPENEM inhibitor
- CARBENICILLIN DISODIUM inhibitor
- CEFTRIAXONE SODIUM inhibitor
- PENICILLIN V inhibitor
- CEFPIROME inhibitor
- CEFDINIR inhibitor
Related proteins · sequence + function similarity
- Peptidoglycan D,D-transpeptidase MrdA 1.00
- Peptidoglycan D,D-transpeptidase MrdA 0.95
- Peptidoglycan D,D-transpeptidase MrdA 0.90
- Peptidoglycan D,D-transpeptidase MrdA 0.86
- Peptidoglycan D,D-transpeptidase MrdA 0.86
- Probable peptidoglycan D,D-transpeptidase PbpC 0.85
- Peptidoglycan D,D-transpeptidase FtsI 0.85
- Probable peptidoglycan D,D-transpeptidase PenA 0.83
- Probable peptidoglycan D,D-transpeptidase PenA 0.83
- Probable peptidoglycan D,D-transpeptidase PenA 0.82
- Penicillin-binding protein 1A 0.82
- Peptidoglycan D,D-transpeptidase FtsI 0.81
Co-cited proteins · studied together in the literature
- Ribosomal RNA large subunit methyltransferase H 1 shared papers
- Peptidoglycan glycosyltransferase MrdB 2 shared papers
- Peptidoglycan D,D-transpeptidase FtsI 1 shared papers
- Stage V sporulation protein E 1 shared papers
- Ribosomal silencing factor RsfS 1 shared papers
- Endolytic peptidoglycan transglycosylase RlpA 1 shared papers
Literature · 12 cited papers
- Structural basis of peptidoglycan synthesis by E. coli RodA-PBP2 complex. Nat. Commun. · 2023
- Structural Basis for E. coli Penicillin Binding Protein (PBP) 2 Inhibition, a Platform for Drug Design. J. Med. Chem. · 2019
- Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol. Syst. Biol. · 2006
- Penicillin-binding protein PBP2 of Escherichia coli localizes preferentially in the lateral wall and at mid-cell in comparison with the old cell pole. Mol. Microbiol. · 2003
- The complete genome sequence of Escherichia coli K-12. Science · 1997
- A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. · 1996
- Cell shape and division in Escherichia coli: experiments with shape and division mutants. J. Bacteriol. · 1985
- Nucleotide sequence of the pbpA gene and characteristics of the deduced amino acid sequence of penicillin-binding protein 2 of Escherichia coli K12. Eur. J. Biochem. · 1986
- Identification of the penicillin-binding active site of penicillin-binding protein 2 of Escherichia coli. J. Biochem. · 1988
- Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillin-binding protein 2 and rodA protein. J. Biol. Chem. · 1986
- Nucleotide sequence of the rodA gene, responsible for the rod shape of Escherichia coli: rodA and the pbpA gene, encoding penicillin-binding protein 2, constitute the rodA operon. J. Bacteriol. · 1989
- Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc. Natl. Acad. Sci. U.S.A. · 1975
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