penicillin-binding protein, 1A family. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]

Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].

Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].

penicillin-binding protein 1B. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of a particular bifunctional transglycosylase/transpeptidase in E. coli and other Proteobacteria, designated penicillin-binding protein 1B. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]

penicillin-binding protein 1C. This subfamily of the penicillin binding proteins includes the member from E. coli designated penicillin-binding protein 1C. Members have both transglycosylase and transpeptidase domains and are involved in forming cross-links in the late stages of peptidoglycan biosynthesis. All members of this subfamily are presumed to have the same basic function. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]

Crystalstructure of PBP1a in complex with compound 17 ((4Z,8S,11E,14S)-5-(2-amino-1,3-thiazol-4-yl)-14-(5,6-dihydroxy-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-8-formyl-2-methyl-6-oxo-3,10-dioxa-4,7,11-triazatetradeca-4,11-diene-2,12,14-tricarboxylic acid) [Pseudomonas aeruginosa PAO1]

ChainA, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDF_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDI_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDI_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDX_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDX_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE0_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE0_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE1_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE1_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii]

E.coli PBP1b in complex with FPI-1465 [Escherichia coli K-12],5HL9_A E. coli PBP1b in complex with acyl-ampicillin and moenomycin [Escherichia coli K-12],5HLA_A E. coli PBP1b in complex with acyl-cephalexin and moenomycin [Escherichia coli K-12],5HLB_A E. coli PBP1b in complex with acyl-aztreonam and moenomycin [Escherichia coli K-12],5HLD_A E. coli PBP1b in complex with acyl-CENTA and moenomycin [Escherichia coli K-12],6YN0_A Structure of E. coli PBP1b with a FtsN peptide activating transglycosylase activity [Escherichia coli K-12],7LQ6_A Chain A, Penicillin-binding protein 1B [Escherichia coli K-12]

CrystalStructure of the Full-Length Transglycosylase PBP1b from Escherichia coli [Escherichia coli K-12]

CrystalStructure of the Full-Length Transglycosylase PBP1b from Escherichia coli [Escherichia coli]

Penicillin-binding protein 1A OS=Aquifex aeolicus (strain VF5) OX=224324 GN=mrcA PE=1 SV=1

Penicillin-binding protein 1A OS=Neisseria gonorrhoeae OX=485 GN=mrcA PE=1 SV=3

Penicillin-binding protein 1A OS=Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090) OX=242231 GN=mrcA PE=3 SV=3

Penicillin-binding protein 1A OS=Neisseria meningitidis serogroup B (strain MC58) OX=122586 GN=mrcA PE=3 SV=1

Penicillin-binding protein 1A OS=Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 / Z2491) OX=122587 GN=mrcA PE=3 SV=1