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mspA | Porin; The major porin in this organism, forms a water-filled channel which favors the permeation of cations, amino acids, iron Fe(3+) and less efficiently phosphate. Does not transport Fe-ExoMS, the predominant siderophore. Plays a role in transport of beta-lactamase and hydrophilic fluoroquinolone antibiotics such as norfloxacin as well as chloramphenicol. There are about 2400 porins in wild-type, 800 in an mspA deletion and 150 in a double mspA-mspC deletion. Different conductance values with maxima at 2.3 and 4.6 nanosiemens might be caused by a simultaneous reconstitution of MspA [...] (211 aa) | ||||
pbpA | Penicillin binding protein transpeptidase domain protein; Cell wall formation. Plays an important role in cell division and cell shape maintenance by cross-linking adjacent peptidoglycan chains through transpeptidation. (491 aa) | ||||
ABK70477.1 | Identified by match to protein family HMM PF03734. (452 aa) | ||||
pbpB | Penicillin binding protein transpeptidase domain protein; Identified by match to protein family HMM PF00905; match to protein family HMM PF03717; Belongs to the transpeptidase family. (648 aa) | ||||
dapD | Tetrahydropicolinate succinylase; Catalyzes the conversion of the cyclic tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using succinyl-CoA. (314 aa) | ||||
ponA1 | Penicillin-binding protein 1; Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits) (By similarity). (785 aa) |