Penicillin-binding protein 1A
Details
- Name
- Penicillin-binding protein 1A
- Synonyms
- PBP-1a
- ponA
- Gene Name
- mrcA
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0001173|Penicillin-binding protein 1A MKFVKYFLILAVCCILLGAGSIYGLYRYIEPQLPDVATLKDVRLQIPMQIYSADGELIAQ YGEKRRIPVTLDQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGAST ITQQLARNFFLSPERTLMRKIKEVFLAIRIEQLLTKDEILELYLNKIYLGYRAYGVGAAA QVYFGKTVDQLTLNEMAVIAGLPKAPSTFNPLYSMDRAVARRNVVLSRMLDEGYITQQQF DQTRTEAINANYHAPEIAFSAPYLSEMVRQEMYNRYGESAYEDGYRIYTTITRKVQQAAQ QAVRNNVLDYDMRHGYRGPANVLWKVGESAWDNNKITDTLKALPTYGPLLPAAVTSANPQ QATAMLADGSTVALSMEGVRWARPYRSDTQQGPTPRKVTDVLQTGQQIWVRQVGDAWWLA QVPEVNSALVSINPQNGAVMALVGGFDFNQSKFNRATQALRQVGSNIKPFLYTAAMDKGL TLASMLNDVPISRWDASAGSDWQPKNSPPQYAGPIRLRQGLGQSKNVVMVRAMRAMGVDY AAEYLQRFGFPAQNIVHTESLALGSASFTPMQVARGYAVMANGGFLVDPWFISKIENDQG GVIFEAKPKVACPECDIPVIYGDTQKSNVLENNDVEDVAISREQQNVSVPMPQLEQANQA LVAKTGAQEYAPHVINTPLAFLIKSALNTNIFGEPGWQGTGWRAGRDLQRRDIGGKTGTT NSSKDAWFSGYGPGVVTSVWIGFDDHRRNLGHTTASGAIKDQISGYEGGAKSAQPAWDAY MKAVLEGVPEQPLTPPPGIVTVNIDRSTGQLANGGNSREEYFIEGTQPTQQAVHEVGTTI IDNGEAQELF
- Number of residues
- 850
- Molecular Weight
- 93635.545
- Theoretical pI
- 6.53
- GO Classification
- Functionspenicillin binding / peptidoglycan glycosyltransferase activity / serine-type D-Ala-D-Ala carboxypeptidase activityProcessescell wall organization / peptidoglycan biosynthetic process / proteolysis / regulation of cell shape / response to antibioticComponentsintegral component of plasma membrane
- General Function
- Serine-type d-ala-d-ala carboxypeptidase activity
- Specific Function
- 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).
- Pfam Domain Function
- Transmembrane Regions
- 6-26
- Cellular Location
- Cell inner membrane
- Gene sequence
>lcl|BSEQ0020469|Penicillin-binding protein 1A (mrcA) GTGAAGTTCGTAAAGTATTTTTTGATCCTTGCAGTCTGTTGCATTCTGCTGGGAGCAGGC TCGATTTATGGCCTATACCGCTACATCGAGCCACAACTGCCGGATGTGGCGACATTAAAA GATGTTCGCCTGCAAATTCCGATGCAGATTTACAGCGCCGATGGCGAGCTGATTGCTCAA TACGGTGAGAAACGTCGTATTCCGGTTACGTTGGATCAAATCCCACCGGAGATGGTGAAA GCCTTTATCGCGACAGAAGACAGCCGCTTCTACGAGCATCACGGCGTTGACCCGGTGGGG ATCTTCCGTGCAGCAAGCGTGGCGCTGTTCTCCGGTCACGCGTCACAAGGGGCAAGTACC ATTACCCAGCAGCTGGCGAGAAACTTCTTCCTCAGTCCAGAACGCACGCTGATGCGTAAG ATTAAGGAAGTCTTCCTCGCGATTCGCATTGAACAGCTGCTGACGAAAGACGAGATCCTC GAGCTTTATCTGAACAAGATTTACCTTGGTTACCGCGCCTATGGTGTCGGTGCTGCGGCA CAAGTCTATTTCGGAAAAACGGTCGACCAACTGACGCTGAACGAAATGGCGGTGATAGCC GGGCTGCCGAAAGCGCCTTCCACCTTCAACCCGCTCTACTCGATGGATCGTGCCGTCGCG CGGCGTAACGTCGTGCTGTCGCGGATGCTGGATGAAGGGTATATCACCCAACAACAGTTC GATCAGACACGCACTGAGGCGATTAACGCTAACTATCACGCGCCGGAGATTGCTTTCTCT GCGCCGTACCTGAGCGAAATGGTGCGCCAGGAGATGTATAACCGTTATGGCGAAAGTGCC TATGAAGACGGTTATCGCATTTACACCACCATCACCCGCAAAGTGCAGCAGGCCGCGCAG CAGGCGGTACGTAATAACGTGCTGGACTACGACATGCGCCACGGCTATCGCGGCCCGGCA AATGTGCTGTGGAAAGTGGGCGAGTCGGCGTGGGATAACAACAAGATTACCGATACGCTG AAGGCGCTGCCAACCTATGGTCCGCTGCTGCCTGCCGCAGTCACCAGCGCCAATCCTCAG CAAGCGACGGCGATGCTGGCGGACGGGTCGACCGTCGCATTGAGTATGGAAGGCGTTCGC TGGGCGCGTCCTTACCGTTCGGATACTCAGCAAGGACCGACGCCGCGTAAAGTGACCGAT GTTCTGCAAACGGGTCAGCAAATCTGGGTTCGTCAGGTTGGCGATGCATGGTGGCTGGCA CAAGTGCCGGAAGTGAACTCGGCGCTGGTGTCGATCAATCCGCAAAACGGTGCCGTTATG GCGCTGGTCGGTGGCTTTGATTTCAATCAGAGCAAGTTTAACCGCGCCACCCAGGCACTG CGTCAGGTGGGTTCCAACATCAAACCGTTCCTCTACACCGCGGCGATGGATAAAGGTCTG ACGCTGGCAAGTATGTTGAACGATGTGCCAATTTCTCGCTGGGATGCAAGTGCCGGTTCT GACTGGCAGCCGAAGAACTCACCACCGCAGTATGCTGGTCCAATTCGCTTACGTCAGGGG CTGGGTCAGTCGAAAAACGTGGTGATGGTACGCGCAATGCGGGCGATGGGCGTCGACTAC GCTGCAGAATATCTGCAACGCTTCGGCTTCCCGGCACAAAACATTGTCCACACCGAATCG CTGGCGCTGGGTTCAGCGTCCTTCACCCCAATGCAGGTGGCGCGCGGCTACGCGGTCATG GCGAACGGCGGCTTCCTGGTGGACCCGTGGTTTATCAGCAAAATTGAAAACGATCAGGGC GGCGTGATTTTCGAAGCGAAACCGAAAGTAGCCTGCCCGGAATGCGATATTCCGGTGATT TACGGTGATACGCAGAAATCGAACGTGCTGGAAAATAACGATGTTGAAGATGTCGCTATC TCCCGCGAGCAGCAGAATGTTTCTGTACCAATGCCGCAGCTGGAGCAGGCAAATCAGGCG TTAGTGGCGAAGACTGGCGCGCAGGAGTACGCACCGCACGTCATCAACACTCCGCTGGCA TTCCTGATTAAGAGTGCTTTGAACACCAATATCTTTGGTGAGCCAGGCTGGCAGGGTACT GGCTGGCGTGCAGGTCGTGATTTGCAGCGTCGCGATATCGGCGGGAAAACCGGGACCACT AACAGTTCGAAAGATGCGTGGTTCTCGGGTTACGGTCCGGGCGTTGTGACCTCGGTCTGG ATTGGCTTTGATGATCACCGTCGTAATCTCGGTCATACAACGGCTTCCGGAGCGATTAAA GATCAGATCTCAGGTTACGAAGGCGGTGCCAAGAGTGCCCAGCCTGCATGGGACGCTTAT ATGAAAGCCGTTCTTGAAGGTGTGCCGGAGCAGCCGCTGACGCCGCCACCGGGTATTGTG ACGGTGAATATCGATCGCAGCACCGGGCAGTTAGCTAATGGTGGCAACAGCCGCGAAGAG TATTTCATCGAAGGTACGCAGCCGACACAACAGGCAGTGCACGAGGTGGGAACGACCATT ATCGATAATGGCGAGGCACAGGAATTGTTCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P02918 UniProtKB Entry Name PBPA_ECOLI GenBank Protein ID 581194 GenBank Gene ID X02164 - General References
- Broome-Smith JK, Edelman A, Yousif S, Spratt BG: The nucleotide sequences of the ponA and ponB genes encoding penicillin-binding protein 1A and 1B of Escherichia coli K12. Eur J Biochem. 1985 Mar 1;147(2):437-46. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Keck W, Glauner B, Schwarz U, Broome-Smith JK, Spratt BG: Sequences of the active-site peptides of three of the high-Mr penicillin-binding proteins of Escherichia coli K-12. Proc Natl Acad Sci U S A. 1985 Apr;82(7):1999-2003. [Article]
- Ishino F, Mitsui K, Tamaki S, Matsuhashi M: Dual enzyme activities of cell wall peptidoglycan synthesis, peptidoglycan transglycosylase and penicillin-sensitive transpeptidase, in purified preparations of Escherichia coli penicillin-binding protein 1A. Biochem Biophys Res Commun. 1980 Nov 17;97(1):287-93. [Article]
- Goffin C, Ghuysen JM: Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol Mol Biol Rev. 1998 Dec;62(4):1079-93. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01598 Imipenem approved yes inhibitor Details DB01329 Cefoperazone approved, investigational yes inhibitor Details DB01332 Ceftizoxime approved, withdrawn yes inhibitor Details DB01333 Cefradine approved yes inhibitor Details DB01327 Cefazolin approved yes inhibitor Details DB01331 Cefoxitin approved yes inhibitor Details DB01328 Cefonicid approved, investigational yes inhibitor Details DB01415 Ceftibuten approved, investigational yes inhibitor Details DB00430 Cefpiramide approved yes inhibitor Details DB00438 Ceftazidime approved yes inhibitor Details DB00274 Cefmetazole approved, investigational yes inhibitor Details DB00303 Ertapenem approved, investigational yes inhibitor Details DB01414 Cefacetrile experimental, vet_approved yes inhibitor Details DB04570 Latamoxef approved, investigational unknown inhibitor Details DB06211 Doripenem approved, investigational yes antagonistinhibitor Details DB01413 Cefepime approved, investigational yes inhibitor Details DB00578 Carbenicillin approved, investigational yes inhibitor Details DB09319 Carindacillin approved, investigational yes inhibitor Details DB09050 Ceftolozane approved, investigational unknown Details DB01602 Bacampicillin approved, investigational yes inhibitor Details DB01000 Cyclacillin approved yes inhibitor Details DB00671 Cefixime approved, investigational yes binder Details