Penicillin-binding protein 2
Details
- Name
- Penicillin-binding protein 2
- Synonyms
- PBP-2
- pbpA
- Gene Name
- mrdA
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0017144|Penicillin-binding protein 2 MKLQNSFRDYTAESALFVRRALVAFLGILLLTGVLIANLYNLQIVRFTDYQTRSNENRIK LVPIAPSRGIIYDRNGIPLALNRTIYQIEMMPEKVDNVQQTLDALRSVVDLTDDDIAAFR KERARSHRFTSIPVKTNLTEVQVARFAVNQYRFPGVEVKGYKRRYYPYGSALTHVIGYVS KINDKDVERLNNDGKLANYAATHDIGKLGIERYYEDVLHGQTGYEEVEVNNRGRVIRQLK EVPPQAGHDIYLTLDLKLQQYIETLLAGSRAAVVVTDPRTGGVLALVSTPSYDPNLFVDG ISSKDYSALLNDPNTPLVNRATQGVYPPASTVKPYVAVSALSAGVITRNTTLFDPGWWQL PGSEKRYRDWKKWGHGRLNVTRSLEESADTFFYQVAYDMGIDRLSEWMGKFGYGHYTGID LAEERSGNMPTREWKQKRFKKPWYQGDTIPVGIGQGYWTATPIQMSKALMILINDGIVKV PHLLMSTAEDGKQVPWVQPHEPPVGDIHSGYWELAKDGMYGVANRPNGTAHKYFASAPYK IAAKSGTAQVFGLKANETYNAHKIAERLRDHKLMTAFAPYNNPQVAVAMILENGGAGPAV GTLMRQILDHIMLGDNNTDLPAENPAVAAAEDH
- Number of residues
- 633
- Molecular Weight
- 70856.1
- Theoretical pI
- 9.16
- GO Classification
- Functionsdrug binding / penicillin binding / peptidoglycan L,D-transpeptidase activity / serine-type D-Ala-D-Ala carboxypeptidase activityProcessescell wall organization / peptidoglycan biosynthetic process / proteolysis / regulation of cell shape / response to antibiotic / response to drugComponentsintegral component of plasma membrane
- General Function
- Serine-type d-ala-d-ala carboxypeptidase activity
- Specific Function
- Cell wall formation; PBP-2 is responsible for the determination of the rod shape of the cell. It synthesizes cross-linked peptidoglycan from lipid intermediates.
- Pfam Domain Function
- Transmembrane Regions
- 22-42
- Cellular Location
- Cell inner membrane
- Gene sequence
>lcl|BSEQ0017145|Penicillin-binding protein 2 (mrdA) ATGAAACTACAGAACTCTTTTCGCGACTATACGGCAGAGTCCGCGCTGTTTGTGCGCCGG GCGCTGGTCGCCTTTTTGGGGATTTTGCTGCTGACCGGCGTGCTTATCGCCAACCTGTAT AATCTGCAAATTGTTCGCTTTACCGACTACCAGACCCGCTCTAATGAAAACCGCATTAAG CTGGTGCCTATCGCGCCCAGCCGCGGCATTATCTACGATCGTAACGGTATCCCTCTGGCC CTCAACCGCACTATCTACCAGATAGAAATGATGCCGGAGAAAGTCGATAACGTGCAGCAA ACGCTGGACGCTTTGCGCAGCGTGGTAGATCTGACCGATGACGATATTGCTGCATTCCGA AAAGAGCGCGCACGTTCACACCGTTTCACCTCTATTCCGGTGAAAACTAACCTGACCGAA GTACAAGTAGCTCGCTTTGCCGTCAATCAGTACCGTTTTCCGGGTGTCGAAGTTAAAGGC TATAAACGTCGTTACTATCCTTACGGTTCGGCGTTGACCCACGTCATCGGCTATGTGTCG AAAATCAACGATAAAGACGTCGAACGCCTGAATAATGACGGCAAACTGGCCAACTATGCG GCAACGCATGATATCGGTAAGCTGGGCATTGAGCGTTACTATGAAGATGTGCTGCACGGT CAGACCGGTTATGAAGAGGTTGAAGTTAACAACCGTGGGCGTGTTATTCGCCAGTTAAAA GAAGTACCACCGCAAGCCGGACACGATATTTACCTGACGCTGGATCTCAAACTCCAGCAA TATATTGAAACGCTGCTGGCGGGTAGCCGCGCAGCTGTGGTAGTCACCGATCCGCGTACA GGTGGGGTGCTGGCGCTGGTTTCCACGCCTAGTTATGACCCAAACTTGTTTGTTGACGGT ATCTCCAGCAAAGATTATTCCGCCTTGTTGAACGATCCGAATACACCGCTGGTGAACCGC GCCACACAGGGGGTTTATCCTCCCGCGTCTACAGTTAAACCCTATGTGGCGGTTTCGGCA TTGAGCGCCGGGGTGATCACGCGCAATACGACGCTGTTTGACCCAGGCTGGTGGCAACTG CCAGGTTCGGAAAAACGTTATCGTGACTGGAAAAAATGGGGCCACGGGCGTCTGAATGTC ACAAGATCGCTGGAAGAATCTGCGGATACCTTCTTCTATCAGGTGGCCTACGATATGGGG ATCGATCGCCTCTCCGAATGGATGGGTAAATTCGGTTATGGTCATTACACCGGTATCGAC CTGGCGGAAGAACGTTCCGGCAACATGCCTACCCGCGAATGGAAACAGAAACGCTTTAAA AAACCGTGGTATCAGGGTGACACCATTCCGGTTGGTATCGGTCAGGGTTACTGGACAGCG ACCCCAATCCAGATGAGTAAGGCACTGATGATCCTGATTAATGACGGTATCGTGAAGGTT CCTCATTTGCTGATGAGCACCGCCGAAGACGGCAAACAGGTGCCATGGGTACAGCCGCAT GAACCGCCCGTCGGCGATATTCATTCCGGTTACTGGGAGCTGGCGAAAGACGGTATGTAC GGTGTTGCTAACCGCCCTAACGGTACGGCGCATAAATACTTTGCTAGCGCACCGTACAAA ATTGCGGCGAAATCCGGTACCGCTCAGGTCTTCGGTCTGAAAGCGAACGAAACCTATAAT GCGCACAAAATTGCCGAGCGTTTACGTGACCACAAACTGATGACCGCCTTTGCGCCATAC AACAATCCGCAAGTGGCTGTCGCCATGATTCTGGAGAACGGTGGTGCGGGTCCGGCGGTT GGTACACTGATGCGCCAGATCCTCGACCACATTATGCTGGGTGATAACAACACCGATCTG CCTGCGGAAAATCCAGCGGTTGCCGCAGCGGAGGACCATTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0AD65 UniProtKB Entry Name PBP2_ECOLI GenBank Protein ID 42314 GenBank Gene ID X04516 - General References
- Asoh S, Matsuzawa H, Ishino F, Strominger JL, Matsuhashi M, Ohta T: 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 Oct 15;160(2):231-8. [Article]
- Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: 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 Jun 30;3(3):137-55. [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]
- Takasuga A, Adachi H, Ishino F, Matsuhashi M, Ohta T, Matsuzawa H: Identification of the penicillin-binding active site of penicillin-binding protein 2 of Escherichia coli. J Biochem. 1988 Nov;104(5):822-6. [Article]
- Matsuzawa H, Asoh S, Kunai K, Muraiso K, Takasuga A, Ohta T: 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 Jan;171(1):558-60. [Article]
- Spratt BG: Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc Natl Acad Sci U S A. 1975 Aug;72(8):2999-3003. [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 DB01327 Cefazolin approved yes inhibitor Details DB01163 Amdinocillin investigational, withdrawn yes inhibitor Details DB01328 Cefonicid approved, investigational yes inhibitor Details DB01413 Cefepime approved, investigational yes inhibitor Details DB01415 Ceftibuten approved, investigational yes inhibitor Details DB00948 Mezlocillin approved, investigational unknown inhibitor Details DB00438 Ceftazidime approved yes inhibitor Details DB00303 Ertapenem approved, investigational yes inhibitor Details DB06211 Doripenem approved, investigational yes antagonistinhibitor Details DB09050 Ceftolozane 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