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
Functions
drug binding / penicillin binding / peptidoglycan L,D-transpeptidase activity / serine-type D-Ala-D-Ala carboxypeptidase activity
Processes
cell wall organization / peptidoglycan biosynthetic process / proteolysis / regulation of cell shape / response to antibiotic / response to drug
Components
integral 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
ResourceLink
UniProtKB IDP0AD65
UniProtKB Entry NamePBP2_ECOLI
GenBank Protein ID42314
GenBank Gene IDX04516
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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 IDNameDrug groupPharmacological action?ActionsDetails
DB01598ImipenemapprovedyesinhibitorDetails
DB01329Cefoperazoneapproved, investigationalyesinhibitorDetails
DB01327CefazolinapprovedyesinhibitorDetails
DB01163Amdinocillininvestigational, withdrawnyesinhibitorDetails
DB01328Cefonicidapproved, investigationalyesinhibitorDetails
DB01413Cefepimeapproved, investigationalyesinhibitorDetails
DB01415Ceftibutenapproved, investigationalyesinhibitorDetails
DB00948Mezlocillinapproved, investigationalunknowninhibitorDetails
DB00438CeftazidimeapprovedyesinhibitorDetails
DB00303Ertapenemapproved, investigationalyesinhibitorDetails
DB06211Doripenemapproved, investigationalyesantagonistinhibitorDetails
DB09050Ceftolozaneapproved, investigationalyesinhibitorDetails
DB00671Cefiximeapproved, investigationalunknownDetails
DB00578Carbenicillinapproved, investigationalyesinhibitorDetails
DB09319Carindacillinapproved, investigationalyesinhibitorDetails
DB09050Ceftolozaneapproved, investigationalunknownDetails
DB01602Bacampicillinapproved, investigationalyesinhibitorDetails
DB01000CyclacillinapprovedyesinhibitorDetails
DB00671Cefiximeapproved, investigationalyesbinderDetails