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
Functions
penicillin binding / peptidoglycan glycosyltransferase activity / serine-type D-Ala-D-Ala carboxypeptidase activity
Processes
cell wall organization / peptidoglycan biosynthetic process / proteolysis / regulation of cell shape / response to antibiotic
Components
integral 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
ResourceLink
UniProtKB IDP02918
UniProtKB Entry NamePBPA_ECOLI
GenBank Protein ID581194
GenBank Gene IDX02164
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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 IDNameDrug groupPharmacological action?ActionsDetails
DB01598ImipenemapprovedyesinhibitorDetails
DB01329Cefoperazoneapproved, investigationalyesinhibitorDetails
DB01332Ceftizoximeapproved, withdrawnyesinhibitorDetails
DB01333CefradineapprovedyesinhibitorDetails
DB01327CefazolinapprovedyesinhibitorDetails
DB01331CefoxitinapprovedyesinhibitorDetails
DB01328Cefonicidapproved, investigationalyesinhibitorDetails
DB01415Ceftibutenapproved, investigationalyesinhibitorDetails
DB00430CefpiramideapprovedyesinhibitorDetails
DB00438CeftazidimeapprovedyesinhibitorDetails
DB00274Cefmetazoleapproved, investigationalyesinhibitorDetails
DB00303Ertapenemapproved, investigationalyesinhibitorDetails
DB01414Cefacetrileexperimental, vet_approvedyesinhibitorDetails
DB04570Latamoxefapproved, investigationalunknowninhibitorDetails
DB06211Doripenemapproved, investigationalyesantagonistinhibitorDetails
DB00578Carbenicillinapproved, investigationalyesinhibitorDetails
DB09319Carindacillinapproved, investigationalyesinhibitorDetails
DB09050Ceftolozaneapproved, investigationalunknownDetails
DB01602Bacampicillinapproved, investigationalyesinhibitorDetails
DB01000CyclacillinapprovedyesinhibitorDetails