Beta-lactamase (P00811)

Identification
Name:Beta-lactamase
Synonyms:
  • Cephalosporinase
Gene Name:ampC
Enzyme Class:
Biological Properties
General Function:Involved in beta-lactamase activity
Specific Function:This protein is a serine beta-lactamase with a substrate specificity for cephalosporins
Cellular Location:Periplasm
SMPDB Pathways:Not Available
KEGG Pathways:
  • Penicillin and cephalosporin biosynthesis ec00311
  • beta-Lactam resistance ec00312
KEGG Reactions:
1.0Penicillin+1.0Thumb ↔ 1.0Penicilloic acid
1.0Penicillin + 1.0Water ↔ 1.0Penicilloic acid
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Substituted beta-amino acid
1.0beta-Lactam + 1.0Water ↔ 1.0Substituted beta-amino acid
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0a β-lactam → 1.0a substituted β-amino acid
1.0Water + 1.0a β-lactam → 1.0a substituted β-amino acid
ReactionCard
Complex Reactions:
1.0A beta-lactam+1.0Thumb → 1.0a substituted beta-amino acid
1.0A beta-lactam + 1.0Water → 1.0a substituted beta-amino acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
outer membrane-bounded periplasmic space
periplasmic space
Function
beta-lactamase activity
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
Process
antibiotic catabolic process
antibiotic metabolic process
cellular metabolic process
drug metabolic process
metabolic process
Gene Properties
Blattner:b4150
Gene OrientationCounterclockwise
Centisome Percentage:94.31
Left Sequence End4375834
Right Sequence End4376967
Gene Sequence:
>1134 bp
ATGTCATCACTGAATATTAAACAGGGAAGTGACGCTCATTTTCCCGATTATCCTCTGGCG
TCGCCCAGTAATAATGAAATTGATTTACTTAATCTAATCTCAGTTTTATGGCGGGCCAAA
AAAACGGTCATGGCGGTCGTTTTTGCGTTTGCCTGCGCAGGCTTGCTGATCTCTTTCATC
CTGCCGCAAAAATGGACCAGCGCGGCGGTTGTCACGCCTCCAGAACCTGTTCAGTGGCAA
GAGTTGGAGAAATCATTCACTAAGCTTCGTGTGCTGGATCTGGATATCAAAATTGATCGT
ACAGAAGCATTTAACCTGTTTATCAAGAAGTTTCAGTCGGTTAGCTTGCTGGAAGAGTAC
CTGCGTTCATCACCTTATGTGATGGACCAATTAAAAGAGGCGAAAATCGACGAACTGGAT
TTGCATCGCGCAATTGTCGCATTGAGCGAAAAAATGAAAGCGGTTGATGACAATGCCAGT
AAGAAAAAAGATGAACCGTCACTGTATACCTCCTGGACGCTAAGTTTTACCGCGCCAACC
AGTGAAGAGGCGCAGACCGTTTTGAGCGGGTATATCGATTATATCTCTACGTTGGTGGTG
AAAGAGTCGCTAGAAAACGTCCGTAATAAACTGGAGATCAAAACCCAGTTTGAAAAAGAA
AAACTGGCTCAGGATCGCATTAAAACGAAAAATCAACTTGATGCAAACATTCAGCGCCTC
AATTATTCACTCGACATTGCCAACGCGGCAGGAATTAAAAAGCCCGTTTACAGTAATGGT
CAGGCCGTTAAAGATGACCCCGATTTTTCTATTTCTCTCGGTGCAGACGGTATTGAACGC
AAACTGGAAATAGAAAAAGCGGTCACTGACGTTGCGGAACTGAACGGTGAATTACGTAAT
CGGCAGTATCTTGTCGAGCAATTAACAAAAGCACATGTCAACGATGTGAATTTTACGCCG
TTTAAATATCAGTTAAGCCCGTCATTGCCAGTGAAAAAAGACGGTCCGGGTAAGGCGATT
ATTGTGATCCTTTCCGCGTTGATCGGCGGGATGGTGGCTTGTGGTGGCGTGCTGTTGCGC
TATGCGATGGCATCCAGAAAACAGGATGCCATGATGGCAGACCACTTAGTTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:377
Protein Molecular Weight:41555
Protein Theoretical pI:9
PDB File:1XGJ
Signaling Regions:
  • 1-19
Transmembrane Regions:
  • None
Protein Sequence:
>Beta-lactamase
MFKTTLCALLITASCSTFAAPQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWG
YADIAKKQPVTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNGI
TLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANSSIGLFGALAVK
PSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGYREGKAVHVSPGALDAEAYGVK
STIEDMARWVQSNLKPLDINEKTLQQGIQLAQSRYWQTGDMYQGLGWEMLDWPVNPDSII
NGSDNKIALAARPVKAITPPTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNY
PNPARVDAAWQILNALQ
References
External Links:
ResourceLink
Uniprot ID:P00811
Uniprot Name:AMPC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674708
PDB ID:1XGJ
Ecogene ID:EG10040
Ecocyc:EG10040
ColiBase:b4150
Kegg Gene:b4150
EchoBASE ID:EB0038
CCDB:AMPC_ECOLI
BacMap:16131975
General Reference:
  • Beadle, B. M., Shoichet, B. K. (2002). "Structural bases of stability-function tradeoffs in enzymes." J Mol Biol 321:285-296. Pubmed: 12144785
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • Grundstrom, T., Jaurin, B. (1982). "Overlap between ampC and frd operons on the Escherichia coli chromosome." Proc Natl Acad Sci U S A 79:1111-1115. Pubmed: 7041115
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Jaurin, B., Grundstrom, T. (1981). "ampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type." Proc Natl Acad Sci U S A 78:4897-4901. Pubmed: 6795623
  • Morandi, F., Caselli, E., Morandi, S., Focia, P. J., Blazquez, J., Shoichet, B. K., Prati, F. (2003). "Nanomolar inhibitors of AmpC beta-lactamase." J Am Chem Soc 125:685-695. Pubmed: 12526668
  • Powers, R. A., Blazquez, J., Weston, G. S., Morosini, M. I., Baquero, F., Shoichet, B. K. (1999). "The complexed structure and antimicrobial activity of a non-beta-lactam inhibitor of AmpC beta-lactamase." Protein Sci 8:2330-2337. Pubmed: 10595535
  • Powers, R. A., Caselli, E., Focia, P. J., Prati, F., Shoichet, B. K. (2001). "Structures of ceftazidime and its transition-state analogue in complex with AmpC beta-lactamase: implications for resistance mutations and inhibitor design." Biochemistry 40:9207-9214. Pubmed: 11478888
  • Usher, K. C., Blaszczak, L. C., Weston, G. S., Shoichet, B. K., Remington, S. J. (1998). "Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design." Biochemistry 37:16082-16092. Pubmed: 9819201