Beta-lactamase
Details
- Name
- Beta-lactamase
- Synonyms
- 3.5.2.6
- ampA
- Cephalosporinase
- Gene Name
- ampC
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0010950|Beta-lactamase MFKTTLCALLITASCSTFAAPQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWG YADIAKKQPVTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNGI TLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANSSIGLFGALAVK PSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGYREGKAVHVSPGALDAEAYGVK STIEDMARWVQSNLKPLDINEKTLQQGIQLAQSRYWQTGDMYQGLGWEMLDWPVNPDSII NGSDNKIALAARPVKAITPPTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNY PNPARVDAAWQILNALQ
- Number of residues
- 377
- Molecular Weight
- 41555.3
- Theoretical pI
- 9.07
- GO Classification
- Functionsbeta-lactamase activityProcessesantibiotic catabolic process / response to antibioticComponentsouter membrane-bounded periplasmic space
- General Function
- Beta-lactamase activity
- Specific Function
- This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
- Pfam Domain Function
- Beta-lactamase (PF00144)
- Transmembrane Regions
- Not Available
- Cellular Location
- Periplasm
- Gene sequence
>lcl|BSEQ0010951|Beta-lactamase (ampC) ATGTTCAAAACGACGCTCTGCGCCTTATTAATTACCGCCTCTTGCTCCACATTTGCTGCC CCTCAACAAATCAACGATATTGTGCATCGCACAATTACCCCGCTTATAGAGCAACAAAAG ATCCCGGGTATGGCGGTGGCGGTAATTTATCAGGGTAAACCTTATTACTTTACCTGGGGC TATGCGGACATCGCCAAAAAGCAGCCCGTCACACAGCAAACGTTGTTTGAGTTAGGTTCG GTCAGCAAAACATTTACTGGCGTGCTTGGTGGCGACGCTATTGCTCGAGGGGAAATCAAG TTAAGCGATCCCACAACAAAATACTGGCCTGAACTTACCGCTAAACAGTGGAATGGGATC ACACTATTACATCTCGCAACCTACACTGCTGGCGGCCTGCCATTGCAGGTGCCGGATGAG GTGAAATCCTCAAGCGACTTGCTGCGCTTCTATCAAAACTGGCAGCCTGCATGGGCTCCA GGAACACAACGTCTGTATGCCAACTCCAGTATCGGTTTGTTCGGCGCACTGGCTGTGAAG CCGTCTGGTTTGAGTTTTGAGCAGGCGATGCAAACTCGTGTCTTCCAGCCACTCAAACTC AACCATACGTGGATTAATGTACCGCCCGCAGAAGAAAAGAATTACGCCTGGGGATATCGC GAAGGTAAGGCAGTGCATGTTTCGCCTGGGGCGTTAGATGCTGAAGCTTATGGTGTGAAG TCGACCATTGAAGATATGGCCCGCTGGGTGCAAAGCAATTTAAAACCCCTTGATATCAAT GAGAAAACGCTTCAACAAGGGATACAACTGGCACAATCTCGCTACTGGCAAACCGGCGAT ATGTATCAGGGCCTGGGCTGGGAAATGCTGGACTGGCCGGTAAATCCTGACAGCATCATT AACGGCAGTGACAATAAAATTGCACTGGCAGCACGCCCCGTAAAAGCGATTACGCCCCCA ACTCCTGCAGTACGCGCATCATGGGTACATAAAACAGGGGCGACCGGCGGATTTGGTAGC TATGTCGCGTTTATTCCAGAAAAAGAGCTGGGTATCGTGATGCTGGCAAACAAAAACTAT CCCAATCCAGCGAGAGTCGACGCCGCCTGGCAGATTCTTAACGCTCTACAGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P00811 UniProtKB Entry Name AMPC_ECOLI GenBank Protein ID 145267 GenBank Gene ID J01611 - General References
- Jaurin B, Grundstrom T: 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. 1981 Aug;78(8):4897-901. [Article]
- Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [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]
- Grundstrom T, Jaurin B: Overlap between ampC and frd operons on the Escherichia coli chromosome. Proc Natl Acad Sci U S A. 1982 Feb;79(4):1111-5. [Article]
- VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
- Usher KC, Blaszczak LC, Weston GS, Shoichet BK, Remington SJ: 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. 1998 Nov 17;37(46):16082-92. [Article]
- Powers RA, Blazquez J, Weston GS, Morosini MI, Baquero F, Shoichet BK: The complexed structure and antimicrobial activity of a non-beta-lactam inhibitor of AmpC beta-lactamase. Protein Sci. 1999 Nov;8(11):2330-7. [Article]
- Powers RA, Caselli E, Focia PJ, Prati F, Shoichet BK: Structures of ceftazidime and its transition-state analogue in complex with AmpC beta-lactamase: implications for resistance mutations and inhibitor design. Biochemistry. 2001 Aug 7;40(31):9207-14. [Article]
- Beadle BM, Shoichet BK: Structural bases of stability-function tradeoffs in enzymes. J Mol Biol. 2002 Aug 9;321(2):285-96. [Article]
- Morandi F, Caselli E, Morandi S, Focia PJ, Blazquez J, Shoichet BK, Prati F: Nanomolar inhibitors of AmpC beta-lactamase. J Am Chem Soc. 2003 Jan 22;125(3):685-95. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01896 M-Aminophenylboronic Acid experimental unknown Details DB02094 N-2-Thiophen-2-Yl-Acetamide Boronic Acid experimental unknown Details DB02247 Hydrolyzed Cephalothin experimental unknown Details DB02503 4-(Carboxyvin-2-Yl)Phenylboronic Acid experimental unknown Details DB02588 (2R)-2-[(1R)-1-{[(2S)-2-Carboxy-2-(4-hydroxyphenyl)acetyl]amino}-1-methoxy-2-oxoethyl]-5-methylene-5,6-dihydro-2H-1,3-oxazine-4-carboxylic acid experimental unknown Details DB02627 4,4'-Biphenyldiboronic Acid experimental unknown Details DB02772 Sucrose approved, experimental, investigational unknown Details DB02797 3-Nitrophenylboronic Acid experimental unknown Details DB02858 3-(4-Benzenesulfonyl-Thiophene-2-Sulfonylamino)-Phenylboronic Acid experimental unknown Details DB00456 Cefalotin approved, investigational, vet_approved yes potentiator Details DB03140 4-Carboxyphenylboronic Acid experimental unknown Details DB03437 (2R,4S)-2-[(1R)-1-{[(2Z)-2-(2-Amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino}-2-oxoethyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid experimental unknown Details DB03530 Acylated ceftazidime experimental unknown Details DB03658 (2R,4S)-2-[(1R)-1-{[(2R)-2-Amino-2-(4-hydroxyphenyl)acetyl]amino}-2-oxoethyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid experimental unknown Details DB04293 7-(2-Amino-2-Phenyl-Acetylamino)-3-Chloro-8-Oxo-1-Aza-Bicyclo[4.2.0]Oct-2-Ene-2-Carboxylic Acid experimental unknown Details DB04360 Benzo[B]Thiophene-2-Boronic Acid experimental unknown Details DB06922 2-[(1R)-1-carboxy-2-naphthalen-1-ylethyl]-1,3-dioxo-2,3-dihydro-1H-isoindole-5-carboxylic acid experimental unknown Details DB07057 (3S)-1-(2-hydroxyphenyl)-5-oxopyrrolidine-3-carboxylic acid experimental unknown Details DB07114 4-[(METHYLSULFONYL)AMINO]BENZOIC ACID experimental unknown Details DB07541 4-(dihydroxyboranyl)-2-({[4-(phenylsulfonyl)thiophen-2-yl]sulfonyl}amino)benzoic acid experimental unknown Details DB04035 Ceftazidime BATSI experimental unknown Details DB07663 2-[(1R)-1-CARBOXY-2-(4-HYDROXYPHENYL)ETHYL]-1,3-DIOXOISOINDOLINE-5-CARBOXYLIC ACID experimental unknown Details DB07803 2-phenyl-1H-imidazole-4-carboxylic acid experimental unknown Details DB07823 (2S)-2-[(3aR,4R,7S,7aS)-1,3-dioxooctahydro-2H-4,7-methanoisoindol-2-yl]propanoic acid experimental unknown Details DB07824 4-ethyl-5-methyl-2-(1H-tetrazol-5-yl)-1,2-dihydro-3H-pyrazol-3-one experimental unknown Details DB07825 (3S)-1-(4-acetylphenyl)-5-oxopyrrolidine-3-carboxylic acid experimental unknown Details DB07850 (1R,2S)-2-(5-thioxo-4,5-dihydro-1H-1,2,4-triazol-3-yl)cyclohexanecarboxylic acid experimental unknown Details DB07927 3-[(4-Carboxy-2-hydroxyphenyl)sulfamoyl]-2-thiophenecarboxylic acid experimental unknown Details DB08306 3-[(3-Nitrophenyl)sulfamoyl]-2-thiophenecarboxylic acid experimental unknown Details DB08336 2-Methyl-2-propanyl [(1R)-2-methyl-1-(1,3,4-oxadiazol-2-yl)propyl]carbamate experimental unknown Details DB08337 2-Methyl-2-propanyl [(1S)-2-methyl-1-(1,3,4-oxadiazol-2-yl)propyl]carbamate experimental unknown Details DB08375 (2R)-2-[(1R)-1-[[(2Z)-2-(2-Amino-1,3-thiazol-4-yl)-2-methoxyiminoacetyl]amino]-2-oxoethyl]-5-methylidene-2H-1,3-thiazine-4-carboxylic acid experimental unknown Details DB08551 3-{(R)-(Dihydroxyboryl)[(2-thienylacetyl)amino]methyl}benzoic acid experimental unknown Details DB08552 (1R)-1-(2-thienylacetylamino)-1-phenylmethylboronic acid experimental unknown Details DB08573 3-[(4-CHLOROANILINO)SULFONYL]THIOPHENE-2-CARBOXYLIC ACID experimental unknown Details DB08623 2-[CARBOXY-(2-THIOPHEN-2-YL-ACETYLAMINO)-METHYL]-5-METHYLENE-5,6-DIHYDRO-2H-[1,3]THIAZINE-4-CARBOXYLIC ACID experimental unknown Details DB08731 2-[(1R)-2-carboxy-1-(naphthalen-1-ylmethyl)ethyl]-1,3-dioxo-2,3-dihydro-1H-isoindole-5-carboxylic acid experimental unknown Details