Beta-lactamase
Details
- Name
- Beta-lactamase
- Synonyms
- 3.5.2.6
- ampA
- Cephalosporinase
- Gene Name
- ampC
- UniProtKB Entry
- P00811Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- 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
- Class C beta-lactamase which confers resistance to penicillins and cephalosporins (PubMed:12323371, PubMed:17956081, PubMed:33199391, PubMed:6998377). Has benzylpenicillin- and cephaloridine-hydrolyzing activity (PubMed:3264154, PubMed:3264155, PubMed:6998377). Has weak cefuroxime, cefotaxime, cefoxitin and oxacillin-hydrolyzing activities (PubMed:3264154, PubMed:3264155).
- Specific Function
- beta-lactamase activity
- Pfam Domain Function
- Beta-lactamase (PF00144)
- Signal Regions
- 1-19
- 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 PDB ID(s) 1C3B, 1FCM, 1FCN, 1FCO, 1FSW, 1FSY, 1GA9, 1I5Q, 1IEL, 1IEM, 1KDS, 1KDW, 1KE0, 1KE3, 1KE4, 1KVL, 1KVM, 1L0D, 1L0E, 1L0F, 1L0G, 1L2S, 1LL5, 1LL9, 1LLB, 1MXO, 1MY8, 1O07, 1PI4, 1PI5, 1XGI, 1XGJ, 2BLS, 2FFY, 2HDQ, 2HDR, 2HDS, 2HDU, 2I72, 2P9V, 2PU2, 2PU4, 2R9W, 2R9X, 2RCX, 3BLS, 3BM6, 3FKV, 3FKW, 3GQZ, 3GR2, 3GRJ, 3GSG, 3GTC, 3GV9, 3GVB, 3IWI, 3IWO, 3IWQ, 3IXB, 3IXD, 3IXG, 3IXH, 3O86, 3O87, 3O88, 4E3I, 4E3J, 4E3K, 4E3L, 4E3M, 4E3N, 4E3O, 4JXG, 4JXS, 4JXV, 4JXW, 4KEN, 4KG2, 4KG5, 4KG6, 4KZ3, 4KZ4, 4KZ5, 4KZ6, 4KZ7, 4KZ8, 4KZ9, 4KZA, 4KZB, 4LV0, 4LV1, 4LV2, 4LV3, 4OKP, 4OLD, 4OLG KEGG ID ecj:JW4111 NCBI Gene ID 948669 - 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]
Associated Data
- Bio-Entities
Bio-Entity Type Beta-lactamase (Escherichia coli (strain K12)) protein primary- Drug Relations