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
Functions
beta-lactamase activity
Processes
antibiotic catabolic process / response to antibiotic
Components
outer 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
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
ResourceLink
UniProtKB IDP00811
UniProtKB Entry NameAMPC_ECOLI
GenBank Protein ID145267
GenBank Gene IDJ01611
General References
  1. 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]
  2. 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]
  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. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. Beadle BM, Shoichet BK: Structural bases of stability-function tradeoffs in enzymes. J Mol Biol. 2002 Aug 9;321(2):285-96. [Article]
  11. 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 IDNameDrug groupPharmacological action?ActionsDetails
DB01896M-Aminophenylboronic AcidexperimentalunknownDetails
DB02094N-2-Thiophen-2-Yl-Acetamide Boronic AcidexperimentalunknownDetails
DB02247Hydrolyzed CephalothinexperimentalunknownDetails
DB025034-(Carboxyvin-2-Yl)Phenylboronic AcidexperimentalunknownDetails
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 acidexperimentalunknownDetails
DB026274,4'-Biphenyldiboronic AcidexperimentalunknownDetails
DB02772Sucroseapproved, experimental, investigationalunknownDetails
DB027973-Nitrophenylboronic AcidexperimentalunknownDetails
DB028583-(4-Benzenesulfonyl-Thiophene-2-Sulfonylamino)-Phenylboronic AcidexperimentalunknownDetails
DB00456Cefalotinapproved, investigational, vet_approvedyespotentiatorDetails
DB031404-Carboxyphenylboronic AcidexperimentalunknownDetails
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 acidexperimentalunknownDetails
DB03530Acylated ceftazidimeexperimentalunknownDetails
DB03658(2R,4S)-2-[(1R)-1-{[(2R)-2-Amino-2-(4-hydroxyphenyl)acetyl]amino}-2-oxoethyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acidexperimentalunknownDetails
DB042937-(2-Amino-2-Phenyl-Acetylamino)-3-Chloro-8-Oxo-1-Aza-Bicyclo[4.2.0]Oct-2-Ene-2-Carboxylic AcidexperimentalunknownDetails
DB04360Benzo[B]Thiophene-2-Boronic AcidexperimentalunknownDetails
DB069222-[(1R)-1-carboxy-2-naphthalen-1-ylethyl]-1,3-dioxo-2,3-dihydro-1H-isoindole-5-carboxylic acidexperimentalunknownDetails
DB07057(3S)-1-(2-hydroxyphenyl)-5-oxopyrrolidine-3-carboxylic acidexperimentalunknownDetails
DB071144-[(METHYLSULFONYL)AMINO]BENZOIC ACIDexperimentalunknownDetails
DB075414-(dihydroxyboranyl)-2-({[4-(phenylsulfonyl)thiophen-2-yl]sulfonyl}amino)benzoic acidexperimentalunknownDetails
DB04035Ceftazidime BATSIexperimentalunknownDetails
DB076632-[(1R)-1-CARBOXY-2-(4-HYDROXYPHENYL)ETHYL]-1,3-DIOXOISOINDOLINE-5-CARBOXYLIC ACIDexperimentalunknownDetails
DB078032-phenyl-1H-imidazole-4-carboxylic acidexperimentalunknownDetails
DB07823(2S)-2-[(3aR,4R,7S,7aS)-1,3-dioxooctahydro-2H-4,7-methanoisoindol-2-yl]propanoic acidexperimentalunknownDetails
DB078244-ethyl-5-methyl-2-(1H-tetrazol-5-yl)-1,2-dihydro-3H-pyrazol-3-oneexperimentalunknownDetails
DB07825(3S)-1-(4-acetylphenyl)-5-oxopyrrolidine-3-carboxylic acidexperimentalunknownDetails
DB07850(1R,2S)-2-(5-thioxo-4,5-dihydro-1H-1,2,4-triazol-3-yl)cyclohexanecarboxylic acidexperimentalunknownDetails
DB079273-[(4-Carboxy-2-hydroxyphenyl)sulfamoyl]-2-thiophenecarboxylic acidexperimentalunknownDetails
DB083063-[(3-Nitrophenyl)sulfamoyl]-2-thiophenecarboxylic acidexperimentalunknownDetails
DB083362-Methyl-2-propanyl [(1R)-2-methyl-1-(1,3,4-oxadiazol-2-yl)propyl]carbamateexperimentalunknownDetails
DB083372-Methyl-2-propanyl [(1S)-2-methyl-1-(1,3,4-oxadiazol-2-yl)propyl]carbamateexperimentalunknownDetails
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 acidexperimentalunknownDetails
DB085513-{(R)-(Dihydroxyboryl)[(2-thienylacetyl)amino]methyl}benzoic acidexperimentalunknownDetails
DB08552(1R)-1-(2-thienylacetylamino)-1-phenylmethylboronic acidexperimentalunknownDetails
DB085733-[(4-CHLOROANILINO)SULFONYL]THIOPHENE-2-CARBOXYLIC ACIDexperimentalunknownDetails
DB086232-[CARBOXY-(2-THIOPHEN-2-YL-ACETYLAMINO)-METHYL]-5-METHYLENE-5,6-DIHYDRO-2H-[1,3]THIAZINE-4-CARBOXYLIC ACIDexperimentalunknownDetails
DB087312-[(1R)-2-carboxy-1-(naphthalen-1-ylmethyl)ethyl]-1,3-dioxo-2,3-dihydro-1H-isoindole-5-carboxylic acidexperimentalunknownDetails