ID AMPC_ECOLI Reviewed; 377 AA. AC P00811; Q2M6F2; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 24-JAN-2024, entry version 194. DE RecName: Full=Beta-lactamase; DE EC=3.5.2.6; DE AltName: Full=Cephalosporinase; DE Flags: Precursor; GN Name=ampC; Synonyms=ampA; OrderedLocusNames=b4150, JW4111; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 20-31. RC STRAIN=K12; RX PubMed=6795623; DOI=10.1073/pnas.78.8.4897; RA Jaurin B., Grundstroem T.; RT "ampC cephalosporinase of Escherichia coli K-12 has a different RT evolutionary origin from that of beta-lactamases of the penicillinase RT type."; RL Proc. Natl. Acad. Sci. U.S.A. 78:4897-4901(1981). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=7610040; DOI=10.1093/nar/23.12.2105; RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.; RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region RT from 92.8 through 100 minutes."; RL Nucleic Acids Res. 23:2105-2119(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29. RX PubMed=7041115; DOI=10.1073/pnas.79.4.1111; RA Grundstroem T., Jaurin B.; RT "Overlap between ampC and frd operons on the Escherichia coli chromosome."; RL Proc. Natl. Acad. Sci. U.S.A. 79:1111-1115(1982). RN [6] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=9819201; DOI=10.1021/bi981210f; RA Usher K.C., Blaszczak L.C., Weston G.S., Shoichet B.K., Remington S.J.; RT "Three-dimensional structure of AmpC beta-lactamase from Escherichia coli RT bound to a transition-state analogue: possible implications for the RT oxyanion hypothesis and for inhibitor design."; RL Biochemistry 37:16082-16092(1998). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS). RX PubMed=10595535; DOI=10.1110/ps.8.11.2330; RA Powers R.A., Blazquez J., Weston G.S., Morosini M.I., Baquero F., RA Shoichet B.K.; RT "The complexed structure and antimicrobial activity of a non-beta-lactam RT inhibitor of AmpC beta-lactamase."; RL Protein Sci. 8:2330-2337(1999). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGUE. RX PubMed=11478888; DOI=10.1021/bi0109358; RA Powers R.A., Caselli E., Focia P.J., Prati F., Shoichet B.K.; RT "Structures of ceftazidime and its transition-state analogue in complex RT with AmpC beta-lactamase: implications for resistance mutations and RT inhibitor design."; RL Biochemistry 40:9207-9214(2001). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS), AND MUTAGENESIS OF SER-80; LYS-83; RP TYR-166; ASN-168 AND LYS-331. RX PubMed=12144785; DOI=10.1016/s0022-2836(02)00599-5; RA Beadle B.M., Shoichet B.K.; RT "Structural bases of stability-function tradeoffs in enzymes."; RL J. Mol. Biol. 321:285-296(2002). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS). RX PubMed=12526668; DOI=10.1021/ja0288338; RA Morandi F., Caselli E., Morandi S., Focia P.J., Blazquez J., Shoichet B.K., RA Prati F.; RT "Nanomolar inhibitors of AmpC beta-lactamase."; RL J. Am. Chem. Soc. 125:685-695(2003). CC -!- FUNCTION: This protein is a serine beta-lactamase with a substrate CC specificity for cephalosporins. CC -!- CATALYTIC ACTIVITY: CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid; CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, CC ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10102}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11478888}. CC -!- SUBCELLULAR LOCATION: Periplasm. CC -!- SIMILARITY: Belongs to the class-C beta-lactamase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J01611; AAA23441.1; -; Genomic_DNA. DR EMBL; U14003; AAA97049.1; -; Genomic_DNA. DR EMBL; U00096; AAC77110.1; -; Genomic_DNA. DR EMBL; AP009048; BAE78154.1; -; Genomic_DNA. DR EMBL; V00277; CAA23537.1; -; Genomic_DNA. DR PIR; A01007; QKEC. DR RefSeq; NP_418574.1; NC_000913.3. DR RefSeq; WP_001336292.1; NZ_LN832404.1. DR PDB; 1C3B; X-ray; 2.25 A; A/B=20-377. DR PDB; 1FCM; X-ray; 2.46 A; A/B=20-377. DR PDB; 1FCN; X-ray; 2.35 A; A/B=20-377. DR PDB; 1FCO; X-ray; 2.20 A; A/B=20-377. DR PDB; 1FSW; X-ray; 1.90 A; A/B=20-376. DR PDB; 1FSY; X-ray; 1.75 A; A/B=20-376. DR PDB; 1GA9; X-ray; 2.10 A; A/B=20-377. DR PDB; 1I5Q; X-ray; 1.83 A; A/B=20-377. DR PDB; 1IEL; X-ray; 2.00 A; A/B=20-377. DR PDB; 1IEM; X-ray; 2.30 A; A/B=20-377. DR PDB; 1KDS; X-ray; 2.15 A; A/B=20-377. DR PDB; 1KDW; X-ray; 2.28 A; A/B=20-377. DR PDB; 1KE0; X-ray; 2.30 A; A/B=20-377. DR PDB; 1KE3; X-ray; 2.15 A; A/B=20-377. DR PDB; 1KE4; X-ray; 1.72 A; A/B=20-377. DR PDB; 1KVL; X-ray; 1.53 A; A/B=20-377. DR PDB; 1KVM; X-ray; 2.06 A; A/B=20-377. DR PDB; 1L0D; X-ray; 1.53 A; A/B=20-377. DR PDB; 1L0E; X-ray; 1.90 A; A/B=20-377. DR PDB; 1L0F; X-ray; 1.66 A; A/B=20-377. DR PDB; 1L0G; X-ray; 1.50 A; A/B=20-377. DR PDB; 1L2S; X-ray; 1.94 A; A/B=20-377. DR PDB; 1LL5; X-ray; 1.80 A; A/B=20-377. DR PDB; 1LL9; X-ray; 1.87 A; A/B=20-377. DR PDB; 1LLB; X-ray; 1.72 A; A/B=20-377. DR PDB; 1MXO; X-ray; 1.83 A; A/B=20-377. DR PDB; 1MY8; X-ray; 1.72 A; A/B=20-377. DR PDB; 1O07; X-ray; 1.71 A; A/B=20-377. DR PDB; 1PI4; X-ray; 1.39 A; A/B=20-377. DR PDB; 1PI5; X-ray; 1.49 A; A/B=20-377. DR PDB; 1XGI; X-ray; 1.96 A; A/B=20-377. DR PDB; 1XGJ; X-ray; 1.97 A; A/B=20-377. DR PDB; 2BLS; X-ray; 2.00 A; A/B=20-377. DR PDB; 2FFY; X-ray; 1.07 A; A/B=20-377. DR PDB; 2HDQ; X-ray; 2.10 A; A/B=20-377. DR PDB; 2HDR; X-ray; 2.20 A; A/B=20-377. DR PDB; 2HDS; X-ray; 1.16 A; A/B=20-377. DR PDB; 2HDU; X-ray; 1.49 A; A/B=20-377. DR PDB; 2I72; X-ray; 2.20 A; A/B=20-377. DR PDB; 2P9V; X-ray; 1.80 A; A/B=20-377. DR PDB; 2PU2; X-ray; 1.86 A; A/B=20-377. DR PDB; 2PU4; X-ray; 2.00 A; A/B=20-377. DR PDB; 2R9W; X-ray; 1.80 A; A/B=20-377. DR PDB; 2R9X; X-ray; 1.90 A; A/B=20-377. DR PDB; 2RCX; X-ray; 2.00 A; A/B=20-377. DR PDB; 3BLS; X-ray; 2.30 A; A/B=20-377. DR PDB; 3BM6; X-ray; 2.10 A; A/B=20-377. DR PDB; 3FKV; X-ray; 1.85 A; A/B=20-377. DR PDB; 3FKW; X-ray; 1.50 A; A/B=20-377. DR PDB; 3GQZ; X-ray; 1.80 A; A/B=20-377. DR PDB; 3GR2; X-ray; 1.80 A; A/B=20-377. DR PDB; 3GRJ; X-ray; 2.49 A; A/B=20-377. DR PDB; 3GSG; X-ray; 2.10 A; A/B=20-377. DR PDB; 3GTC; X-ray; 1.90 A; A/B=20-377. DR PDB; 3GV9; X-ray; 1.80 A; A/B=20-377. DR PDB; 3GVB; X-ray; 1.80 A; A/B=20-377. DR PDB; 3IWI; X-ray; 1.64 A; A/B=20-377. DR PDB; 3IWO; X-ray; 1.90 A; A/B=20-377. DR PDB; 3IWQ; X-ray; 1.84 A; A/B=20-377. DR PDB; 3IXB; X-ray; 1.63 A; A/B=20-377. DR PDB; 3IXD; X-ray; 2.64 A; A/B=20-377. DR PDB; 3IXG; X-ray; 2.14 A; A/B=20-377. DR PDB; 3IXH; X-ray; 2.30 A; A/B=20-377. DR PDB; 3O86; X-ray; 1.60 A; A/B=20-377. DR PDB; 3O87; X-ray; 1.78 A; A/B=20-377. DR PDB; 3O88; X-ray; 1.64 A; A/B=20-377. DR PDB; 4E3I; X-ray; 1.60 A; A/B=20-377. DR PDB; 4E3J; X-ray; 1.80 A; A/B=20-377. DR PDB; 4E3K; X-ray; 1.43 A; A/B=20-377. DR PDB; 4E3L; X-ray; 1.43 A; A/B=20-377. DR PDB; 4E3M; X-ray; 1.44 A; A/B=20-377. DR PDB; 4E3N; X-ray; 1.49 A; A/B=20-377. DR PDB; 4E3O; X-ray; 1.60 A; A/B=20-377. DR PDB; 4JXG; X-ray; 1.65 A; A/B=20-377. DR PDB; 4JXS; X-ray; 1.90 A; A/B=20-377. DR PDB; 4JXV; X-ray; 1.76 A; A/B=20-377. DR PDB; 4JXW; X-ray; 2.30 A; A/B=20-377. DR PDB; 4KEN; X-ray; 1.89 A; B=20-377. DR PDB; 4KG2; X-ray; 1.89 A; A/B=20-377. DR PDB; 4KG5; X-ray; 2.11 A; A/B/C/D=20-377. DR PDB; 4KG6; X-ray; 1.75 A; A/B/C/D=20-377. DR PDB; 4KZ3; X-ray; 1.67 A; A/B=20-377. DR PDB; 4KZ4; X-ray; 1.42 A; A/B=20-377. DR PDB; 4KZ5; X-ray; 1.35 A; A/B=20-377. DR PDB; 4KZ6; X-ray; 1.68 A; A/B=20-377. DR PDB; 4KZ7; X-ray; 1.43 A; A/B=20-377. DR PDB; 4KZ8; X-ray; 2.28 A; A/B=20-377. DR PDB; 4KZ9; X-ray; 1.72 A; A/B=20-377. DR PDB; 4KZA; X-ray; 1.60 A; A/B=20-377. DR PDB; 4KZB; X-ray; 1.37 A; A/B=20-377. DR PDB; 4LV0; X-ray; 1.65 A; A/B=20-377. DR PDB; 4LV1; X-ray; 1.74 A; A/B=20-377. DR PDB; 4LV2; X-ray; 1.65 A; A/B=20-377. DR PDB; 4LV3; X-ray; 1.42 A; A/B=20-377. DR PDB; 4OKP; X-ray; 1.37 A; A/B=20-377. DR PDB; 4OLD; X-ray; 1.48 A; A/B=20-377. DR PDB; 4OLG; X-ray; 1.71 A; A/B=20-377. DR PDB; 5JOC; X-ray; 1.75 A; A/B=21-377. DR PDB; 6DPT; X-ray; 1.79 A; A/B=20-377. DR PDB; 6DPX; X-ray; 1.90 A; A/B=20-377. DR PDB; 6DPY; X-ray; 1.91 A; A/B=20-377. DR PDB; 6DPZ; X-ray; 1.50 A; A/B=20-377. DR PDB; 6T35; X-ray; 1.75 A; A=20-377. DR PDB; 6T3D; X-ray; 1.50 A; A=20-377. DR PDB; 6T5Y; X-ray; 1.30 A; A=20-377. DR PDB; 6T7L; X-ray; 1.47 A; A=20-377. DR PDB; 6TBW; X-ray; 1.51 A; A=20-377. DR PDB; 6TPM; X-ray; 1.72 A; A=20-377. DR PDB; 6WHF; X-ray; 1.40 A; A/B=19-377. DR PDB; 6X9Y; X-ray; 1.90 A; A/B=20-377. DR PDB; 6XFS; X-ray; 2.70 A; A/B/C/D=19-377. DR PDB; 6XG1; X-ray; 1.22 A; A/B=19-377. DR PDB; 6YEN; X-ray; 1.42 A; A=20-377. DR PDB; 6YEO; X-ray; 2.04 A; A/B/C/D=20-377. DR PDB; 6YPD; X-ray; 1.60 A; A=20-377. DR PDBsum; 1C3B; -. DR PDBsum; 1FCM; -. DR PDBsum; 1FCN; -. DR PDBsum; 1FCO; -. DR PDBsum; 1FSW; -. DR PDBsum; 1FSY; -. DR PDBsum; 1GA9; -. DR PDBsum; 1I5Q; -. DR PDBsum; 1IEL; -. DR PDBsum; 1IEM; -. DR PDBsum; 1KDS; -. DR PDBsum; 1KDW; -. DR PDBsum; 1KE0; -. DR PDBsum; 1KE3; -. DR PDBsum; 1KE4; -. DR PDBsum; 1KVL; -. DR PDBsum; 1KVM; -. DR PDBsum; 1L0D; -. DR PDBsum; 1L0E; -. DR PDBsum; 1L0F; -. DR PDBsum; 1L0G; -. DR PDBsum; 1L2S; -. DR PDBsum; 1LL5; -. DR PDBsum; 1LL9; -. DR PDBsum; 1LLB; -. DR PDBsum; 1MXO; -. DR PDBsum; 1MY8; -. DR PDBsum; 1O07; -. DR PDBsum; 1PI4; -. DR PDBsum; 1PI5; -. DR PDBsum; 1XGI; -. DR PDBsum; 1XGJ; -. DR PDBsum; 2BLS; -. DR PDBsum; 2FFY; -. DR PDBsum; 2HDQ; -. DR PDBsum; 2HDR; -. DR PDBsum; 2HDS; -. DR PDBsum; 2HDU; -. DR PDBsum; 2I72; -. DR PDBsum; 2P9V; -. DR PDBsum; 2PU2; -. DR PDBsum; 2PU4; -. DR PDBsum; 2R9W; -. DR PDBsum; 2R9X; -. DR PDBsum; 2RCX; -. DR PDBsum; 3BLS; -. DR PDBsum; 3BM6; -. DR PDBsum; 3FKV; -. DR PDBsum; 3FKW; -. DR PDBsum; 3GQZ; -. DR PDBsum; 3GR2; -. DR PDBsum; 3GRJ; -. DR PDBsum; 3GSG; -. DR PDBsum; 3GTC; -. DR PDBsum; 3GV9; -. DR PDBsum; 3GVB; -. DR PDBsum; 3IWI; -. DR PDBsum; 3IWO; -. DR PDBsum; 3IWQ; -. DR PDBsum; 3IXB; -. DR PDBsum; 3IXD; -. DR PDBsum; 3IXG; -. DR PDBsum; 3IXH; -. DR PDBsum; 3O86; -. DR PDBsum; 3O87; -. DR PDBsum; 3O88; -. DR PDBsum; 4E3I; -. DR PDBsum; 4E3J; -. DR PDBsum; 4E3K; -. DR PDBsum; 4E3L; -. DR PDBsum; 4E3M; -. DR PDBsum; 4E3N; -. DR PDBsum; 4E3O; -. DR PDBsum; 4JXG; -. DR PDBsum; 4JXS; -. DR PDBsum; 4JXV; -. DR PDBsum; 4JXW; -. DR PDBsum; 4KEN; -. DR PDBsum; 4KG2; -. DR PDBsum; 4KG5; -. DR PDBsum; 4KG6; -. DR PDBsum; 4KZ3; -. DR PDBsum; 4KZ4; -. DR PDBsum; 4KZ5; -. DR PDBsum; 4KZ6; -. DR PDBsum; 4KZ7; -. DR PDBsum; 4KZ8; -. DR PDBsum; 4KZ9; -. DR PDBsum; 4KZA; -. DR PDBsum; 4KZB; -. DR PDBsum; 4LV0; -. DR PDBsum; 4LV1; -. DR PDBsum; 4LV2; -. DR PDBsum; 4LV3; -. DR PDBsum; 4OKP; -. DR PDBsum; 4OLD; -. DR PDBsum; 4OLG; -. DR PDBsum; 5JOC; -. DR PDBsum; 6DPT; -. DR PDBsum; 6DPX; -. DR PDBsum; 6DPY; -. DR PDBsum; 6DPZ; -. DR PDBsum; 6T35; -. DR PDBsum; 6T3D; -. DR PDBsum; 6T5Y; -. DR PDBsum; 6T7L; -. DR PDBsum; 6TBW; -. DR PDBsum; 6TPM; -. DR PDBsum; 6WHF; -. DR PDBsum; 6X9Y; -. DR PDBsum; 6XFS; -. DR PDBsum; 6XG1; -. DR PDBsum; 6YEN; -. DR PDBsum; 6YEO; -. DR PDBsum; 6YPD; -. DR AlphaFoldDB; P00811; -. DR SMR; P00811; -. DR BioGRID; 4261277; 168. DR IntAct; P00811; 1. DR STRING; 511145.b4150; -. DR BindingDB; P00811; -. DR ChEMBL; CHEMBL2026; -. DR DrugBank; DB08552; (1R)-1-(2-thienylacetylamino)-1-phenylmethylboronic acid. DR DrugBank; DB07850; (1R,2S)-2-(5-thioxo-4,5-dihydro-1H-1,2,4-triazol-3-yl)cyclohexanecarboxylic acid. DR DrugBank; 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. DR DrugBank; 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. DR DrugBank; 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. DR DrugBank; 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. DR DrugBank; DB07823; (2S)-2-[(3aR,4R,7S,7aS)-1,3-dioxooctahydro-2H-4,7-methanoisoindol-2-yl]propanoic acid. DR DrugBank; DB07057; (3S)-1-(2-hydroxyphenyl)-5-oxopyrrolidine-3-carboxylic acid. DR DrugBank; DB07825; (3S)-1-(4-acetylphenyl)-5-oxopyrrolidine-3-carboxylic acid. DR DrugBank; DB07663; 2-[(1R)-1-CARBOXY-2-(4-HYDROXYPHENYL)ETHYL]-1,3-DIOXOISOINDOLINE-5-CARBOXYLIC ACID. DR DrugBank; DB06922; 2-[(1R)-1-carboxy-2-naphthalen-1-ylethyl]-1,3-dioxo-2,3-dihydro-1H-isoindole-5-carboxylic acid. DR DrugBank; DB08731; 2-[(1R)-2-carboxy-1-(naphthalen-1-ylmethyl)ethyl]-1,3-dioxo-2,3-dihydro-1H-isoindole-5-carboxylic acid. DR DrugBank; DB08623; 2-[CARBOXY-(2-THIOPHEN-2-YL-ACETYLAMINO)-METHYL]-5-METHYLENE-5,6-DIHYDRO-2H-[1,3]THIAZINE-4-CARBOXYLIC ACID. DR DrugBank; DB08336; 2-Methyl-2-propanyl [(1R)-2-methyl-1-(1,3,4-oxadiazol-2-yl)propyl]carbamate. DR DrugBank; DB08337; 2-Methyl-2-propanyl [(1S)-2-methyl-1-(1,3,4-oxadiazol-2-yl)propyl]carbamate. DR DrugBank; DB07803; 2-phenyl-1H-imidazole-4-carboxylic acid. DR DrugBank; DB02858; 3-(4-Benzenesulfonyl-Thiophene-2-Sulfonylamino)-Phenylboronic Acid. DR DrugBank; DB08306; 3-[(3-Nitrophenyl)sulfamoyl]-2-thiophenecarboxylic acid. DR DrugBank; DB07927; 3-[(4-Carboxy-2-hydroxyphenyl)sulfamoyl]-2-thiophenecarboxylic acid. DR DrugBank; DB08573; 3-[(4-CHLOROANILINO)SULFONYL]THIOPHENE-2-CARBOXYLIC ACID. DR DrugBank; DB02797; 3-Nitrophenylboronic Acid. DR DrugBank; DB08551; 3-{(R)-(Dihydroxyboryl)[(2-thienylacetyl)amino]methyl}benzoic acid. DR DrugBank; DB02627; 4,4'-Biphenyldiboronic Acid. DR DrugBank; DB02503; 4-(Carboxyvin-2-Yl)Phenylboronic Acid. DR DrugBank; DB07541; 4-(dihydroxyboranyl)-2-({[4-(phenylsulfonyl)thiophen-2-yl]sulfonyl}amino)benzoic acid. DR DrugBank; DB07114; 4-[(METHYLSULFONYL)AMINO]BENZOIC ACID. DR DrugBank; DB03140; 4-Carboxyphenylboronic Acid. DR DrugBank; DB07824; 4-ethyl-5-methyl-2-(1H-tetrazol-5-yl)-1,2-dihydro-3H-pyrazol-3-one. DR DrugBank; DB04293; 7-(2-Amino-2-Phenyl-Acetylamino)-3-Chloro-8-Oxo-1-Aza-Bicyclo[4.2.0]Oct-2-Ene-2-Carboxylic Acid. DR DrugBank; DB03530; Acylated ceftazidime. DR DrugBank; DB04360; Benzo[B]Thiophene-2-Boronic Acid. DR DrugBank; DB00456; Cefalotin. DR DrugBank; DB04035; Ceftazidime BATSI. DR DrugBank; DB02247; Hydrolyzed Cephalothin. DR DrugBank; DB01896; M-Aminophenylboronic Acid. DR DrugBank; DB02094; N-2-Thiophen-2-Yl-Acetamide Boronic Acid. DR DrugBank; DB02772; Sucrose. DR DrugCentral; P00811; -. DR MEROPS; S12.006; -. DR jPOST; P00811; -. DR PaxDb; 511145-b4150; -. DR EnsemblBacteria; AAC77110; AAC77110; b4150. DR GeneID; 948669; -. DR KEGG; ecj:JW4111; -. DR KEGG; eco:b4150; -. DR PATRIC; fig|1411691.4.peg.2548; -. DR EchoBASE; EB0038; -. DR eggNOG; COG1680; Bacteria. DR HOGENOM; CLU_020027_10_0_6; -. DR InParanoid; P00811; -. DR OMA; ANRNYPN; -. DR OrthoDB; 5377431at2; -. DR PhylomeDB; P00811; -. DR BioCyc; EcoCyc:EG10040-MONOMER; -. DR BioCyc; MetaCyc:EG10040-MONOMER; -. DR BRENDA; 3.5.2.6; 2026. DR SABIO-RK; P00811; -. DR EvolutionaryTrace; P00811; -. DR PRO; PR:P00811; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0008800; F:beta-lactamase activity; IDA:EcoliWiki. DR GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1. DR InterPro; IPR001466; Beta-lactam-related. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR001586; Beta-lactam_class-C_AS. DR PANTHER; PTHR46825:SF8; BETA-LACTAMASE-RELATED; 1. DR PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1. DR Pfam; PF00144; Beta-lactamase; 1. DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1. DR PROSITE; PS00336; BETA_LACTAMASE_C; 1. DR SWISS-2DPAGE; P00811; -. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic resistance; Direct protein sequencing; Hydrolase; KW Periplasm; Reference proteome; Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000269|PubMed:6795623" FT CHAIN 20..377 FT /note="Beta-lactamase" FT /id="PRO_0000016958" FT ACT_SITE 80 FT /note="Acyl-ester intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10102, FT ECO:0000269|PubMed:6795623" FT ACT_SITE 166 FT /note="Proton acceptor" FT BINDING 331..333 FT /ligand="substrate" FT /evidence="ECO:0000250" FT MUTAGEN 80 FT /note="S->D,E,G: Loss of activity." FT /evidence="ECO:0000269|PubMed:12144785" FT MUTAGEN 83 FT /note="K->Q,T: Lowers activity more than 1000-fold and FT increases protein stability." FT /evidence="ECO:0000269|PubMed:12144785" FT MUTAGEN 166 FT /note="Y->E: Lowers activity more than 1000-fold." FT /evidence="ECO:0000269|PubMed:12144785" FT MUTAGEN 168 FT /note="N->D,H: Lowers activity more than 1000-fold." FT /evidence="ECO:0000269|PubMed:12144785" FT MUTAGEN 331 FT /note="K->A: Lowers activity more than 1000-fold." FT /evidence="ECO:0000269|PubMed:12144785" FT HELIX 22..39 FT /evidence="ECO:0007829|PDB:2FFY" FT STRAND 42..50 FT /evidence="ECO:0007829|PDB:2FFY" FT STRAND 53..63 FT /evidence="ECO:0007829|PDB:2FFY" FT TURN 64..67 FT /evidence="ECO:0007829|PDB:2FFY" FT STRAND 75..77 FT /evidence="ECO:0007829|PDB:2FFY" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:2FFY" FT HELIX 82..95 FT /evidence="ECO:0007829|PDB:2FFY" FT HELIX 105..108 FT /evidence="ECO:0007829|PDB:2FFY" FT HELIX 110..112 FT /evidence="ECO:0007829|PDB:6YEO" FT HELIX 115..117 FT /evidence="ECO:0007829|PDB:2FFY" FT HELIX 122..126 FT /evidence="ECO:0007829|PDB:2FFY" FT HELIX 144..153 FT /evidence="ECO:0007829|PDB:2FFY" FT STRAND 162..164 FT /evidence="ECO:0007829|PDB:2FFY" FT HELIX 168..178 FT /evidence="ECO:0007829|PDB:2FFY" FT TURN 179..183 FT /evidence="ECO:0007829|PDB:2FFY" FT HELIX 186..193 FT /evidence="ECO:0007829|PDB:2FFY" FT TURN 194..199 FT /evidence="ECO:0007829|PDB:2FFY" FT STRAND 204..206 FT /evidence="ECO:0007829|PDB:2FFY" FT HELIX 209..214 FT /evidence="ECO:0007829|PDB:2FFY" FT STRAND 218..220 FT /evidence="ECO:0007829|PDB:2FFY" FT STRAND 223..225 FT /evidence="ECO:0007829|PDB:2FFY" FT TURN 229..231 FT /evidence="ECO:0007829|PDB:3IWI" FT HELIX 233..236 FT /evidence="ECO:0007829|PDB:2FFY" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:4OLD" FT HELIX 243..254 FT /evidence="ECO:0007829|PDB:2FFY" FT HELIX 256..258 FT /evidence="ECO:0007829|PDB:2FFY" FT HELIX 262..271 FT /evidence="ECO:0007829|PDB:2FFY" FT STRAND 273..278 FT /evidence="ECO:0007829|PDB:2FFY" FT STRAND 281..283 FT /evidence="ECO:0007829|PDB:2FFY" FT STRAND 288..293 FT /evidence="ECO:0007829|PDB:2FFY" FT HELIX 296..301 FT /evidence="ECO:0007829|PDB:2FFY" FT STRAND 303..305 FT /evidence="ECO:0007829|PDB:3GR2" FT STRAND 306..308 FT /evidence="ECO:0007829|PDB:2FFY" FT STRAND 310..313 FT /evidence="ECO:0007829|PDB:2BLS" FT STRAND 315..321 FT /evidence="ECO:0007829|PDB:2FFY" FT STRAND 325..335 FT /evidence="ECO:0007829|PDB:2FFY" FT STRAND 338..345 FT /evidence="ECO:0007829|PDB:2FFY" FT HELIX 346..348 FT /evidence="ECO:0007829|PDB:2FFY" FT STRAND 350..358 FT /evidence="ECO:0007829|PDB:2FFY" FT HELIX 362..376 FT /evidence="ECO:0007829|PDB:2FFY" SQ SEQUENCE 377 AA; 41556 MW; 3C6FB4FE4EF96C9F CRC64; MFKTTLCALL ITASCSTFAA PQQINDIVHR TITPLIEQQK IPGMAVAVIY QGKPYYFTWG YADIAKKQPV TQQTLFELGS VSKTFTGVLG GDAIARGEIK LSDPTTKYWP ELTAKQWNGI TLLHLATYTA GGLPLQVPDE VKSSSDLLRF YQNWQPAWAP GTQRLYANSS IGLFGALAVK PSGLSFEQAM QTRVFQPLKL NHTWINVPPA EEKNYAWGYR EGKAVHVSPG ALDAEAYGVK STIEDMARWV QSNLKPLDIN EKTLQQGIQL AQSRYWQTGD MYQGLGWEML DWPVNPDSII NGSDNKIALA ARPVKAITPP TPAVRASWVH KTGATGGFGS YVAFIPEKEL GIVMLANKNY PNPARVDAAW QILNALQ //