AMPC_ECOLI
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 03-AUG-2022, entry version 188.
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; Proteobacteria; 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}.
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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 SWISS-2DPAGE; P00811; -.
DR jPOST; P00811; -.
DR PaxDb; P00811; -.
DR PRIDE; P00811; -.
DR EnsemblBacteria; AAC77110; AAC77110; b4150.
DR EnsemblBacteria; BAE78154; BAE78154; BAE78154.
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 PhylomeDB; P00811; -.
DR BioCyc; EcoCyc:EG10040-MON; -.
DR BioCyc; MetaCyc:EG10040-MON; -.
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; -; 1.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001586; Beta-lactam_class-C_AS.
DR Pfam; PF00144; Beta-lactamase; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR PROSITE; PS00336; BETA_LACTAMASE_C; 1.
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
