ID AMPC_ENTCL Reviewed; 381 AA. AC P05364; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1988, sequence version 1. DT 24-JAN-2024, entry version 126. DE RecName: Full=Beta-lactamase; DE EC=3.5.2.6; DE AltName: Full=Cephalosporinase; DE Flags: Precursor; GN Name=ampC; OS Enterobacter cloacae. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=550; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MHN1, P99, and Q908R; RX PubMed=3260487; DOI=10.1042/bj2500753; RA Galleni M., Lindberg F., Normark S., Cole S., Honore N., Joris B., RA Frere J.-M.; RT "Sequence and comparative analysis of three Enterobacter cloacae ampC beta- RT lactamase genes and their products."; RL Biochem. J. 250:753-760(1988). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RC STRAIN=P99; RX PubMed=8248237; DOI=10.1073/pnas.90.23.11257; RA Lobkovsky E., Moews P.C., Liu H., Zhao H., Frere J.-M., Knox J.R.; RT "Evolution of an enzyme activity: crystallographic structure at 2-A RT resolution of cephalosporinase from the ampC gene of Enterobacter cloacae RT P99 and comparison with a class A penicillinase."; RL Proc. Natl. Acad. Sci. U.S.A. 90:11257-11261(1993). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RC STRAIN=P99; RX PubMed=8204611; DOI=10.1021/bi00188a004; RA Lobkovsky E., Billings E.M., Moews P.C., Rahil J., Pratt R.F., Knox J.R.; RT "Crystallographic structure of a phosphonate derivative of the Enterobacter RT cloacae P99 cephalosporinase: mechanistic interpretation of a beta- RT lactamase transition-state analog."; RL Biochemistry 33:6762-6772(1994). 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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. CC -!- MISCELLANEOUS: The sequence shown is that of strain P99. 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; X07274; CAA30257.1; -; Genomic_DNA. DR EMBL; X08082; CAA30879.1; -; Genomic_DNA. DR EMBL; X08081; CAA30878.1; -; Genomic_DNA. DR PIR; S00404; PNKBP. DR PIR; S00405; PNKBQ. DR PIR; S00406; PNKBM. DR PDB; 1BLS; X-ray; 2.30 A; A/B=21-381. DR PDB; 1GCE; X-ray; 1.80 A; A=21-381. DR PDB; 1RGZ; X-ray; 1.37 A; A=22-381. DR PDB; 1XX2; X-ray; 1.88 A; A/B=21-381. DR PDB; 1Y54; X-ray; 2.10 A; A=21-381. DR PDB; 2Q9M; X-ray; 2.05 A; A=22-380. DR PDB; 2Q9N; X-ray; 2.20 A; A=22-380. DR PDB; 3S4X; X-ray; 1.95 A; A=21-381. DR PDB; 4XUX; X-ray; 1.75 A; A=21-381. DR PDB; 5HAI; X-ray; 2.74 A; A=21-381. DR PDB; 5XHR; X-ray; 1.80 A; A=21-381. DR PDB; 7TI1; X-ray; 2.00 A; A=1-381. DR PDBsum; 1BLS; -. DR PDBsum; 1GCE; -. DR PDBsum; 1RGZ; -. DR PDBsum; 1XX2; -. DR PDBsum; 1Y54; -. DR PDBsum; 2Q9M; -. DR PDBsum; 2Q9N; -. DR PDBsum; 3S4X; -. DR PDBsum; 4XUX; -. DR PDBsum; 5HAI; -. DR PDBsum; 5XHR; -. DR PDBsum; 7TI1; -. DR AlphaFoldDB; P05364; -. DR SMR; P05364; -. DR BindingDB; P05364; -. DR ChEMBL; CHEMBL2725; -. DR DrugBank; DB08110; (1R,4S,7AS)-1-(1-FORMYLPROP-1-EN-1-YL)-4-METHOXY-2,4,5,6,7,7A-HEXAHYDRO-1H-ISOINDOLE-3-CARBOXYLIC ACID. DR DrugBank; DB08109; (1S,4R,7AR)-4-BUTOXY-1-[(1R)-1-FORMYLPROPYL]-2,4,5,6,7,7A-HEXAHYDRO-1H-ISOINDOLE-3-CARBOXYLIC ACID. DR DrugBank; DB03970; (7R)-7-(6,7-Dihydro-5H-cyclopenta[d]imidazo[2,1-b][1,3]thiazol-2-yl)-2,7-dihydro-1,4-thiazepine-3,6-dicarboxylic acid. DR DrugBank; DB04123; (P-Iodophenylacetylamino)Methylphosphinic Acid. DR DrugBank; DB02876; 3-(4-carbamoyl-1-carboxy-2-methylsulfonyl-buta-1,3-dienylamino)-indolizine-2-carboxylic acid. DR DrugBank; DB02122; 4-iodo-acetamido phenylboronic acid. DR DrugBank; DB02816; 7-(1-Methyl-1,2,3-Triazol-4-Yl)-6-Formyl-2,7-Dihydro-[1,4]Thiazepine-3-Carboxylic Acid, Brl42715, C6-(N1-Methyl-1,2,3-Triazolylmethylene)Penem. DR DrugBank; DB09060; Avibactam. DR DrugBank; DB12377; Relebactam. DR DrugBank; DB12107; Vaborbactam. DR DrugCentral; P05364; -. DR MEROPS; S12.006; -. DR BRENDA; 3.5.2.6; 155. DR SABIO-RK; P05364; -. DR EvolutionaryTrace; P05364; -. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC. 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. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic resistance; Hydrolase; Periplasm; Signal. FT SIGNAL 1..20 FT CHAIN 21..381 FT /note="Beta-lactamase" FT /id="PRO_0000016959" FT ACT_SITE 84 FT /note="Acyl-ester intermediate" FT ACT_SITE 170 FT /note="Proton acceptor" FT BINDING 335..337 FT /ligand="substrate" FT VARIANT 3 FT /note="R -> I (in strain: MHN1)" FT VARIANT 14 FT /note="I -> L (in strain: MHN1)" FT VARIANT 21 FT /note="T -> A (in strain: MHN1)" FT VARIANT 36 FT /note="I -> V (in strain: MHN1 and Q980R)" FT VARIANT 58 FT /note="P -> S (in strain: MHN1)" FT VARIANT 108 FT /note="A -> P (in strain: MHN1 and Q980R)" FT VARIANT 152 FT /note="L -> V (in strain: Q980R)" FT VARIANT 262 FT /note="N -> K (in strain: MHN1)" FT VARIANT 319 FT /note="A -> V (in strain: Q980R)" FT VARIANT 362 FT /note="T -> K (in strain: MHN1)" FT HELIX 25..42 FT /evidence="ECO:0007829|PDB:1RGZ" FT STRAND 46..54 FT /evidence="ECO:0007829|PDB:1RGZ" FT STRAND 57..67 FT /evidence="ECO:0007829|PDB:1RGZ" FT TURN 68..71 FT /evidence="ECO:0007829|PDB:1RGZ" FT STRAND 79..81 FT /evidence="ECO:0007829|PDB:1RGZ" FT HELIX 83..85 FT /evidence="ECO:0007829|PDB:1RGZ" FT HELIX 86..99 FT /evidence="ECO:0007829|PDB:1RGZ" FT HELIX 109..112 FT /evidence="ECO:0007829|PDB:1RGZ" FT HELIX 119..121 FT /evidence="ECO:0007829|PDB:1RGZ" FT HELIX 126..130 FT /evidence="ECO:0007829|PDB:1RGZ" FT HELIX 148..157 FT /evidence="ECO:0007829|PDB:1RGZ" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:1RGZ" FT HELIX 172..182 FT /evidence="ECO:0007829|PDB:1RGZ" FT HELIX 184..186 FT /evidence="ECO:0007829|PDB:1RGZ" FT HELIX 190..197 FT /evidence="ECO:0007829|PDB:1RGZ" FT TURN 198..203 FT /evidence="ECO:0007829|PDB:1RGZ" FT STRAND 207..210 FT /evidence="ECO:0007829|PDB:1RGZ" FT HELIX 213..218 FT /evidence="ECO:0007829|PDB:1RGZ" FT STRAND 222..224 FT /evidence="ECO:0007829|PDB:1RGZ" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:1RGZ" FT HELIX 237..241 FT /evidence="ECO:0007829|PDB:1RGZ" FT HELIX 247..258 FT /evidence="ECO:0007829|PDB:1RGZ" FT HELIX 260..262 FT /evidence="ECO:0007829|PDB:1RGZ" FT HELIX 266..275 FT /evidence="ECO:0007829|PDB:1RGZ" FT STRAND 277..282 FT /evidence="ECO:0007829|PDB:1RGZ" FT STRAND 285..287 FT /evidence="ECO:0007829|PDB:1RGZ" FT STRAND 292..297 FT /evidence="ECO:0007829|PDB:1RGZ" FT HELIX 300..307 FT /evidence="ECO:0007829|PDB:1RGZ" FT HELIX 309..312 FT /evidence="ECO:0007829|PDB:1RGZ" FT STRAND 319..325 FT /evidence="ECO:0007829|PDB:1RGZ" FT STRAND 329..338 FT /evidence="ECO:0007829|PDB:1RGZ" FT STRAND 343..349 FT /evidence="ECO:0007829|PDB:1RGZ" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:1RGZ" FT STRAND 354..362 FT /evidence="ECO:0007829|PDB:1RGZ" FT HELIX 366..379 FT /evidence="ECO:0007829|PDB:1RGZ" SQ SEQUENCE 381 AA; 41302 MW; 90F56ABAF07AA304 CRC64; MMRKSLCCAL LLGISCSALA TPVSEKQLAE VVANTITPLM KAQSVPGMAV AVIYQGKPHY YTFGKADIAA NKPVTPQTLF ELGSISKTFT GVLGGDAIAR GEISLDDAVT RYWPQLTGKQ WQGIRMLDLA TYTAGGLPLQ VPDEVTDNAS LLRFYQNWQP QWKPGTTRLY ANASIGLFGA LAVKPSGMPY EQAMTTRVLK PLKLDHTWIN VPKAEEAHYA WGYRDGKAVR VSPGMLDAQA YGVKTNVQDM ANWVMANMAP ENVADASLKQ GIALAQSRYW RIGSMYQGLG WEMLNWPVEA NTVVEGSDSK VALAPLPVAE VNPPAPPVKA SWVHKTGSTG GFGSYVAFIP EKQIGIVMLA NTSYPNPARV EAAYHILEAL Q //