ID AMPC_ENTCL STANDARD; PRT; 381 AA. AC P05364; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 01-FEB-2005 (Rel. 46, Last annotation update) DE Beta-lactamase precursor (EC 3.5.2.6) (Cephalosporinase). GN Name=ampC; OS Enterobacter cloacae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter. OX NCBI_TaxID=550; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MHN1, P99, and Q908R; RX MEDLINE=88268750; PubMed=3260487; 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 RT beta-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 MEDLINE=94068583; PubMed=8248237; 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 RT cloacae 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 MEDLINE=94263990; PubMed=8204611; RA Lobkovsky E., Billings E.M., Moews P.C., Rahil J., Pratt R.F., RA Knox J.R.; RT "Crystallographic structure of a phosphonate derivative of the RT Enterobacter cloacae P99 cephalosporinase: mechanistic interpretation RT of a beta-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: A beta-lactam + H(2)O = a substituted beta- CC amino acid. CC -!- SUBCELLULAR LOCATION: Periplasmic (By similarity). CC -!- MISCELLANEOUS: The sequence shown is that of strain P99. CC -!- SIMILARITY: Belongs to the class-C beta-lactamase family. CC -------------------------------------------------------------------------- CC This Swiss-Prot entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use as long as its content is in no way modified and this statement is not CC removed. CC -------------------------------------------------------------------------- DR EMBL; X07274; CAA30257.1; -. DR EMBL; X08082; CAA30879.1; -. DR EMBL; X08081; CAA30878.1; -. DR PIR; S00404; PNKBP. DR PIR; S00406; PNKBM. DR PDB; 1BLS; X-ray; A/B=21-381. DR PDB; 1XX2; X-ray; A/B=21-381. DR InterPro; IPR001586; Beta_lactam_C_AS. DR InterPro; IPR001466; Beta_lactamase. DR Pfam; PF00144; Beta-lactamase; 1. DR PROSITE; PS00336; BETA_LACTAMASE_C; 1. KW 3D-structure; Antibiotic resistance; Hydrolase; Periplasmic; Signal. FT SIGNAL 1 20 FT CHAIN 21 381 Beta-lactamase. FT ACT_SITE 84 84 Acyl-ester intermediate. FT ACT_SITE 170 170 Proton acceptor. FT SITE 335 337 Substrate binding. FT VARIANT 3 3 R -> I (in strain MHN1). FT VARIANT 14 14 I -> L (in strain MHN1). FT VARIANT 21 21 T -> A (in strain MHN1). FT VARIANT 36 36 I -> V (in strain MHN1 and strain Q980R). FT VARIANT 58 58 P -> S (in strain MHN1). FT VARIANT 108 108 A -> P (in strain MHN1 and strain Q980R). FT VARIANT 152 152 L -> V (in strain Q980R). FT VARIANT 262 262 N -> K (in strain MHN1). FT VARIANT 319 319 A -> V (in strain Q980R). FT VARIANT 362 362 T -> K (in strain MHN1). FT HELIX 25 42 FT TURN 43 44 FT STRAND 47 54 FT TURN 55 56 FT STRAND 57 67 FT TURN 68 71 FT STRAND 72 73 FT TURN 76 77 FT STRAND 79 81 FT HELIX 83 85 FT HELIX 86 100 FT TURN 101 101 FT TURN 105 106 FT STRAND 108 108 FT HELIX 109 111 FT TURN 112 112 FT TURN 114 115 FT HELIX 119 121 FT TURN 122 123 FT STRAND 125 125 FT HELIX 126 131 FT TURN 132 132 FT TURN 143 144 FT HELIX 148 157 FT TURN 164 165 FT STRAND 167 168 FT HELIX 172 182 FT TURN 183 183 FT HELIX 184 186 FT HELIX 190 197 FT TURN 198 198 FT HELIX 199 202 FT TURN 203 203 FT TURN 205 206 FT STRAND 207 208 FT TURN 213 215 FT HELIX 216 218 FT STRAND 219 219 FT STRAND 222 223 FT STRAND 228 229 FT TURN 235 236 FT HELIX 237 240 FT TURN 241 241 FT STRAND 244 245 FT HELIX 247 258 FT HELIX 260 262 FT HELIX 266 275 FT TURN 276 276 FT STRAND 278 282 FT TURN 283 284 FT STRAND 285 287 FT STRAND 292 295 FT HELIX 300 306 FT TURN 307 307 FT HELIX 309 312 FT TURN 313 313 FT STRAND 316 317 FT STRAND 319 325 FT STRAND 331 338 FT STRAND 343 349 FT HELIX 350 352 FT TURN 353 353 FT STRAND 354 360 FT STRAND 362 362 FT HELIX 366 378 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 //