ID BLAN_ENTCL STANDARD; PRT; 292 AA. AC P52663; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-FEB-2005 (Rel. 46, Last annotation update) DE Imipenem-hydrolyzing beta-lactamase precursor (EC 3.5.2.6) DE (Carbapenemase) (NMC-A). GN Name=nmcA; OS Enterobacter cloacae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter. OX NCBI_TaxID=550; RN [1] RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 28-34. RC STRAIN=NOR-1; RX MEDLINE=94329582; PubMed=8052644; RA Naas T., Nordmann P.; RT "Analysis of a carbapenem-hydrolyzing class A beta-lactamase from RT Enterobacter cloacae and of its LysR-type regulatory protein."; RL Proc. Natl. Acad. Sci. U.S.A. 91:7693-7697(1994). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS). RC STRAIN=NOR-1; RX MEDLINE=99395084; PubMed=10464248; DOI=10.1074/jbc.274.36.25260; RA Mourey L., Kotra L.P., Bellettini J., Bulychev A., O'Brien M., RA Miller M.J., Mobashery S., Samama J.-P.; RT "Inhibition of the broad spectrum nonmetallocarbapenamase of class A RT (NMC-A) beta-lactamase from Enterobacter cloacae by monocyclic beta- RT lactams."; RL J. Biol. Chem. 274:25260-25265(1999). CC -!- FUNCTION: Hydrolyzes carbapenems such as imipenem, which are CC extended-spectrum beta-lactam antibiotics. CC -!- CATALYTIC ACTIVITY: A beta-lactam + H(2)O = a substituted beta- CC amino acid. CC -!- SIMILARITY: Belongs to the class-A 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; Z21956; CAA79967.1; -. DR PIR; S35915; S35915. DR PDB; 1BUE; X-ray; A=28-292. DR PDB; 1BUL; X-ray; @=28-292. DR InterPro; IPR001466; Beta_lactamase. DR InterPro; IPR000871; Beta_lactamase_A. DR Pfam; PF00144; Beta-lactamase; 1. DR PRINTS; PR00118; BLACTAMASEA. DR PROSITE; PS00146; BETA_LACTAMASE_A; FALSE_NEG. KW 3D-structure; Antibiotic resistance; Direct protein sequencing; KW Hydrolase; Signal. FT SIGNAL 1 27 FT CHAIN 28 292 Imipenem-hydrolyzing beta-lactamase. FT ACT_SITE 71 71 Acyl-ester intermediate. FT SITE 236 238 Substrate binding (By similarity). FT DISULFID 70 240 FT TURN 30 31 FT HELIX 32 42 FT TURN 43 43 FT STRAND 45 52 FT TURN 53 55 FT STRAND 58 61 FT TURN 63 64 FT STRAND 67 68 FT HELIX 70 73 FT HELIX 74 86 FT TURN 87 88 FT TURN 92 93 FT STRAND 95 96 FT TURN 99 100 FT HELIX 108 112 FT TURN 113 116 FT STRAND 118 119 FT HELIX 120 129 FT HELIX 133 142 FT TURN 143 144 FT HELIX 146 156 FT TURN 157 158 FT STRAND 163 163 FT TURN 168 169 FT HELIX 170 172 FT TURN 176 177 FT TURN 180 181 FT STRAND 182 183 FT HELIX 185 197 FT HELIX 203 214 FT TURN 215 215 FT TURN 220 222 FT HELIX 223 226 FT TURN 229 230 FT STRAND 232 239 FT TURN 243 244 FT STRAND 246 253 FT TURN 255 256 FT STRAND 260 267 FT TURN 271 272 FT HELIX 277 289 FT TURN 290 290 SQ SEQUENCE 292 AA; 32075 MW; 4D33FD8669998F1B CRC64; MSLNVKQSRI AILFSSCLIS ISFFSQANTK GIDEIKNLET DFNGRIGVYA LDTGSGKSFS YRANERFPLC SSFKGFLAAA VLKGSQDNRL NLNQIVNYNT RSLEFHSPIT TKYKDNGMSL GDMAAAALQY SDNGATNIIL ERYIGGPEGM TKFMRSIGDE DFRLDRWELD LNTAIPGDER DTSTPAAVAK SLKTLALGNI LSEHEKETYQ TWLKGNTTGA ARIRASVPSD WVVGDKTGSC GAYGTANDYA VVWPKNRAPL IISVYTTKNE KEAKHEDKVI AEASRIAIDN LK //