ID AMPD_ENTCL STANDARD; PRT; 187 AA. AC P82973; Q00831; DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2001, sequence version 1. DT 07-FEB-2006, entry version 25. DE Protein ampD. GN Name=ampD; OS Enterobacter cloacae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=550; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=14; RX MEDLINE=93199292; PubMed=8383940; RA Kopp U., Wiedemann B., Lindquist S., Normark S.; RT "Sequences of wild-type and mutant ampD genes of Citrobacter freundii RT and Enterobacter cloacae."; RL Antimicrob. Agents Chemother. 37:224-228(1993). CC -!- FUNCTION: Putative signaling protein in beta-lactamase regulation. CC AmpD seems not to act as a direct sensor for beta-lactams. It CC hydrolyzes 1,6-anhydro-N-acetylmuramoyl-L-alanyl-D-3-glutamyl- CC meso-diaminopimelic acid to the tripeptide L-alanyl-gamma-D- CC glutamyl-meso-diaminopimelate (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z14003; CAA78391.1; -; Genomic_DNA. DR PIR; A48901; A48901. DR HSSP; P82974; 1J3G. DR SMR; P82973; 1-187. DR InterPro; IPR002502; Amidase_2. DR Pfam; PF01510; Amidase_2; 1. DR SMART; SM00644; Ami_2; 1. KW Cell wall; Hydrolase. FT CHAIN 1 187 Protein ampD. FT /FTId=PRO_0000164412. SQ SEQUENCE 187 AA; 20839 MW; F1D23B55B84E71C8 CRC64; MLLENGWLVD ARHVPSPHHD CRPEDEKPTL LVVHNISLPP GEFGGPWIDA LFTGTIDPDA HPFFAEIAHL ALSADCLIRR DGEVVQYVPF DKRAWHAGVS MYQGRERCND FSIGIELEGT DTTPYTDAQY EKLVAVTQTL IGRYPAIADN ITGHSDIAPE RKTDPGPAFD WSRFHAMLTT SSDKEIT //