ID   AMPD_ENTCL              Reviewed;         187 AA.
AC   P82973; Q00831;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2001, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD {ECO:0000250|UniProtKB:P13016};
DE            EC=3.5.1.28 {ECO:0000250|UniProtKB:P13016};
DE   AltName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000250|UniProtKB:P13016};
GN   Name=ampD {ECO:0000303|PubMed:8383940};
OS   Enterobacter cloacae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=550;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=14;
RX   PubMed=8383940; DOI=10.1128/aac.37.2.224;
RA   Kopp U., Wiedemann B., Lindquist S., Normark S.;
RT   "Sequences of wild-type and mutant ampD genes of Citrobacter freundii and
RT   Enterobacter cloacae.";
RL   Antimicrob. Agents Chemother. 37:224-228(1993).
CC   -!- FUNCTION: Involved in cell wall peptidoglycan recycling. Specifically
CC       cleaves the amide bond between the lactyl group of N-acetylmuramic acid
CC       and the alpha-amino group of the L-alanine in degradation products
CC       containing an anhydro N-acetylmuramyl moiety.
CC       {ECO:0000250|UniProtKB:P13016}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC         Evidence={ECO:0000250|UniProtKB:P13016};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P82974};
CC       Note=Zn(2+) is required for amidase activity.
CC       {ECO:0000250|UniProtKB:P82974};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P13016}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; Z14003; CAA78391.1; -; Genomic_DNA.
DR   PIR; A48901; A48901.
DR   AlphaFoldDB; P82973; -.
DR   SMR; P82973; -.
DR   STRING; 1399774.JDWH01000001_gene2360; -.
DR   eggNOG; COG3023; Bacteria.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 3.40.80.10; -; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   Pfam; PF01510; Amidase_2; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF55846; SSF55846; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Cytoplasm; Hydrolase; Metal-binding;
KW   Zinc.
FT   CHAIN           1..187
FT                   /note="1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD"
FT                   /id="PRO_0000164412"
FT   DOMAIN          29..167
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        116
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P75820"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P82974"
FT   BINDING         154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P82974"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P82974"
FT   SITE            162
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P75820"
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