ID   AMPD_SALTS              Reviewed;         187 AA.
AC   E1W818; P30013; Q9L4I4;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 54.
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; OrderedLocusNames=SL1344_0146;
OS   Salmonella typhimurium (strain SL1344).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=216597;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SL1344;
RA   Cano D., Casadesus J., Garcia-del Portillo F.;
RT   "Characterization of a Salmonella-specific region located between ampE and
RT   aroP genes.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL1344;
RX   PubMed=22538806; DOI=10.1073/pnas.1201061109;
RA   Kroger C., Dillon S.C., Cameron A.D., Papenfort K., Sivasankaran S.K.,
RA   Hokamp K., Chao Y., Sittka A., Hebrard M., Handler K., Colgan A.,
RA   Leekitcharoenphon P., Langridge G.C., Lohan A.J., Loftus B., Lucchini S.,
RA   Ussery D.W., Dorman C.J., Thomson N.R., Vogel J., Hinton J.C.;
RT   "The transcriptional landscape and small RNAs of Salmonella enterica
RT   serovar Typhimurium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:E1277-E1286(2012).
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; AJ242516; CAB89835.1; -; Genomic_DNA.
DR   EMBL; FQ312003; CBW16249.1; -; Genomic_DNA.
DR   RefSeq; WP_000936329.1; NZ_QASL01000007.1.
DR   AlphaFoldDB; E1W818; -.
DR   SMR; E1W818; -.
DR   EnsemblBacteria; CBW16249; CBW16249; SL1344_0146.
DR   KEGG; sey:SL1344_0146; -.
DR   PATRIC; fig|216597.6.peg.162; -.
DR   HOGENOM; CLU_049290_1_0_6; -.
DR   OMA; PFTDAQY; -.
DR   BioCyc; SENT216597:SL1344_RS00745-MON; -.
DR   Proteomes; UP000008962; Chromosome.
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_0000405414"
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;  20913 MW;  9E7EBAC553AEDFE1 CRC64;
     MLPDKGWLVE ARRVPSPHYD CRPDDEKPSL LVVHNISLPP GEFGGPWIDA LFTGTIDPDA
     HPFFAEIAHL RVSAHCLIRR DGEIVQYVPF DKRAWHAGVS NYQGRERCND FSIGIELEGT
     DTLAYTDAQY QQLAAVTRTL IASYPAIADN MTGHCNIAPD RKTDPGPAFD WPRFRALVAL
     SSHKEMT