ID   AMPD_SALTY              Reviewed;         187 AA.
AC   P0CL03; P30013; Q9L4I4;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 57.
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=STM0146;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95.
RC   STRAIN=LT2;
RX   PubMed=8419294; DOI=10.1128/jb.175.2.479-486.1993;
RA   Hughes K.T., Dessen A., Gray J.P., Grubmeyer C.;
RT   "The Salmonella typhimurium nadC gene: sequence determination by use of
RT   Mud-P22 and purification of quinolinate phosphoribosyltransferase.";
RL   J. Bacteriol. 175:479-486(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; AE006468; AAL19110.1; -; Genomic_DNA.
DR   EMBL; L07292; AAA03224.1; -; Genomic_DNA.
DR   RefSeq; NP_459151.1; NC_003197.2.
DR   RefSeq; WP_000936330.1; NC_003197.2.
DR   AlphaFoldDB; P0CL03; -.
DR   SMR; P0CL03; -.
DR   STRING; 99287.STM0146; -.
DR   PaxDb; P0CL03; -.
DR   EnsemblBacteria; AAL19110; AAL19110; STM0146.
DR   GeneID; 1251664; -.
DR   KEGG; stm:STM0146; -.
DR   PATRIC; fig|99287.12.peg.155; -.
DR   HOGENOM; CLU_049290_1_0_6; -.
DR   PhylomeDB; P0CL03; -.
DR   BioCyc; SENT99287:STM0146-MON; -.
DR   Proteomes; UP000001014; 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; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IBA:GO_Central.
DR   GO; GO:0009254; P:peptidoglycan turnover; IBA:GO_Central.
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   Reference proteome; Zinc.
FT   CHAIN           1..187
FT                   /note="1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD"
FT                   /id="PRO_0000164415"
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;  20943 MW;  9E7EBAC553BA8EA4 CRC64;
     MLPDKGWLVE ARRVPSPHYD CRPDDEKPSL LVVHNISLPP GEFGGPWIDA LFTGTIDPDA
     HPFFAEIAHL RVSAHCLIRR DGEIVQYVPF DKRAWHAGVS NYQGRERCND FSIGIELEGT
     DTLAYTDAQY QQLAAVTRTL IASYPAIADN MTGHCNITPD RKTDPGPAFD WPRFRALVAL
     SSHKEMT