AMPD_ECOLI
ID AMPD_ECOLI Reviewed; 183 AA.
AC P13016;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD {ECO:0000305};
DE EC=3.5.1.28 {ECO:0000269|PubMed:19309146};
DE AltName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000305};
GN Name=ampD; OrderedLocusNames=b0110, JW0106;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12;
RX PubMed=2691840; DOI=10.1111/j.1365-2958.1989.tb00259.x;
RA Lindquist S., Galleni M., Lindberg F., Normark S.;
RT "Signalling proteins in enterobacterial AmpC beta-lactamase regulation.";
RL Mol. Microbiol. 3:1091-1102(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12;
RX PubMed=2607970; DOI=10.1111/j.1365-2958.1989.tb00262.x;
RA Honore N., Nicolas M.H., Cole S.T.;
RT "Regulation of enterobacterial cephalosporinase production: the role of a
RT membrane-bound sensory transducer.";
RL Mol. Microbiol. 3:1121-1130(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-92.
RC STRAIN=K12;
RX PubMed=7959070; DOI=10.1016/0378-1119(94)90851-6;
RA Whitchurch C.B., Mattick J.S.;
RT "Escherichia coli contains a set of genes homologous to those involved in
RT protein secretion, DNA uptake and the assembly of type-4 fimbriae in other
RT bacteria.";
RL Gene 150:9-15(1994).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19309146; DOI=10.1021/ja808498m;
RA Hesek D., Lee M., Zhang W., Noll B.C., Mobashery S.;
RT "Total synthesis of N-acetylglucosamine-1,6-anhydro-N-
RT acetylmuramylpentapeptide and evaluation of its turnover by AmpD from
RT Escherichia coli.";
RL J. Am. Chem. Soc. 131:5187-5193(2009).
CC -!- FUNCTION: Involved in cell wall peptidoglycan recycling
CC (PubMed:19309146). Specifically cleaves the amide bond between the
CC lactyl group of N-acetylmuramic acid and the alpha-amino group of the
CC L-alanine in degradation products containing an anhydro N-acetylmuramyl
CC moiety (PubMed:19309146). Is also involved in beta-lactamase induction
CC (PubMed:2691840, PubMed:2607970). {ECO:0000269|PubMed:19309146,
CC ECO:0000269|PubMed:2607970, ECO:0000269|PubMed:2691840}.
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:0000269|PubMed:19309146};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1760 uM for N-acetyl-beta-D-glucosamine-(1-->4)-1,6-anhydro-N-
CC acetyl-beta-D-muramyl-L-Ala-gamma-D-Glu-meso-DAP-D-Ala-D-Ala
CC {ECO:0000269|PubMed:19309146};
CC Note=kcat is 0.4 sec(-1). {ECO:0000269|PubMed:19309146};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:19309146}.
CC -!- INDUCTION: Inactivation of AmpD results in AmpR-dependent
CC hyperinduction and AmpD affects beta-lactam susceptibility in the
CC absence of cloned C.freundii amp genes suggesting a linkage between
CC AmpD and peptidoglycan synthesis.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000305}.
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DR EMBL; X15237; CAA33314.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73221.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96679.1; -; Genomic_DNA.
DR EMBL; L28105; AAC36921.1; -; Genomic_DNA.
DR PIR; S05569; S05569.
DR RefSeq; NP_414652.1; NC_000913.3.
DR RefSeq; WP_000923721.1; NZ_STEB01000010.1.
DR AlphaFoldDB; P13016; -.
DR SMR; P13016; -.
DR BioGRID; 4261895; 176.
DR STRING; 511145.b0110; -.
DR jPOST; P13016; -.
DR PaxDb; P13016; -.
DR PRIDE; P13016; -.
DR EnsemblBacteria; AAC73221; AAC73221; b0110.
DR EnsemblBacteria; BAB96679; BAB96679; BAB96679.
DR GeneID; 66671602; -.
DR GeneID; 948877; -.
DR KEGG; ecj:JW0106; -.
DR KEGG; eco:b0110; -.
DR PATRIC; fig|1411691.4.peg.2172; -.
DR EchoBASE; EB0039; -.
DR eggNOG; COG3023; Bacteria.
DR HOGENOM; CLU_049290_1_0_6; -.
DR InParanoid; P13016; -.
DR OMA; PFTDAQY; -.
DR PhylomeDB; P13016; -.
DR BioCyc; EcoCyc:EG10041-MON; -.
DR BioCyc; MetaCyc:EG10041-MON; -.
DR PRO; PR:P13016; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009392; F:N-acetyl-anhydromuramoyl-L-alanine amidase activity; IDA:EcoCyc.
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; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Cytoplasm; Hydrolase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..183
FT /note="1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD"
FT /id="PRO_0000164413"
FT DOMAIN 30..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 183 AA; 20536 MW; F62910F8F889043D CRC64;
MLLEQGWLVG ARRVPSPHYD CRPDDETPTL LVVHNISLPP GEFGGPWIDA LFTGTIDPQA
HPFFAEIAHL RVSAHCLIRR DGEIVQYVPF DKRAWHAGVS QYQGRERCND FSIGIELEGT
DTLAYTDAQY QQLAAVTRAL IDCYPDIAKN MTGHCDIAPD RKTDPGPAFD WARFRVLVSK
ETT
