ID   MLTD_ECOL6              Reviewed;         452 AA.
AC   P0AEZ8; P23931; P32982; P77350;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Membrane-bound lytic murein transglycosylase D;
DE            EC=4.2.2.n1;
DE   AltName: Full=Murein hydrolase D;
DE   AltName: Full=Regulatory protein DniR;
DE   Flags: Precursor;
GN   Name=mltD; Synonyms=dniR; OrderedLocusNames=c0248;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Murein-degrading enzyme. May play a role in recycling of
CC       muropeptides during cell elongation and/or cell division (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage
CC         between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC         (GlcNAc) residues in peptidoglycan, from either the reducing or the
CC         non-reducing ends of the peptidoglycan chains, with concomitant
CC         formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n1;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- DOMAIN: LysM domains are thought to be involved in peptidoglycan
CC       binding.
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014075; AAN78738.1; -; Genomic_DNA.
DR   RefSeq; WP_000644685.1; NC_004431.1.
DR   AlphaFoldDB; P0AEZ8; -.
DR   SMR; P0AEZ8; -.
DR   STRING; 199310.c0248; -.
DR   CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   EnsemblBacteria; AAN78738; AAN78738; c0248.
DR   GeneID; 66671499; -.
DR   KEGG; ecc:c0248; -.
DR   eggNOG; COG0741; Bacteria.
DR   eggNOG; COG1388; Bacteria.
DR   HOGENOM; CLU_009520_1_4_6; -.
DR   OMA; ARHMPTE; -.
DR   BioCyc; ECOL199310:C0248-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR   CDD; cd00118; LysM; 2.
DR   Gene3D; 3.10.350.10; -; 2.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR000189; Transglyc_AS.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   Pfam; PF01476; LysM; 2.
DR   Pfam; PF01464; SLT; 1.
DR   SMART; SM00257; LysM; 2.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   SUPFAM; SSF54106; SSF54106; 2.
DR   PROSITE; PS51782; LYSM; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Lipoprotein; Lyase;
KW   Membrane; Palmitate; Repeat; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           16..452
FT                   /note="Membrane-bound lytic murein transglycosylase D"
FT                   /id="PRO_0000044623"
FT   DOMAIN          341..384
FT                   /note="LysM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          400..448
FT                   /note="LysM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   REGION          113..198
FT                   /note="Slt-type domain"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10071"
FT   LIPID           16
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           16
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   452 AA;  49417 MW;  80CD5BBE5F5949E8 CRC64;
     MKAKAILLAS VLLVGCQSTG NVQQHAQSLS AAGQGEAAKF TSQARWMDDG TSIAPDGDLW
     AFIGDELKMG IPENDRIREQ KQKYLRNKSY LHDVTLRAEP YMYWIAGQVK KRNMPMELVL
     LPIVESAFDP HATSGANAAG IWQIIPSTGR NYGLKQTRNY DARRDVVAST TAALNMMQRL
     NKMFDGDWLL TVAAYNSGEG RVMKAIKTNK ARGKSTDFWS LPLPQETKQY VPKMLALSDI
     LKNSKRYGVR LPTTDESRAL ARVHLSSPVE MAKVADMAGI SVSKLKTFNA GVKGSTLGAS
     GPQYVMVPKK HADQLRESLA SGEIAAVQST LVADNTPLNS RVYTVRSGDT LSSIASRLGV
     STKDLQQWNK LRGSKLKPGQ SLTIGAGSSA QRLANNSDSI TYRVRKGDSL SSIAKRHGVN
     IKDVMRWNSD TANLQPGDKL TLFVKNNNMP DS