MLTD_ECOLI
ID MLTD_ECOLI Reviewed; 452 AA.
AC P0AEZ7; 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 134.
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, yafG; OrderedLocusNames=b0211, JW5018;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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 35-452.
RC STRAIN=K12;
RX PubMed=1663890; DOI=10.1016/0378-1097(91)90355-e;
RA Kajie S., Ideta R., Yamato I., Anraku Y.;
RT "Molecular cloning and DNA sequence of dniR, a gene affecting anaerobic
RT expression of the Escherichia coli hexaheme nitrite reductase.";
RL FEMS Microbiol. Lett. 67:205-211(1991).
RN [6]
RP SIMILARITY TO SLT.
RX PubMed=8203016; DOI=10.1016/0968-0004(94)90201-1;
RA Koonin E.V., Rudd K.E.;
RT "A conserved domain in putative bacterial and bacteriophage
RT transglycosylases.";
RL Trends Biochem. Sci. 19:106-107(1994).
RN [7]
RP STRUCTURE BY NMR OF 398-445.
RX PubMed=10843862; DOI=10.1006/jmbi.2000.3778;
RA Bateman A., Bycroft M.;
RT "The structure of a LysM domain from E. coli membrane-bound lytic murein
RT transglycosylase D (MltD).";
RL J. Mol. Biol. 299:1113-1119(2000).
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 -!- CAUTION: Was originally thought to be involved in hexaheme nitrite
CC reductase (cytochrome c552) expression. {ECO:0000305|PubMed:1663890}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA43144.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U70214; AAB08633.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73316.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77882.2; -; Genomic_DNA.
DR EMBL; X60739; CAA43144.1; ALT_FRAME; Genomic_DNA.
DR PIR; E64745; E64745.
DR RefSeq; NP_414747.1; NC_000913.3.
DR RefSeq; WP_000644685.1; NZ_STEB01000020.1.
DR PDB; 1E0G; NMR; -; A=398-445.
DR PDBsum; 1E0G; -.
DR AlphaFoldDB; P0AEZ7; -.
DR SMR; P0AEZ7; -.
DR BioGRID; 4261468; 281.
DR DIP; DIP-48010N; -.
DR IntAct; P0AEZ7; 5.
DR STRING; 511145.b0211; -.
DR PaxDb; P0AEZ7; -.
DR PRIDE; P0AEZ7; -.
DR DNASU; 945694; -.
DR EnsemblBacteria; AAC73316; AAC73316; b0211.
DR EnsemblBacteria; BAA77882; BAA77882; BAA77882.
DR GeneID; 66671499; -.
DR GeneID; 945694; -.
DR KEGG; ecj:JW5018; -.
DR KEGG; eco:b0211; -.
DR PATRIC; fig|511145.12.peg.213; -.
DR EchoBASE; EB0242; -.
DR eggNOG; COG0741; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR HOGENOM; CLU_009520_1_4_6; -.
DR InParanoid; P0AEZ7; -.
DR OMA; ARHMPTE; -.
DR PhylomeDB; P0AEZ7; -.
DR BioCyc; EcoCyc:EG10246-MON; -.
DR BioCyc; MetaCyc:EG10246-MON; -.
DR EvolutionaryTrace; P0AEZ7; -.
DR PRO; PR:P0AEZ7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016020; C:membrane; NAS:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0008932; F:lytic endotransglycosylase activity; IDA:EcoCyc.
DR GO; GO:0008933; F:lytic transglycosylase activity; IDA:EcoCyc.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; IMP:EcoliWiki.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell wall biogenesis/degradation; Lipoprotein;
KW Lyase; Membrane; Palmitate; Reference proteome; 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_0000032801"
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"
FT CONFLICT 69..72
FT /note="MGIP -> DGNS (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="D -> A (in Ref. 5)"
FT /evidence="ECO:0000305"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:1E0G"
FT HELIX 410..416
FT /evidence="ECO:0007829|PDB:1E0G"
FT HELIX 421..427
FT /evidence="ECO:0007829|PDB:1E0G"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:1E0G"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:1E0G"
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
