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Protein

Membrane-bound lytic murein transglycosylase D

Gene

mltD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division (By similarity).By similarity

Catalytic activityi

Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei125 – 1251PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • cell wall organization Source: UniProtKB-KW
  • peptidoglycan metabolic process Source: InterPro
  • positive regulation of oxidoreductase activity Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciEcoCyc:EG10246-MONOMER.
ECOL316407:JW5018-MONOMER.
MetaCyc:EG10246-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane-bound lytic murein transglycosylase D (EC:4.2.2.n1)
Alternative name(s):
Murein hydrolase D
Regulatory protein DniR
Gene namesi
Name:mltD
Synonyms:dniR, yafG
Ordered Locus Names:b0211, JW5018
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10246. mltD.

Subcellular locationi

GO - Cellular componenti

  • cell outer membrane Source: EcoCyc
  • membrane Source: EcoliWiki
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515PROSITE-ProRule annotationAdd
BLAST
Chaini16 – 452437Membrane-bound lytic murein transglycosylase DPRO_0000032801Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi16 – 161N-palmitoyl cysteinePROSITE-ProRule annotation
Lipidationi16 – 161S-diacylglycerol cysteinePROSITE-ProRule annotation

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiP0AEZ7.
PRIDEiP0AEZ7.

Interactioni

Protein-protein interaction databases

BioGridi4261468. 281 interactions.
DIPiDIP-48010N.
IntActiP0AEZ7. 4 interactions.
STRINGi511145.b0211.

Structurei

Secondary structure

1
452
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi401 – 4044Combined sources
Helixi410 – 4167Combined sources
Helixi421 – 4277Combined sources
Helixi431 – 4333Combined sources
Beta strandi438 – 4414Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E0GNMR-A398-445[»]
ProteinModelPortaliP0AEZ7.
SMRiP0AEZ7. Positions 262-445.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AEZ7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini341 – 38444LysM 1PROSITE-ProRule annotationAdd
BLAST
Domaini400 – 44849LysM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni113 – 19886Slt-type domainAdd
BLAST

Domaini

LysM domains are thought to be involved in peptidoglycan binding.

Sequence similaritiesi

Belongs to the transglycosylase Slt family.Curated
Contains 2 LysM domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4105E9H. Bacteria.
COG0741. LUCA.
HOGENOMiHOG000258639.
InParanoidiP0AEZ7.
KOiK08307.
OMAiYNPAYNQ.
PhylomeDBiP0AEZ7.

Family and domain databases

Gene3Di3.10.350.10. 2 hits.
InterProiIPR018392. LysM_dom.
IPR023346. Lysozyme-like_dom.
IPR000189. Transglyc_AS.
IPR008258. Transglycosylase_SLT_dom_1.
[Graphical view]
PfamiPF01476. LysM. 2 hits.
PF01464. SLT. 1 hit.
[Graphical view]
SMARTiSM00257. LysM. 2 hits.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
SSF54106. SSF54106. 2 hits.
PROSITEiPS51782. LYSM. 2 hits.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AEZ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAKAILLAS VLLVGCQSTG NVQQHAQSLS AAGQGEAAKF TSQARWMDDG
60 70 80 90 100
TSIAPDGDLW AFIGDELKMG IPENDRIREQ KQKYLRNKSY LHDVTLRAEP
110 120 130 140 150
YMYWIAGQVK KRNMPMELVL LPIVESAFDP HATSGANAAG IWQIIPSTGR
160 170 180 190 200
NYGLKQTRNY DARRDVVAST TAALNMMQRL NKMFDGDWLL TVAAYNSGEG
210 220 230 240 250
RVMKAIKTNK ARGKSTDFWS LPLPQETKQY VPKMLALSDI LKNSKRYGVR
260 270 280 290 300
LPTTDESRAL ARVHLSSPVE MAKVADMAGI SVSKLKTFNA GVKGSTLGAS
310 320 330 340 350
GPQYVMVPKK HADQLRESLA SGEIAAVQST LVADNTPLNS RVYTVRSGDT
360 370 380 390 400
LSSIASRLGV STKDLQQWNK LRGSKLKPGQ SLTIGAGSSA QRLANNSDSI
410 420 430 440 450
TYRVRKGDSL SSIAKRHGVN IKDVMRWNSD TANLQPGDKL TLFVKNNNMP

DS
Length:452
Mass (Da):49,417
Last modified:December 20, 2005 - v1
Checksum:i80CD5BBE5F5949E8
GO

Sequence cautioni

The sequence CAA43144 differs from that shown. Reason: Frameshift at positions 55, 87 and 226. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 724MGIP → DGNS (PubMed:1663890).Curated
Sequence conflicti217 – 2171D → A (PubMed:1663890).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70214 Genomic DNA. Translation: AAB08633.1.
U00096 Genomic DNA. Translation: AAC73316.1.
AP009048 Genomic DNA. Translation: BAA77882.2.
X60739 Genomic DNA. Translation: CAA43144.1. Frameshift.
PIRiE64745.
RefSeqiNP_414747.1. NC_000913.3.
WP_000644685.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73316; AAC73316; b0211.
BAA77882; BAA77882; BAA77882.
GeneIDi945694.
KEGGiecj:JW5018.
eco:b0211.
PATRICi32115535. VBIEscCol129921_0213.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70214 Genomic DNA. Translation: AAB08633.1.
U00096 Genomic DNA. Translation: AAC73316.1.
AP009048 Genomic DNA. Translation: BAA77882.2.
X60739 Genomic DNA. Translation: CAA43144.1. Frameshift.
PIRiE64745.
RefSeqiNP_414747.1. NC_000913.3.
WP_000644685.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E0GNMR-A398-445[»]
ProteinModelPortaliP0AEZ7.
SMRiP0AEZ7. Positions 262-445.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261468. 281 interactions.
DIPiDIP-48010N.
IntActiP0AEZ7. 4 interactions.
STRINGi511145.b0211.

Proteomic databases

PaxDbiP0AEZ7.
PRIDEiP0AEZ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73316; AAC73316; b0211.
BAA77882; BAA77882; BAA77882.
GeneIDi945694.
KEGGiecj:JW5018.
eco:b0211.
PATRICi32115535. VBIEscCol129921_0213.

Organism-specific databases

EchoBASEiEB0242.
EcoGeneiEG10246. mltD.

Phylogenomic databases

eggNOGiENOG4105E9H. Bacteria.
COG0741. LUCA.
HOGENOMiHOG000258639.
InParanoidiP0AEZ7.
KOiK08307.
OMAiYNPAYNQ.
PhylomeDBiP0AEZ7.

Enzyme and pathway databases

BioCyciEcoCyc:EG10246-MONOMER.
ECOL316407:JW5018-MONOMER.
MetaCyc:EG10246-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AEZ7.
PROiP0AEZ7.

Family and domain databases

Gene3Di3.10.350.10. 2 hits.
InterProiIPR018392. LysM_dom.
IPR023346. Lysozyme-like_dom.
IPR000189. Transglyc_AS.
IPR008258. Transglycosylase_SLT_dom_1.
[Graphical view]
PfamiPF01476. LysM. 2 hits.
PF01464. SLT. 1 hit.
[Graphical view]
SMARTiSM00257. LysM. 2 hits.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
SSF54106. SSF54106. 2 hits.
PROSITEiPS51782. LYSM. 2 hits.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMLTD_ECOLI
AccessioniPrimary (citable) accession number: P0AEZ7
Secondary accession number(s): P23931, P32982, P77350
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: September 7, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be involved in hexaheme nitrite reductase (cytochrome c552) expression.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.