Membrane-bound lytic murein transglycosylase D precursor

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P0AEZ7 (MLTD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Membrane-bound lytic murein transglycosylase D
EC=4.2.2.n1

Alternative name(s):
Murein hydrolase D
Regulatory protein dniR

Gene names

Name:	mltD
Synonyms:	dniR, yafG
Ordered Locus Names:	b0211, JW5018

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division By similarity.
Catalytic activity	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.
Subcellular location	Cell membrane; Lipid-anchor Probable.
Domain	LysM repeats are thought to be involved in peptidoglycan binding.
Sequence similarities	Belongs to the transglycosylase slt family. Contains 2 LysM repeats.
Caution	Was originally (Ref.5) thought to be involved in hexaheme nitrite reductase (cytochrome c552) expression.
Sequence caution	The sequence CAA43144.1 differs from that shown. Reason: Frameshift at positions 55, 87 and 226.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cell membrane Membrane
Domain	Repeat Signal
Molecular function	Lyase
PTM	Lipoprotein Palmitate
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	carbon-oxygen lyase activity, acting on polysaccharides Inferred from electronic annotation. Source: EC lytic transglycosylase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 15

Potential

Chain

16 – 452

437

Membrane-bound lytic murein transglycosylase D

PRO_0000032801

Regions

Repeat

343 – 385

LysM 1

Repeat

402 – 443

LysM 2

Region

113 – 198

Slt-type domain

Sites

Active site

125

By similarity

Amino acid modifications

Lipidation

N-palmitoyl cysteine Potential

Lipidation

S-diacylglycerol cysteine Potential

Experimental info

Sequence conflict

69 – 72

MGIP → DGNS Ref.5

Sequence conflict

217

D → A Ref.5

Secondary structure

452

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AEZ7 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 80CD5BBE5F5949E8
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FASTA

452

49,417

        10         20         30         40         50         60 
MKAKAILLAS VLLVGCQSTG NVQQHAQSLS AAGQGEAAKF TSQARWMDDG TSIAPDGDLW 

        70         80         90        100        110        120 
AFIGDELKMG IPENDRIREQ KQKYLRNKSY LHDVTLRAEP YMYWIAGQVK KRNMPMELVL 

       130        140        150        160        170        180 
LPIVESAFDP HATSGANAAG IWQIIPSTGR NYGLKQTRNY DARRDVVAST TAALNMMQRL 

       190        200        210        220        230        240 
NKMFDGDWLL TVAAYNSGEG RVMKAIKTNK ARGKSTDFWS LPLPQETKQY VPKMLALSDI 

       250        260        270        280        290        300 
LKNSKRYGVR LPTTDESRAL ARVHLSSPVE MAKVADMAGI SVSKLKTFNA GVKGSTLGAS 

       310        320        330        340        350        360 
GPQYVMVPKK HADQLRESLA SGEIAAVQST LVADNTPLNS RVYTVRSGDT LSSIASRLGV 

       370        380        390        400        410        420 
STKDLQQWNK LRGSKLKPGQ SLTIGAGSSA QRLANNSDSI TYRVRKGDSL SSIAKRHGVN 

       430        440        450 
IKDVMRWNSD TANLQPGDKL TLFVKNNNMP DS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region." Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Molecular cloning and DNA sequence of dniR, a gene affecting anaerobic expression of the Escherichia coli hexaheme nitrite reductase." Kajie S., Ideta R., Yamato I., Anraku Y. FEMS Microbiol. Lett. 67:205-211(1991) [PubMed: 1663890] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-452. Strain: K12.
[6]	"A conserved domain in putative bacterial and bacteriophage transglycosylases." Koonin E.V., Rudd K.E. Trends Biochem. Sci. 19:106-107(1994) [PubMed: 8203016] [Abstract] Cited for: SIMILARITY TO SLT.
[7]	"The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD)." Bateman A., Bycroft M. J. Mol. Biol. 299:1113-1119(2000) [PubMed: 10843862] [Abstract] Cited for: STRUCTURE BY NMR OF 398-445.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

E64745.

RefSeq

NP_414747.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E0G	NMR	-	A	398-445	[»]

ProteinModelPortal

P0AEZ7.

SMR

P0AEZ7. Positions 99-249, 340-386, 398-445.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48010N.

IntAct

P0AEZ7. 4 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000002923; EBESCP00000002923; EBESCG00000002388.
EBESCT00000015861; EBESCP00000015152; EBESCG00000014921.

GeneID

945694.

GenomeReviews

Gene locus JW5018 in contig AP009048_GR.
Gene locus b0211 in contig U00096_GR.

KEGG

ecj:JW5018.
eco:b0211.

PATRIC

32115535. VBIEscCol129921_0213.

Organism-specific databases

EchoBASE

EB0242.

EcoGene

EG10246. mltD.

Phylogenomic databases

eggNOG

COG0741.

GeneTree

EBGT00050000011852.

HOGENOM

HBG519241.

OMA

YAIAAYN.

PhylomeDB

P0AEZ7.

ProtClustDB

PRK10783.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10246-MONOMER.

Gene expression databases

Genevestigator

P0AEZ7.

Family and domain databases

InterPro

IPR023346. Lysozyme-like_dom.
IPR008258. Lytic_TGlycosylase-like_cat.
IPR018392. Peptidoglycan-bd_lysin.
IPR002482. Peptidoglycan-bd_Lysin_subgr.
IPR000189. Transglyc_AS.
[Graphical view]

K08307.

Pfam

PF01476. LysM. 2 hits.
PF01464. SLT. 1 hit.
[Graphical view]

SMART

SM00257. LysM. 2 hits.
[Graphical view]

SUPFAM

SSF53955. SSF53955. 1 hit.

PROSITE

PS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MLTD_ECOLI

Accession

Primary (citable) accession number: P0AEZ7
Secondary accession number(s): P23931, P32982, P77350

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents