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P0AGC3 (SLT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Soluble lytic murein transglycosylase

EC=4.2.2.n1
Alternative name(s):
Exomuramidase
Peptidoglycan lytic exotransglycosylase
Slt70
Gene names
Name:slt
Synonyms:sltY
Ordered Locus Names:b4392, JW4355
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length645 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Murein-degrading enzyme. Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan. May play a role in recycling of muropeptides during cell elongation and/or cell division.

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

Periplasm. Note: Tightly associated with the murein sacculus.

Sequence similarities

Belongs to the transglycosylase Slt family.

Sequence caution

The sequence AAA97288.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.1
Chain28 – 645618Soluble lytic murein transglycosylase
PRO_0000032778

Regions

Region492 – 58291Slt-type domain

Sites

Active site5051

Amino acid modifications

Disulfide bond133 ↔ 166

Experimental info

Mutagenesis5051E → Q: Inactivates the enzyme.
Sequence conflict5831P → L in AAA24634. Ref.1

Secondary structure

........................................................................................... 645
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AGC3 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: F8B0115376E8A947

FASTA64573,353
        10         20         30         40         50         60 
MEKAKQVTWR LLAAGVCLLT VSSVARADSL DEQRSRYAQI KQAWDNRQMD VVEQMMPGLK 

        70         80         90        100        110        120 
DYPLYPYLEY RQITDDLMNQ PAVTVTNFVR ANPTLPPART LQSRFVNELA RREDWRGLLA 

       130        140        150        160        170        180 
FSPEKPGTTE AQCNYYYAKW NTGQSEEAWQ GAKELWLTGK SQPNACDKLF SVWRASGKQD 

       190        200        210        220        230        240 
PLAYLERIRL AMKAGNTGLV TVLAGQMPAD YQTIASAIIS LANNPNTVLT FARTTGATDF 

       250        260        270        280        290        300 
TRQMAAVAFA SVARQDAENA RLMIPSLAQA QQLNEDQIQE LRDIVAWRLM GNDVTDEQAK 

       310        320        330        340        350        360 
WRDDAIMRSQ STSLIERRVR MALGTGDRRG LNTWLARLPM EAKEKDEWRY WQADLLLERG 

       370        380        390        400        410        420 
REAEAKEILH QLMQQRGFYP MVAAQRIGEE YELKIDKAPQ NVDSALTQGP EMARVRELMY 

       430        440        450        460        470        480 
WNLDNTARSE WANLVKSKSK TEQAQLARYA FNNQWWDLSV QATIAGKLWD HLEERFPLAY 

       490        500        510        520        530        540 
NDLFKRYTSG KEIPQSYAMA IARQESAWNP KVKSPVGASG LMQIMPGTAT HTVKMFSIPG 

       550        560        570        580        590        600 
YSSPGQLLDP ETNINIGTSY LQYVYQQFGN NRIFSSAAYN AGPGRVRTWL GNSAGRIDAV 

       610        620        630        640 
AFVESIPFSE TRGYVKNVLA YDAYYRYFMG DKPTLMSATE WGRRY 

« Hide

References

« Hide 'large scale' references
[1]"Murein-metabolizing enzymes from Escherichia coli: sequence analysis and controlled overexpression of the slt gene, which encodes the soluble lytic transglycosylase."
Engel H., Kazemier B., Keck W.
J. Bacteriol. 173:6773-6782(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-41.
[2]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
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 277:1453-1462(1997) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"DNA sequence of the E. coli trpR gene and prediction of the amino acid sequence of Trp repressor."
Singleton C.K., Roeder W.D., Bogosian G., Somerville R.L., Weith H.L.
Nucleic Acids Res. 8:1551-1560(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 549-639.
[6]"Nucleotide sequence and expression of Escherichia coli trpR, the structural gene for the trp aporepressor."
Gunsalus R.P., Yanofsky C.
Proc. Natl. Acad. Sci. U.S.A. 77:7117-7121(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 640-645.
[7]"Molecular cloning, overexpression and mapping of the slt gene encoding the soluble lytic transglycosylase of Escherichia coli."
Betzner A.S., Keck W.
Mol. Gen. Genet. 219:489-491(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE MAPPING.
[8]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[9]"Crystallization of the soluble lytic transglycosylase from Escherichia coli K12."
Rozeboom H.J., Dijkstra B.W., Engel H., Keck W.
J. Mol. Biol. 212:557-559(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Strain: K12.
[10]"Doughnut-shaped structure of a bacterial muramidase revealed by X-ray crystallography."
Thunnissen A.-M.W.H., Dijkstra A.J., Kalk K.H., Rozeboom H.J., Engel H., Keck W., Dijkstra B.W.
Nature 367:750-753(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[11]"Structure of the 70-kDa soluble lytic transglycosylase complexed with bulgecin A. Implications for the enzymatic mechanism."
Thunnissen A.-M.W.H., Rozeboom H.J., Kalk K.H., Dijkstra B.W.
Biochemistry 34:12729-12737(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[12]"High resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment."
van Asselt E.J., Thunnissen A.-M.W.H., Dijkstra B.W.
J. Mol. Biol. 291:877-898(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M69185 Genomic DNA. Translation: AAA24634.1.
U14003 Genomic DNA. Translation: AAA97288.1. Different initiation.
U00096 Genomic DNA. Translation: AAC77345.2.
AP009048 Genomic DNA. Translation: BAE78381.1.
J01715 Genomic DNA. No translation available.
PIRQQECW1. S56616.
RefSeqNP_418809.4. NC_000913.3.
YP_492522.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QSAX-ray1.65A28-645[»]
1QTEX-ray1.90A28-645[»]
1SLYX-ray2.80A28-645[»]
ProteinModelPortalP0AGC3.
SMRP0AGC3. Positions 28-645.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0AGC3. 5 interactions.
STRING511145.b4392.

Protein family/group databases

CAZyGH23. Glycoside Hydrolase Family 23.

Proteomic databases

PaxDbP0AGC3.
PRIDEP0AGC3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77345; AAC77345; b4392.
BAE78381; BAE78381; BAE78381.
GeneID12931805.
948908.
KEGGecj:Y75_p4276.
eco:b4392.
PATRIC32124402. VBIEscCol129921_4541.

Organism-specific databases

EchoBASEEB0943.
EcoGeneEG10950. slt.

Phylogenomic databases

eggNOGCOG0741.
HOGENOMHOG000275388.
KOK08309.
OMAQPAACDT.
OrthoDBEOG6S52QZ.
PhylomeDBP0AGC3.

Enzyme and pathway databases

BioCycEcoCyc:EG10950-MONOMER.
ECOL316407:JW4355-MONOMER.
MetaCyc:EG10950-MONOMER.

Gene expression databases

GenevestigatorP0AGC3.

Family and domain databases

Gene3D1.10.1240.20. 1 hit.
1.25.20.10. 1 hit.
InterProIPR023346. Lysozyme-like_dom.
IPR016026. Lytic_TGlyclase_suprhlx_U/L.
IPR012289. Lytic_TGlycosylase_superhlx_L.
IPR008939. Lytic_TGlycosylase_superhlx_U.
IPR008258. TGlycosylase-like_SLT.
IPR000189. Transglyc_AS.
[Graphical view]
PfamPF01464. SLT. 1 hit.
PF14718. SLT_L. 1 hit.
[Graphical view]
SUPFAMSSF48435. SSF48435. 1 hit.
SSF53955. SSF53955. 1 hit.
PROSITEPS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AGC3.
PROP0AGC3.

Entry information

Entry nameSLT_ECOLI
AccessionPrimary (citable) accession number: P0AGC3
Secondary accession number(s): P03810 expand/collapse secondary AC list , P76820, Q2M5S5, Q8XB18
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 20, 2005
Last modified: May 14, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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