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Protein

Soluble lytic murein transglycosylase

Gene

slt

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

Functioni

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 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 sitei505 – 5051

GO - Molecular functioni

  1. carbon-oxygen lyase activity, acting on polysaccharides Source: UniProtKB-EC
  2. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro
  3. lytic transglycosylase activity Source: EcoliWiki

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. peptidoglycan metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

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

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

Names & Taxonomyi

Protein namesi
Recommended name:
Soluble lytic murein transglycosylase (EC:4.2.2.n1)
Alternative name(s):
Exomuramidase
Peptidoglycan lytic exotransglycosylase
Slt70
Gene namesi
Name:slt
Synonyms:sltY
Ordered Locus Names:b4392, JW4355
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10950. slt.

Subcellular locationi

  1. Periplasm

  2. Note: Tightly associated with the murein sacculus.

GO - Cellular componenti

  1. membrane Source: InterPro
  2. outer membrane-bounded periplasmic space Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi505 – 5051E → Q: Inactivates the enzyme.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Chaini28 – 645618Soluble lytic murein transglycosylasePRO_0000032778Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi133 ↔ 166

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP0AGC3.
PRIDEiP0AGC3.

Expressioni

Gene expression databases

GenevestigatoriP0AGC3.

Interactioni

Protein-protein interaction databases

IntActiP0AGC3. 5 interactions.
STRINGi511145.b4392.

Structurei

Secondary structure

1
645
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 4516Combined sources
Helixi49 – 557Combined sources
Helixi57 – 593Combined sources
Helixi65 – 7511Combined sources
Helixi76 – 794Combined sources
Helixi82 – 9110Combined sources
Helixi96 – 11116Combined sources
Helixi115 – 1217Combined sources
Helixi129 – 14113Combined sources
Helixi145 – 15612Combined sources
Helixi166 – 17510Combined sources
Helixi181 – 19313Combined sources
Helixi197 – 2059Combined sources
Helixi209 – 2113Combined sources
Helixi212 – 22312Combined sources
Helixi225 – 2273Combined sources
Helixi228 – 2347Combined sources
Helixi239 – 25517Combined sources
Helixi257 – 27014Combined sources
Helixi275 – 28713Combined sources
Beta strandi291 – 2933Combined sources
Helixi296 – 30712Combined sources
Helixi312 – 32413Combined sources
Helixi328 – 33710Combined sources
Helixi342 – 3443Combined sources
Helixi346 – 35813Combined sources
Helixi362 – 37312Combined sources
Helixi378 – 3869Combined sources
Helixi405 – 4084Combined sources
Helixi410 – 42011Combined sources
Helixi424 – 43512Combined sources
Helixi440 – 45213Combined sources
Helixi456 – 46510Combined sources
Helixi472 – 4754Combined sources
Helixi481 – 4888Combined sources
Beta strandi491 – 4933Combined sources
Helixi495 – 50612Combined sources
Turni520 – 5234Combined sources
Helixi526 – 53611Combined sources
Helixi544 – 5485Combined sources
Helixi550 – 56718Combined sources
Turni568 – 5703Combined sources
Helixi572 – 58110Combined sources
Helixi583 – 59311Combined sources
Helixi599 – 6057Combined sources
Helixi609 – 62820Combined sources
Helixi638 – 6425Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QSAX-ray1.65A28-645[»]
1QTEX-ray1.90A28-645[»]
1SLYX-ray2.80A28-645[»]
ProteinModelPortaliP0AGC3.
SMRiP0AGC3. Positions 28-645.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AGC3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni492 – 58291Slt-type domainAdd
BLAST

Sequence similaritiesi

Belongs to the transglycosylase Slt family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0741.
HOGENOMiHOG000275388.
InParanoidiP0AGC3.
KOiK08309.
OMAiVDWHERY.
OrthoDBiEOG6S52QZ.
PhylomeDBiP0AGC3.

Family and domain databases

Gene3Di1.10.1240.20. 1 hit.
1.25.20.10. 1 hit.
InterProiIPR023346. 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]
PfamiPF01464. SLT. 1 hit.
PF14718. SLT_L. 1 hit.
[Graphical view]
SUPFAMiSSF48435. SSF48435. 1 hit.
SSF53955. SSF53955. 1 hit.
PROSITEiPS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0AGC3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKAKQVTWR LLAAGVCLLT VSSVARADSL DEQRSRYAQI KQAWDNRQMD
60 70 80 90 100
VVEQMMPGLK DYPLYPYLEY RQITDDLMNQ PAVTVTNFVR ANPTLPPART
110 120 130 140 150
LQSRFVNELA RREDWRGLLA FSPEKPGTTE AQCNYYYAKW NTGQSEEAWQ
160 170 180 190 200
GAKELWLTGK SQPNACDKLF SVWRASGKQD PLAYLERIRL AMKAGNTGLV
210 220 230 240 250
TVLAGQMPAD YQTIASAIIS LANNPNTVLT FARTTGATDF TRQMAAVAFA
260 270 280 290 300
SVARQDAENA RLMIPSLAQA QQLNEDQIQE LRDIVAWRLM GNDVTDEQAK
310 320 330 340 350
WRDDAIMRSQ STSLIERRVR MALGTGDRRG LNTWLARLPM EAKEKDEWRY
360 370 380 390 400
WQADLLLERG REAEAKEILH QLMQQRGFYP MVAAQRIGEE YELKIDKAPQ
410 420 430 440 450
NVDSALTQGP EMARVRELMY WNLDNTARSE WANLVKSKSK TEQAQLARYA
460 470 480 490 500
FNNQWWDLSV QATIAGKLWD HLEERFPLAY NDLFKRYTSG KEIPQSYAMA
510 520 530 540 550
IARQESAWNP KVKSPVGASG LMQIMPGTAT HTVKMFSIPG YSSPGQLLDP
560 570 580 590 600
ETNINIGTSY LQYVYQQFGN NRIFSSAAYN AGPGRVRTWL GNSAGRIDAV
610 620 630 640
AFVESIPFSE TRGYVKNVLA YDAYYRYFMG DKPTLMSATE WGRRY
Length:645
Mass (Da):73,353
Last modified:December 20, 2005 - v1
Checksum:iF8B0115376E8A947
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti583 – 5831P → L in AAA24634 (PubMed:1938883).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS56616. QQECW1.
RefSeqiNP_418809.4. NC_000913.3.
YP_492522.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77345; AAC77345; b4392.
BAE78381; BAE78381; BAE78381.
GeneIDi12931805.
948908.
KEGGiecj:Y75_p4276.
eco:b4392.
PATRICi32124402. VBIEscCol129921_4541.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS56616. QQECW1.
RefSeqiNP_418809.4. NC_000913.3.
YP_492522.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QSAX-ray1.65A28-645[»]
1QTEX-ray1.90A28-645[»]
1SLYX-ray2.80A28-645[»]
ProteinModelPortaliP0AGC3.
SMRiP0AGC3. Positions 28-645.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0AGC3. 5 interactions.
STRINGi511145.b4392.

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

Proteomic databases

PaxDbiP0AGC3.
PRIDEiP0AGC3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77345; AAC77345; b4392.
BAE78381; BAE78381; BAE78381.
GeneIDi12931805.
948908.
KEGGiecj:Y75_p4276.
eco:b4392.
PATRICi32124402. VBIEscCol129921_4541.

Organism-specific databases

EchoBASEiEB0943.
EcoGeneiEG10950. slt.

Phylogenomic databases

eggNOGiCOG0741.
HOGENOMiHOG000275388.
InParanoidiP0AGC3.
KOiK08309.
OMAiVDWHERY.
OrthoDBiEOG6S52QZ.
PhylomeDBiP0AGC3.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0AGC3.
PROiP0AGC3.

Gene expression databases

GenevestigatoriP0AGC3.

Family and domain databases

Gene3Di1.10.1240.20. 1 hit.
1.25.20.10. 1 hit.
InterProiIPR023346. 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]
PfamiPF01464. SLT. 1 hit.
PF14718. SLT_L. 1 hit.
[Graphical view]
SUPFAMiSSF48435. SSF48435. 1 hit.
SSF53955. SSF53955. 1 hit.
PROSITEiPS00922. TRANSGLYCOSYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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).

Entry informationi

Entry nameiSLT_ECOLI
AccessioniPrimary (citable) accession number: P0AGC3
Secondary accession number(s): P03810
, P76820, Q2M5S5, Q8XB18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 20, 2005
Last modified: January 7, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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

External Data

Dasty 3

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 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.