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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)DescriptionActionsGraphical viewLength
Active sitei5051

GO - Molecular functioni

  • exo-oligoalginate lyase activity Source: UniProtKB-EC
  • gellan lyase activity Source: UniProtKB-EC
  • hydrolase activity, hydrolyzing O-glycosyl compounds Source: EcoCyc
  • lytic transglycosylase activity Source: EcoliWiki

GO - Biological processi

  • cell wall organization Source: UniProtKB-KW
  • peptidoglycan catabolic process Source: EcoCyc
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10950. slt.

Subcellular locationi

  • Periplasm

  • Note: Tightly associated with the murein sacculus.

GO - Cellular componenti

  • membrane Source: InterPro
  • outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi505E → Q: Inactivates the enzyme. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 271 PublicationAdd BLAST27
ChainiPRO_000003277828 – 645Soluble lytic murein transglycosylaseAdd BLAST618

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi133 ↔ 166

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP0AGC3.
PRIDEiP0AGC3.

Interactioni

Protein-protein interaction databases

BioGridi4260799. 185 interactors.
IntActiP0AGC3. 5 interactors.
STRINGi511145.b4392.

Structurei

Secondary structure

1645
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 45Combined sources16
Helixi49 – 55Combined sources7
Helixi57 – 59Combined sources3
Helixi65 – 75Combined sources11
Helixi76 – 79Combined sources4
Helixi82 – 91Combined sources10
Helixi96 – 111Combined sources16
Helixi115 – 121Combined sources7
Helixi129 – 141Combined sources13
Helixi145 – 156Combined sources12
Helixi166 – 175Combined sources10
Helixi181 – 193Combined sources13
Helixi197 – 205Combined sources9
Helixi209 – 211Combined sources3
Helixi212 – 223Combined sources12
Helixi225 – 227Combined sources3
Helixi228 – 234Combined sources7
Helixi239 – 255Combined sources17
Helixi257 – 270Combined sources14
Helixi275 – 287Combined sources13
Beta strandi291 – 293Combined sources3
Helixi296 – 307Combined sources12
Helixi312 – 324Combined sources13
Helixi328 – 337Combined sources10
Helixi342 – 344Combined sources3
Helixi346 – 358Combined sources13
Helixi362 – 373Combined sources12
Helixi378 – 386Combined sources9
Helixi405 – 408Combined sources4
Helixi410 – 420Combined sources11
Helixi424 – 435Combined sources12
Helixi440 – 452Combined sources13
Helixi456 – 465Combined sources10
Helixi472 – 475Combined sources4
Helixi481 – 488Combined sources8
Beta strandi491 – 493Combined sources3
Helixi495 – 506Combined sources12
Turni520 – 523Combined sources4
Helixi526 – 536Combined sources11
Helixi544 – 548Combined sources5
Helixi550 – 567Combined sources18
Turni568 – 570Combined sources3
Helixi572 – 581Combined sources10
Helixi583 – 593Combined sources11
Helixi599 – 605Combined sources7
Helixi609 – 628Combined sources20
Helixi638 – 642Combined sources5

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0AGC3.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni492 – 582Slt-type domainAdd BLAST91

Sequence similaritiesi

Belongs to the transglycosylase Slt family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107SC1. Bacteria.
COG0741. LUCA.
HOGENOMiHOG000275388.
InParanoidiP0AGC3.
KOiK08309.
OMAiVDWHERY.
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.
IPR000189. Transglyc_AS.
IPR008258. Transglycosylase_SLT_dom_1.
[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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti583P → L in AAA24634 (PubMed:1938883).Curated1

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.
WP_000409451.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77345; AAC77345; b4392.
BAE78381; BAE78381; BAE78381.
GeneIDi948908.
KEGGiecj:JW4355.
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.
WP_000409451.1. NZ_LN832404.1.

3D structure databases

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

Protein-protein interaction databases

BioGridi4260799. 185 interactors.
IntActiP0AGC3. 5 interactors.
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.
GeneIDi948908.
KEGGiecj:JW4355.
eco:b4392.
PATRICi32124402. VBIEscCol129921_4541.

Organism-specific databases

EchoBASEiEB0943.
EcoGeneiEG10950. slt.

Phylogenomic databases

eggNOGiENOG4107SC1. Bacteria.
COG0741. LUCA.
HOGENOMiHOG000275388.
InParanoidiP0AGC3.
KOiK08309.
OMAiVDWHERY.
PhylomeDBiP0AGC3.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0AGC3.
PROiP0AGC3.

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.
IPR000189. Transglyc_AS.
IPR008258. Transglycosylase_SLT_dom_1.
[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...

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: November 30, 2016
This is version 99 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

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.