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P0AGC3

- SLT_ECOLI

UniProt

P0AGC3 - SLT_ECOLI

Protein

Soluble lytic murein transglycosylase

Gene

slt

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (20 Dec 2005)
      Previous versions | rss
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    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. peptidoglycan metabolic process Source: InterPro

    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10950. slt.

    Subcellular locationi

    Periplasm
    Note: Tightly associated with the murein sacculus.

    GO - Cellular componenti

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

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK08309.
    OMAiQPAACDT.
    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

    MEKAKQVTWR LLAAGVCLLT VSSVARADSL DEQRSRYAQI KQAWDNRQMD    50
    VVEQMMPGLK DYPLYPYLEY RQITDDLMNQ PAVTVTNFVR ANPTLPPART 100
    LQSRFVNELA RREDWRGLLA FSPEKPGTTE AQCNYYYAKW NTGQSEEAWQ 150
    GAKELWLTGK SQPNACDKLF SVWRASGKQD PLAYLERIRL AMKAGNTGLV 200
    TVLAGQMPAD YQTIASAIIS LANNPNTVLT FARTTGATDF TRQMAAVAFA 250
    SVARQDAENA RLMIPSLAQA QQLNEDQIQE LRDIVAWRLM GNDVTDEQAK 300
    WRDDAIMRSQ STSLIERRVR MALGTGDRRG LNTWLARLPM EAKEKDEWRY 350
    WQADLLLERG REAEAKEILH QLMQQRGFYP MVAAQRIGEE YELKIDKAPQ 400
    NVDSALTQGP EMARVRELMY WNLDNTARSE WANLVKSKSK TEQAQLARYA 450
    FNNQWWDLSV QATIAGKLWD HLEERFPLAY NDLFKRYTSG KEIPQSYAMA 500
    IARQESAWNP KVKSPVGASG LMQIMPGTAT HTVKMFSIPG YSSPGQLLDP 550
    ETNINIGTSY LQYVYQQFGN NRIFSSAAYN AGPGRVRTWL GNSAGRIDAV 600
    AFVESIPFSE TRGYVKNVLA YDAYYRYFMG DKPTLMSATE WGRRY 645
    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.

    Experimental Info

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    PIRi S56616. QQECW1.
    RefSeqi NP_418809.4. NC_000913.3.
    YP_492522.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QSA X-ray 1.65 A 28-645 [» ]
    1QTE X-ray 1.90 A 28-645 [» ]
    1SLY X-ray 2.80 A 28-645 [» ]
    ProteinModelPortali P0AGC3.
    SMRi P0AGC3. Positions 28-645.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P0AGC3. 5 interactions.
    STRINGi 511145.b4392.

    Protein family/group databases

    CAZyi GH23. Glycoside Hydrolase Family 23.

    Proteomic databases

    PaxDbi P0AGC3.
    PRIDEi P0AGC3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77345 ; AAC77345 ; b4392 .
    BAE78381 ; BAE78381 ; BAE78381 .
    GeneIDi 12931805.
    948908.
    KEGGi ecj:Y75_p4276.
    eco:b4392.
    PATRICi 32124402. VBIEscCol129921_4541.

    Organism-specific databases

    EchoBASEi EB0943.
    EcoGenei EG10950. slt.

    Phylogenomic databases

    eggNOGi COG0741.
    HOGENOMi HOG000275388.
    KOi K08309.
    OMAi QPAACDT.
    OrthoDBi EOG6S52QZ.
    PhylomeDBi P0AGC3.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10950-MONOMER.
    ECOL316407:JW4355-MONOMER.
    MetaCyc:EG10950-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AGC3.
    PROi P0AGC3.

    Gene expression databases

    Genevestigatori P0AGC3.

    Family and domain databases

    Gene3Di 1.10.1240.20. 1 hit.
    1.25.20.10. 1 hit.
    InterProi IPR023346. 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 ]
    Pfami PF01464. SLT. 1 hit.
    PF14718. SLT_L. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48435. SSF48435. 1 hit.
    SSF53955. SSF53955. 1 hit.
    PROSITEi PS00922. TRANSGLYCOSYLASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 85 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