SLT_ECOLI
ID SLT_ECOLI Reviewed; 645 AA.
AC P0AGC3; P03810; P76820; Q2M5S5; Q8XB18;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Soluble lytic murein transglycosylase;
DE EC=4.2.2.n1;
DE AltName: Full=Exomuramidase;
DE AltName: Full=Peptidoglycan lytic exotransglycosylase;
DE AltName: Full=Slt70;
DE Flags: Precursor;
GN Name=slt; Synonyms=sltY; OrderedLocusNames=b4392, JW4355;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-41.
RX PubMed=1938883; DOI=10.1128/jb.173.21.6773-6782.1991;
RA Engel H., Kazemier B., Keck W.;
RT "Murein-metabolizing enzymes from Escherichia coli: sequence analysis and
RT controlled overexpression of the slt gene, which encodes the soluble lytic
RT transglycosylase.";
RL J. Bacteriol. 173:6773-6782(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 549-639.
RX PubMed=7001368; DOI=10.1093/nar/8.7.1551;
RA Singleton C.K., Roeder W.D., Bogosian G., Somerville R.L., Weith H.L.;
RT "DNA sequence of the E. coli trpR gene and prediction of the amino acid
RT sequence of Trp repressor.";
RL Nucleic Acids Res. 8:1551-1560(1980).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 640-645.
RX PubMed=7012834; DOI=10.1073/pnas.77.12.7117;
RA Gunsalus R.P., Yanofsky C.;
RT "Nucleotide sequence and expression of Escherichia coli trpR, the
RT structural gene for the trp aporepressor.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:7117-7121(1980).
RN [7]
RP GENE MAPPING.
RX PubMed=2695826; DOI=10.1007/bf00259625;
RA Betzner A.S., Keck W.;
RT "Molecular cloning, overexpression and mapping of the slt gene encoding the
RT soluble lytic transglycosylase of Escherichia coli.";
RL Mol. Gen. Genet. 219:489-491(1989).
RN [8]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RC STRAIN=K12;
RX PubMed=2184239; DOI=10.1016/0022-2836(90)90221-7;
RA Rozeboom H.J., Dijkstra B.W., Engel H., Keck W.;
RT "Crystallization of the soluble lytic transglycosylase from Escherichia
RT coli K12.";
RL J. Mol. Biol. 212:557-559(1990).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=8107871; DOI=10.1038/367750a0;
RA Thunnissen A.-M.W.H., Dijkstra A.J., Kalk K.H., Rozeboom H.J., Engel H.,
RA Keck W., Dijkstra B.W.;
RT "Doughnut-shaped structure of a bacterial muramidase revealed by X-ray
RT crystallography.";
RL Nature 367:750-753(1994).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=7548026; DOI=10.1021/bi00039a032;
RA Thunnissen A.-M.W.H., Rozeboom H.J., Kalk K.H., Dijkstra B.W.;
RT "Structure of the 70-kDa soluble lytic transglycosylase complexed with
RT bulgecin A. Implications for the enzymatic mechanism.";
RL Biochemistry 34:12729-12737(1995).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=10452894; DOI=10.1006/jmbi.1999.3013;
RA van Asselt E.J., Thunnissen A.-M.W.H., Dijkstra B.W.;
RT "High resolution crystal structures of the Escherichia coli lytic
RT transglycosylase Slt70 and its complex with a peptidoglycan fragment.";
RL J. Mol. Biol. 291:877-898(1999).
CC -!- FUNCTION: Murein-degrading enzyme. Catalyzes the cleavage of the
CC glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine
CC residues in peptidoglycan. May play a role in recycling of muropeptides
CC during cell elongation and/or cell division.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage
CC between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC (GlcNAc) residues in peptidoglycan, from either the reducing or the
CC non-reducing ends of the peptidoglycan chains, with concomitant
CC formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n1;
CC -!- SUBCELLULAR LOCATION: Periplasm. Note=Tightly associated with the
CC murein sacculus.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97288.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M69185; AAA24634.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97288.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77345.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78381.1; -; Genomic_DNA.
DR EMBL; J01715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S56616; QQECW1.
DR RefSeq; NP_418809.4; NC_000913.3.
DR RefSeq; WP_000409451.1; NZ_STEB01000033.1.
DR PDB; 1QSA; X-ray; 1.65 A; A=28-645.
DR PDB; 1QTE; X-ray; 1.90 A; A=28-645.
DR PDB; 1SLY; X-ray; 2.80 A; A=28-645.
DR PDBsum; 1QSA; -.
DR PDBsum; 1QTE; -.
DR PDBsum; 1SLY; -.
DR AlphaFoldDB; P0AGC3; -.
DR SMR; P0AGC3; -.
DR BioGRID; 4260799; 206.
DR IntAct; P0AGC3; 5.
DR STRING; 511145.b4392; -.
DR DrugBank; DB02595; (2R,3S,5S)-2-(Hydroxymethyl)-5-[(2-sulfoethyl)carbamoyl]-3-pyrrolidiniumyl 2-acetamido-2-deoxy-4-O-sulfo-beta-D-glucopyranoside.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR jPOST; P0AGC3; -.
DR PaxDb; P0AGC3; -.
DR PRIDE; P0AGC3; -.
DR EnsemblBacteria; AAC77345; AAC77345; b4392.
DR EnsemblBacteria; BAE78381; BAE78381; BAE78381.
DR GeneID; 66671720; -.
DR GeneID; 948908; -.
DR KEGG; ecj:JW4355; -.
DR KEGG; eco:b4392; -.
DR PATRIC; fig|1411691.4.peg.2292; -.
DR EchoBASE; EB0943; -.
DR eggNOG; COG0741; Bacteria.
DR HOGENOM; CLU_019016_1_1_6; -.
DR InParanoid; P0AGC3; -.
DR OMA; RQESAFM; -.
DR PhylomeDB; P0AGC3; -.
DR BioCyc; EcoCyc:EG10950-MON; -.
DR BioCyc; MetaCyc:EG10950-MON; -.
DR EvolutionaryTrace; P0AGC3; -.
DR PRO; PR:P0AGC3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; IDA:EcoCyc.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0008932; F:lytic endotransglycosylase activity; IDA:EcoCyc.
DR GO; GO:0008933; F:lytic transglycosylase activity; IDA:EcoliWiki.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IDA:EcoCyc.
DR Gene3D; 1.10.1240.20; -; 1.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR037061; Lytic_TGlycoase_superhlx_L_sf.
DR InterPro; IPR012289; Lytic_TGlycosylase_superhlx_L.
DR InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
DR InterPro; IPR000189; Transglyc_AS.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR Pfam; PF01464; SLT; 1.
DR Pfam; PF14718; SLT_L; 1.
DR SUPFAM; SSF48435; SSF48435; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Disulfide bond; Lyase; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:1938883"
FT CHAIN 28..645
FT /note="Soluble lytic murein transglycosylase"
FT /id="PRO_0000032778"
FT REGION 492..582
FT /note="Slt-type domain"
FT ACT_SITE 505
FT DISULFID 133..166
FT MUTAGEN 505
FT /note="E->Q: Inactivates the enzyme."
FT CONFLICT 583
FT /note="P -> L (in Ref. 1; AAA24634)"
FT /evidence="ECO:0000305"
FT HELIX 30..45
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 96..111
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 129..141
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 145..156
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 212..223
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 239..255
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 257..270
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 275..287
FT /evidence="ECO:0007829|PDB:1QSA"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1QTE"
FT HELIX 296..307
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 312..324
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 346..358
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 362..373
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 378..386
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 410..420
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 424..435
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 440..452
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 456..465
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 472..475
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 481..488
FT /evidence="ECO:0007829|PDB:1QSA"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 495..506
FT /evidence="ECO:0007829|PDB:1QSA"
FT TURN 520..523
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 526..536
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 544..548
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 550..567
FT /evidence="ECO:0007829|PDB:1QSA"
FT TURN 568..570
FT /evidence="ECO:0007829|PDB:1SLY"
FT HELIX 572..581
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 583..593
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 599..605
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 609..628
FT /evidence="ECO:0007829|PDB:1QSA"
FT HELIX 638..642
FT /evidence="ECO:0007829|PDB:1QSA"
SQ SEQUENCE 645 AA; 73353 MW; F8B0115376E8A947 CRC64;
MEKAKQVTWR LLAAGVCLLT VSSVARADSL DEQRSRYAQI KQAWDNRQMD VVEQMMPGLK
DYPLYPYLEY RQITDDLMNQ PAVTVTNFVR ANPTLPPART LQSRFVNELA RREDWRGLLA
FSPEKPGTTE AQCNYYYAKW NTGQSEEAWQ GAKELWLTGK SQPNACDKLF SVWRASGKQD
PLAYLERIRL AMKAGNTGLV TVLAGQMPAD YQTIASAIIS LANNPNTVLT FARTTGATDF
TRQMAAVAFA SVARQDAENA RLMIPSLAQA QQLNEDQIQE LRDIVAWRLM GNDVTDEQAK
WRDDAIMRSQ STSLIERRVR MALGTGDRRG LNTWLARLPM EAKEKDEWRY WQADLLLERG
REAEAKEILH QLMQQRGFYP MVAAQRIGEE YELKIDKAPQ NVDSALTQGP EMARVRELMY
WNLDNTARSE WANLVKSKSK TEQAQLARYA FNNQWWDLSV QATIAGKLWD HLEERFPLAY
NDLFKRYTSG KEIPQSYAMA IARQESAWNP KVKSPVGASG LMQIMPGTAT HTVKMFSIPG
YSSPGQLLDP ETNINIGTSY LQYVYQQFGN NRIFSSAAYN AGPGRVRTWL GNSAGRIDAV
AFVESIPFSE TRGYVKNVLA YDAYYRYFMG DKPTLMSATE WGRRY
