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   27-MAR-2024, entry version 140.
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; Pseudomonadota; 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; 511145-b4392; -.
DR   EnsemblBacteria; AAC77345; AAC77345; b4392.
DR   GeneID; 75202926; -.
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   OrthoDB; 92254at2; -.
DR   PhylomeDB; P0AGC3; -.
DR   BioCyc; EcoCyc:EG10950-MONOMER; -.
DR   BioCyc; MetaCyc:EG10950-MONOMER; -.
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: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   CDD; cd13401; Slt70-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 1.25.20.10; Bacterial muramidases; 1.
DR   Gene3D; 1.10.1240.20; Lytic transglycosylase, superhelical linker domain; 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   PANTHER; PTHR37423:SF2; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR   PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 1.
DR   Pfam; PF01464; SLT; 1.
DR   Pfam; PF14718; SLT_L; 1.
DR   SUPFAM; SSF48435; Bacterial muramidases; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 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
//