SLT_ECO57
ID SLT_ECO57 Reviewed; 645 AA.
AC P0AGC4; P03810; P76820; Q8XB18;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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; OrderedLocusNames=Z5994, ECs5350;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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 (By similarity).
CC {ECO:0000250}.
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 {ECO:0000250}. Note=Tightly associated
CC with the murein sacculus. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG59572.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB38773.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG59572.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB38773.1; ALT_INIT; Genomic_DNA.
DR PIR; F91297; F91297.
DR PIR; H86138; H86138.
DR RefSeq; NP_313377.2; NC_002695.1.
DR RefSeq; WP_000409451.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AGC4; -.
DR SMR; P0AGC4; -.
DR STRING; 155864.EDL933_5736; -.
DR EnsemblBacteria; AAG59572; AAG59572; Z5994.
DR EnsemblBacteria; BAB38773; BAB38773; ECs_5350.
DR GeneID; 66671720; -.
DR GeneID; 913492; -.
DR KEGG; ece:Z5994; -.
DR KEGG; ecs:ECs_5350; -.
DR PATRIC; fig|386585.9.peg.5598; -.
DR eggNOG; COG0741; Bacteria.
DR HOGENOM; CLU_019016_1_1_6; -.
DR OMA; RQESAFM; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
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 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Disulfide bond; Lyase; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..645
FT /note="Soluble lytic murein transglycosylase"
FT /id="PRO_0000045261"
FT REGION 492..582
FT /note="Slt-type domain"
FT ACT_SITE 505
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10071"
FT DISULFID 133..166
FT /evidence="ECO:0000250"
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
