ID   SLT_SALTY               Reviewed;         645 AA.
AC   P39434;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   19-DEC-2001, sequence version 2.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=Soluble lytic murein transglycosylase;
DE            EC=4.2.2.n1;
DE   AltName: Full=Peptidoglycan lytic exotransglycosylase;
DE   AltName: Full=Slt70;
DE   Flags: Precursor;
GN   Name=slt; OrderedLocusNames=STM4582;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(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:0000305}.
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL23397.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE006468; AAL23397.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_463438.3; NC_003197.2.
DR   AlphaFoldDB; P39434; -.
DR   SMR; P39434; -.
DR   STRING; 99287.STM4582; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   PaxDb; P39434; -.
DR   EnsemblBacteria; AAL23397; AAL23397; STM4582.
DR   GeneID; 1256108; -.
DR   KEGG; stm:STM4582; -.
DR   PATRIC; fig|99287.12.peg.4825; -.
DR   HOGENOM; CLU_019016_1_1_6; -.
DR   OMA; RQESAFM; -.
DR   PhylomeDB; P39434; -.
DR   Proteomes; UP000001014; 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:0000255"
FT   CHAIN           28..645
FT                   /note="Soluble lytic murein transglycosylase"
FT                   /id="PRO_0000032779"
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;  73620 MW;  4980ED7426958D7C CRC64;
     MDRAKPFVWR LVAASVCLLT FCHLARADSL EEQRNRYAQI KQAWDNRQMD VVEQMMPGLK
     DYPLYPYLEY RKITDDLMNQ PAIAVTQFVR ANPTLPPART LQSRFVNELA RREDWRGLLA
     FSPEKPGTTE AQCNYYYAKW STGQTEAAWQ GAKDLWLTGK SQPNACDKLF SVWRASGKQD
     PLAYLERIRL AMKAGNTGLV TVLAGQMPAE YQTIASAIIT LANDPNNVLI FARTTGATDF
     TRQMAEVAFA SVARQDAENA RLMIPSLVQA QKLNEEQTQA LRDIVAWRLM GNDVTDAQAK
     WRDDAIMRSQ STSLIERRVR MALGMGDRRG LNTWLARLPM EAKEKDEWRY WQADLLLERG
     RDAEAKEILH ALMQKRGFYP MVAAQRLGEE YTLKIDKAPA NVNSALTQGP EMARVRELMY
     WNLDNTARSE WANLVKSRSK SEQAQLARYA FNQHWWDLSV QATIAGKLWD HLEERFPLAY
     NDLFTRYTRG KDISQSYAMA IARQESAWNP KVKSPVGASG LMQIMPGTAT HTVKMFSIPD
     YRGPGQLLEP ETNINIGTSY LQYVYQQFGN NRIFASAAYN AGPGRVRTWL GNSAGRIDAV
     AFVESIPFSE TRGYVKNVLA YDAYYRHFMG QKEALMSDSE WQRRY