ID   Q0T803_SHIF8            Unreviewed;       452 AA.
AC   Q0T803;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=peptidoglycan lytic exotransglycosylase {ECO:0000256|ARBA:ARBA00012587};
DE            EC=4.2.2.n1 {ECO:0000256|ARBA:ARBA00012587};
GN   Name=dniR {ECO:0000313|EMBL:ABF02473.1};
GN   OrderedLocusNames=SFV_0195 {ECO:0000313|EMBL:ABF02473.1};
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384 {ECO:0000313|EMBL:ABF02473.1, ECO:0000313|Proteomes:UP000000659};
RN   [1] {ECO:0000313|EMBL:ABF02473.1, ECO:0000313|Proteomes:UP000000659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401 {ECO:0000313|EMBL:ABF02473.1,
RC   ECO:0000313|Proteomes:UP000000659};
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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         Evidence={ECO:0000256|ARBA:ARBA00001420};
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC       {ECO:0000256|ARBA:ARBA00007734}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000266; ABF02473.1; -; Genomic_DNA.
DR   RefSeq; WP_000644677.1; NC_008258.1.
DR   AlphaFoldDB; Q0T803; -.
DR   CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   KEGG; sfv:SFV_0195; -.
DR   HOGENOM; CLU_009520_1_4_6; -.
DR   Proteomes; UP000000659; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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   CDD; cd00118; LysM; 2.
DR   CDD; cd16894; MltD-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.10.350.10; LysM domain; 2.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR000189; Transglyc_AS.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   PANTHER; PTHR33734; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2; 1.
DR   PANTHER; PTHR33734:SF22; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE D; 1.
DR   Pfam; PF01476; LysM; 2.
DR   Pfam; PF01464; SLT; 1.
DR   SMART; SM00257; LysM; 2.
DR   SUPFAM; SSF54106; LysM domain; 2.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS51782; LYSM; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT   DOMAIN          341..384
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          400..448
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
SQ   SEQUENCE   452 AA;  49476 MW;  43CD5B416C59484A CRC64;
     MKAKAILLAS VLLVGCQSTG NVQQHAQSLS AAGQGEAAKF TSQARWMDDG TSIAPDGDLW
     AFIGDELKMG IPENDRIREQ KQKYLRNKSY LHDVTLRAEP YMYWIAGQVK KRNMPMELVL
     LPIVESAFDP HATSGANAAG IWQIIPSTGR NYGLKQTRNY DARRDVVAST TAALNMMQRL
     NKMFDDDWLL TVAAYNSGEG RVMKAIKTNK ARGKSTDFWS LPLPQETKQY VPKMLALSDI
     LKNSKRYGVR LPTTDESRAL ARVHLSSPVE MAKVADMAGI SVSKLKTFNA GVKGSTLGAS
     GPQYVMVPKK HADQLRESLA SGEIAAVQST LVADNTPLNS RVYTVRSGDT LSSIASRLGV
     STKDLQQWNK LRGSKLKPGQ SLTIGAGSSA QRLANNSDSI TYRVRKGDSL SSIAKRHGVN
     IKDVMRWNSD TANLQPGDKL TLFVKNNNMP DS
//