ID   D8IBK0_BRAP9            Unreviewed;       466 AA.
AC   D8IBK0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Membrane-bound lytic murein transglycosylase D {ECO:0000313|EMBL:ADK30523.1};
GN   OrderedLocusNames=BP951000_0520 {ECO:0000313|EMBL:ADK30523.1};
OS   Brachyspira pilosicoli (strain ATCC BAA-1826 / 95/1000).
OC   Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC   Brachyspira.
OX   NCBI_TaxID=759914 {ECO:0000313|EMBL:ADK30523.1, ECO:0000313|Proteomes:UP000000332};
RN   [1] {ECO:0000313|EMBL:ADK30523.1, ECO:0000313|Proteomes:UP000000332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1826 / 95/1000 {ECO:0000313|Proteomes:UP000000332};
RX   PubMed=20625514; DOI=10.1371/journal.pone.0011455;
RA   Wanchanthuek P., Bellgard M.I., La T., Ryan K., Moolhuijzen P., Chapman B.,
RA   Black M., Schibeci D., Hunter A., Barrero R., Phillips N.D., Hampson D.J.;
RT   "The complete genome sequence of the pathogenic intestinal spirochete
RT   Brachyspira pilosicoli and comparison with other Brachyspira genomes.";
RL   PLoS ONE 5:E11455-E11455(2010).
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC       {ECO:0000256|ARBA:ARBA00007734}.
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DR   EMBL; CP002025; ADK30523.1; -; Genomic_DNA.
DR   RefSeq; WP_013243477.1; NC_014330.1.
DR   AlphaFoldDB; D8IBK0; -.
DR   SMR; D8IBK0; -.
DR   STRING; 759914.BP951000_0520; -.
DR   CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   GeneID; 56439099; -.
DR   KEGG; bpo:BP951000_0520; -.
DR   eggNOG; COG0741; Bacteria.
DR   eggNOG; COG1388; Bacteria.
DR   HOGENOM; CLU_009520_1_0_12; -.
DR   InParanoid; D8IBK0; -.
DR   Proteomes; UP000000332; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
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; PTHR37423:SF2; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR   PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 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; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000332}.
FT   DOMAIN          330..373
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          417..460
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
SQ   SEQUENCE   466 AA;  53792 MW;  2B8906DFC676DFD3 CRC64;
     MKIKILKRKR ILAIFLIVLI FFVNSCDTFD LYLRKGLDGV NLYELTVYGE ALGSDIKVVE
     LRGFNVDDFR TERVSYYLDR YQGSWRPHMQ KIIDRAQIYL PYIKQVFAEK GVPEDLAYLP
     IIESSFYPQA VSHAGAAGLW QFMPMTGAIY NLKVNYWSDD RFDPERSTKA AAEHLMRLDE
     NFKSWVIALI AYNAGGGRIS RAIKQVKSNN FYDLLRAKVL PKETEEYIPK YVASVIIAKN
     PEKFGFKINK PKVVFPEGDL VYVDDAADLS IIADMIDAET EDLKALNPHL SRGVTPPGMV
     RYPLRIPEGK EQLFYDTFGK IPASERVTFR RHEVKMNETL SHLSRFYNVP MQAIVEINKL
     KSRNLNIGQQ VMIPIQGLDN AKQVDLAQYE EEQERIREGK FVYFESLPPP DYEYKDIMYH
     IRAGDTLWII ARKFKVDVAE IKAWNKLDSN VLSIGSEIFL RIPVNK
//