ID   A0A1N7MHC5_9BACT        Unreviewed;       471 AA.
AC   A0A1N7MHC5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Membrane-bound lytic murein transglycosylase D {ECO:0000313|EMBL:SIS85584.1};
GN   ORFNames=SAMN05421761_10694 {ECO:0000313|EMBL:SIS85584.1};
OS   Belliella pelovolcani.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Belliella.
OX   NCBI_TaxID=529505 {ECO:0000313|EMBL:SIS85584.1, ECO:0000313|Proteomes:UP000186026};
RN   [1] {ECO:0000313|EMBL:SIS85584.1, ECO:0000313|Proteomes:UP000186026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46698 {ECO:0000313|EMBL:SIS85584.1,
RC   ECO:0000313|Proteomes:UP000186026};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC       {ECO:0000256|ARBA:ARBA00007734}.
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DR   EMBL; FTOP01000006; SIS85584.1; -; Genomic_DNA.
DR   RefSeq; WP_076500609.1; NZ_FTOP01000006.1.
DR   AlphaFoldDB; A0A1N7MHC5; -.
DR   STRING; 529505.SAMN05421761_10694; -.
DR   OrthoDB; 9815002at2; -.
DR   Proteomes; UP000186026; Unassembled WGS sequence.
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; 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; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..471
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012546279"
FT   DOMAIN          356..399
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          426..470
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
SQ   SEQUENCE   471 AA;  53101 MW;  3AED4E3556EEA832 CRC64;
     MKKNLKSIAL TALSVLFGST VLYGQEIFDI NTLGITEETI TPNYQFEYIP DFTYDDVARK
     IKTMETDMPF ELNDRIFSFI NYFAVRNRDY TKMVLEREAI YFPMFDEILA KHDMPSDIKY
     LAIIESGLNP RARSRVGAMG LWQFMPATGR MYNLHTNYDI DDRMDPELAT DAAAKYLKSL
     YKMFGNWELA LAAYNCGPGN VRKAIRRSGG KQTFWGVYDY LPRETRSYVP QFQAIMYLMR
     HVEDHNLYLE EPTYPIAYSK IQFNQELDLE QLAALSGICI EDLEKLNPSI QNRLIPASHK
     HLALKVPASK ASLIAENKAE FKEAVALTNE RIVELRTTVA AESGIKATAV PTGDLITYKV
     KSGDVLGSIA QRHGTTVTNI KNWNNLSSNT IRVGQNLKIY SNKPISNPTN VTLAENSISS
     NGSGSKVYTV QPGDSLWLIS KKLNGVTIDQ IKKLNNLNSN QIKPGQKLII G
//