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Database: UniProt
Entry: A0A2W7MYV9_9BACT
LinkDB: A0A2W7MYV9_9BACT
Original site: A0A2W7MYV9_9BACT 
ID   A0A2W7MYV9_9BACT        Unreviewed;       319 AA.
AC   A0A2W7MYV9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Peptidoglycan hydrolase {ECO:0000256|ARBA:ARBA00032108};
GN   ORFNames=LX69_02806 {ECO:0000313|EMBL:PZX12851.1};
OS   Breznakibacter xylanolyticus.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC   Breznakibacter.
OX   NCBI_TaxID=990 {ECO:0000313|EMBL:PZX12851.1, ECO:0000313|Proteomes:UP000249239};
RN   [1] {ECO:0000313|EMBL:PZX12851.1, ECO:0000313|Proteomes:UP000249239}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6779 {ECO:0000313|EMBL:PZX12851.1,
RC   ECO:0000313|Proteomes:UP000249239};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PZX12851.1}.
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DR   EMBL; QKZK01000029; PZX12851.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2W7MYV9; -.
DR   OrthoDB; 977752at2; -.
DR   Proteomes; UP000249239; Unassembled WGS sequence.
DR   GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00118; LysM; 2.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.10.350.10; LysM domain; 1.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR   PANTHER; PTHR33308; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR   PANTHER; PTHR33308:SF9; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR   Pfam; PF01832; Glucosaminidase; 1.
DR   Pfam; PF01476; LysM; 2.
DR   SMART; SM00257; LysM; 2.
DR   SMART; SM00047; LYZ2; 1.
DR   SUPFAM; SSF54106; LysM domain; 1.
DR   PROSITE; PS51782; LYSM; 1.
PE   4: Predicted;
KW   Antimicrobial {ECO:0000256|ARBA:ARBA00022638};
KW   Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PZX12851.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249239};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..319
FT                   /note="Peptidoglycan hydrolase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016040208"
FT   DOMAIN          270..314
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
SQ   SEQUENCE   319 AA;  36782 MW;  013964CF0D79857A CRC64;
     MNSKYLTIAL ACCLSLGSHK LVAQRMSTQN YVEQYSKWAV VEMKRTGVPA SITLAQGILE
     SSSGNSSLAV DANNHFGIKC HDWTGKKVYK DDDTKNECFR HYDSAYDSYV DHSNFLRGRQ
     RYAALFELET TDYKGWAHGL RKAGYATDPN YPAKLIKYIE DYQLYRYDFH IDNDAVAAND
     DFEQNVSTSS KRKTDDFVIN MGQSHPIKYN NGVAYIEVGE NDTFESISKE FAMRAWEIYH
     YNDIASSDNI KKYRILYIKP KHNKAHPNHD THSVKQGETM HYISQKYGIK LKRLFKYNHL
     TIGTEPKAGD ILQLRKMQD
//
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