ID   A0A1Y3VW71_9BACT        Unreviewed;       305 AA.
AC   A0A1Y3VW71;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Peptidoglycan hydrolase {ECO:0000256|ARBA:ARBA00032108};
GN   ORFNames=B5G13_11450 {ECO:0000313|EMBL:OUN65215.1};
OS   Butyricimonas sp. An62.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Odoribacteraceae;
OC   Butyricimonas.
OX   NCBI_TaxID=1965649 {ECO:0000313|EMBL:OUN65215.1, ECO:0000313|Proteomes:UP000196559};
RN   [1] {ECO:0000313|Proteomes:UP000196559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An62 {ECO:0000313|Proteomes:UP000196559};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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:OUN65215.1}.
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DR   EMBL; NFHW01000003; OUN65215.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3VW71; -.
DR   OrthoDB; 977752at2; -.
DR   Proteomes; UP000196559; 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; 2.
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; 2.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196559};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..305
FT                   /note="Peptidoglycan hydrolase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013299938"
FT   DOMAIN          254..298
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
SQ   SEQUENCE   305 AA;  35125 MW;  BA23BCD16B5858B7 CRC64;
     MSKIYVILFL SFICVNICGA STDSRKAFIK KYKSIAIEEM DRTGIPASIK LAQGMLESGC
     GTSKLAVNAN NHFGIKCHNW NGASFTMDDD KRNECFRKYR NPEESWVDHS EFLLTRPRYA
     FLFDLPKTDY KGWAKGLKKA GYATASDYAQ KLIKIIEEEE LYQFDRPAKK VRPIPNELNY
     KLSESKNYQS RVVYINRIPS VKVKEGDTFE NIAQYFNIPL KKLLKYNDKN ELSIRTGMHV
     FLAKKKNKAP KGYTFHKTKA GDTMYMISQI YGIKLAKLLQ YNYMENGEQP QVGEMISLRG
     PAQLY
//