ID   A0A3P1T3C2_9BACT        Unreviewed;       297 AA.
AC   A0A3P1T3C2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Peptidoglycan hydrolase {ECO:0000256|ARBA:ARBA00032108};
GN   ORFNames=EII32_00550 {ECO:0000313|EMBL:RRD02983.1};
OS   Prevotella sp. OH937_COT-195.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=2491051 {ECO:0000313|EMBL:RRD02983.1, ECO:0000313|Proteomes:UP000267043};
RN   [1] {ECO:0000313|EMBL:RRD02983.1, ECO:0000313|Proteomes:UP000267043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OH937_COT-195 {ECO:0000313|EMBL:RRD02983.1,
RC   ECO:0000313|Proteomes:UP000267043};
RA   Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA   Eisen J.A., Holcombe L.J., O'Flynn C.;
RT   "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT   for Automated Genome-Based Taxonomic Assignment.";
RL   Submitted (NOV-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:RRD02983.1}.
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DR   EMBL; RQZH01000001; RRD02983.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P1T3C2; -.
DR   OrthoDB; 977752at2; -.
DR   Proteomes; UP000267043; 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   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; 2.
PE   4: Predicted;
KW   Antimicrobial {ECO:0000256|ARBA:ARBA00022638};
KW   Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..297
FT                   /note="Peptidoglycan hydrolase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018285058"
FT   DOMAIN          194..238
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          252..296
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
SQ   SEQUENCE   297 AA;  33849 MW;  41BF673DEB103F57 CRC64;
     MRIIYVMLIV LASALNCSAQ GTGLNSAYLK YIKQYSGLAV EQMKLYRIPA SITLAQGLIE
     SGAGQSELAR NGNNHFGIKC HDWQGRKVYH DDDLVGECFR AYDNVRQSYE DHSLFLVKGR
     RYRSLFSLSI NDYRGWARGL KAAGYATNPS YAEILIRIIE QYRLHDFDKG KVHHRRPIGT
     DEEDFNVLVC NGTPYVVVRS GDTFRTISDM TGVSVRRLAK YNEMPKNSVL KQGTPIYLQK
     KPKRASKAYR GKYHEVRVGE SMHSIAQLYA MRVETLYKIN CLSPDYGIKA GDKLRIR
//