ID A0A180F2P7_9BACT Unreviewed; 284 AA.
AC A0A180F2P7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peptidoglycan hydrolase {ECO:0000256|ARBA:ARBA00032108};
GN Name=lytG {ECO:0000313|EMBL:OAV66608.1};
GN ORFNames=Barb4_02818 {ECO:0000313|EMBL:OAV66608.1};
OS Bacteroidales bacterium Barb4.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1633200 {ECO:0000313|EMBL:OAV66608.1, ECO:0000313|Proteomes:UP000078495};
RN [1] {ECO:0000313|EMBL:OAV66608.1, ECO:0000313|Proteomes:UP000078495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Barb4 {ECO:0000313|EMBL:OAV66608.1,
RC ECO:0000313|Proteomes:UP000078495};
RA Tai V., Carpenter K.J., Weber P.K., Nalepa C.A., Perlman S.J.,
RA Keeling P.J.;
RT "Genomic and NanoSIMS analyses of nitrogen-fixing bacterial ectosymbionts
RT of a protist inhabiting a wood-eating cockroach.";
RL Submitted (DEC-2015) 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:OAV66608.1}.
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DR EMBL; LBCX01000199; OAV66608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A180F2P7; -.
DR PATRIC; fig|1633200.3.peg.1876; -.
DR Proteomes; UP000078495; Unassembled WGS sequence.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
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; 1.
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; 1.
DR SMART; SM00047; LYZ2; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
PE 4: Predicted;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022638};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW Glycosidase {ECO:0000313|EMBL:OAV66608.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OAV66608.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078495};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..284
FT /note="Peptidoglycan hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008108506"
FT DOMAIN 22..168
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
SQ SEQUENCE 284 AA; 32668 MW; 19689AE8AD93BCE6 CRC64;
MRVFMRLVWV LALLAVVGGV AAQHKNAAYQ RYIDRYGALA AEQQKKYRIP ASVTLAQGIM
ESGAGAGRLA VESNNHFGIK CHDDWRGGRV YHDDDRRGEC FRKYKRAEDS YEDHSRFLTE
RSHYSRLFKL NITDYKGWAK GLQQCGYATD RAYANKLIKI IEDYELYRPA PLKRAVYKGH
GLIYIHALTD DSFERMAGDL DFSAKKLRKY NEVPEGFPLQ KGDIVYLQKK KRKAGKPHYN
HAVQIGESMH GIAQKYGIQI KSLYKLNKKT LDYIPAEGDV LRLR
//
