ID A0A1I0QT92_9BACT Unreviewed; 483 AA.
AC A0A1I0QT92;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Peptidoglycan hydrolase {ECO:0000256|ARBA:ARBA00032108};
GN ORFNames=SAMN04488122_1730 {ECO:0000313|EMBL:SEW30792.1};
OS Chitinophaga arvensicola.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=29529 {ECO:0000313|EMBL:SEW30792.1, ECO:0000313|Proteomes:UP000199310};
RN [1] {ECO:0000313|EMBL:SEW30792.1, ECO:0000313|Proteomes:UP000199310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3695 {ECO:0000313|EMBL:SEW30792.1,
RC ECO:0000313|Proteomes:UP000199310};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOJG01000001; SEW30792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0QT92; -.
DR STRING; 29529.SAMN04488122_1730; -.
DR OrthoDB; 977752at2; -.
DR Proteomes; UP000199310; 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; 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; SM00257; LysM; 3.
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:SEW30792.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..483
FT /note="Peptidoglycan hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011571723"
FT DOMAIN 438..481
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 188..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 53852 MW; 54B461B9837FEF4E CRC64;
MQVRKFLLTV SFLIGLVTVL HAQNITTQQY IATYKNLAIE EMRRSGVPAA IKLAQGIVET
QSGNGTLCLQ SNNHFGIKCK NTWTGKTIKY DDDAAQECFR VYETARDSYR DHSDFLHANP
RYSFLFQFDG DDYKSWAFGL KQAGYATNKT YPQQLIKVIE DYNLQQYTLI AMGKDPSDGG
AATDKTQYAE VTEKETRTSP GRKNHNTTTT TKQTPGSFPK GIFEINGRKA VYVKAGTSLI
QLADQRNMRL RKLVRFNDLE NDNPPKKDMI VFLQKKSKRG SKEFHPVVNG ETMHDVAQAE
GVQLRWLRRR NKMNEGEEPA AGQRLTLDGF ASSAPRLAKN TRVLKEEDQE PPEDFSPRKA
LDGIKEEVAK NTTGGTAVPE IKPAPQGGVP VAMIEDLKKA GTVTTSGGTA GTPKASMPQP
QSQPATPKPA PAQRSNTQYH DVQPKETLYG IAKMYNQSVT QLQEWNNLQG FDIKIGQRLL
VSK
//
