ID A0A1I6KS43_9GAMM Unreviewed; 581 AA.
AC A0A1I6KS43;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Lysozyme {ECO:0000256|ARBA:ARBA00012732, ECO:0000256|RuleBase:RU003788};
DE EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732, ECO:0000256|RuleBase:RU003788};
GN ORFNames=SAMN05216570_0925 {ECO:0000313|EMBL:SFR94049.1};
OS Dyella sp. OK004.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1855292 {ECO:0000313|EMBL:SFR94049.1, ECO:0000313|Proteomes:UP000198834};
RN [1] {ECO:0000313|EMBL:SFR94049.1, ECO:0000313|Proteomes:UP000198834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK004 {ECO:0000313|EMBL:SFR94049.1,
RC ECO:0000313|Proteomes:UP000198834};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC between N-acetyl-D-glucosamine residues in chitodextrins.;
CC EC=3.2.1.17; Evidence={ECO:0000256|ARBA:ARBA00000632,
CC ECO:0000256|RuleBase:RU003788};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC {ECO:0000256|RuleBase:RU003788}.
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DR EMBL; FOZI01000001; SFR94049.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6KS43; -.
DR STRING; 1855292.SAMN05216570_0925; -.
DR Proteomes; UP000198834; Unassembled WGS sequence.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; 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:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd00118; LysM; 4.
DR CDD; cd00737; lyz_endolysin_autolysin; 1.
DR Gene3D; 1.10.530.40; -; 1.
DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR Gene3D; 3.10.350.10; LysM domain; 4.
DR HAMAP; MF_04110; ENDOLYSIN_T4; 1.
DR InterPro; IPR033907; Endolysin_autolysin.
DR InterPro; IPR034690; Endolysin_T4_type.
DR InterPro; IPR002196; Glyco_hydro_24.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR023347; Lysozyme_dom_sf.
DR PANTHER; PTHR33734; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2; 1.
DR Pfam; PF01476; LysM; 4.
DR Pfam; PF00959; Phage_lysozyme; 1.
DR SMART; SM00257; LysM; 4.
DR SUPFAM; SSF54106; LysM domain; 4.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51782; LYSM; 4.
PE 3: Inferred from homology;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529,
KW ECO:0000256|RuleBase:RU003788};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638,
KW ECO:0000256|RuleBase:RU003788};
KW Glycosidase {ECO:0000256|RuleBase:RU003788};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Hydrolase {ECO:0000256|RuleBase:RU003788};
KW Reference proteome {ECO:0000313|Proteomes:UP000198834}.
FT DOMAIN 21..66
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 262..307
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 318..363
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 380..425
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 53..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..255
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 58567 MW; 6319A91663E30005 CRC64;
MTAVSAVRST QTLAASGDNS ATYTVQHGDS LSGIAQRFGV SLAALEAANP QISNPDRIYP
GDRVTIPGDH GGGTPAPVGG STPPAGNAGP ASGFSISQNG VKMIEGFEGY SEKAYPDPGT
GGAPWTIGYG HTGGVQPGQT ITRAQAEEYL KQDLGWAQDA VRKNVHVPIN QNQFDALVSL
TYNLGANGYP GLLSKLNGGD YAGAQQMFGQ YVHGGGHVLP GLVSRRAQEA ALFGSSAPAG
APAPAPTPAP APAPAPGGAH GGSYTVQPGD TLSGIAQRQG VSLQALEAAN PQIGNFNHIY
PRQVIHLPGG GGSAPAGGSY TVRSGDSLSG IATSHGVSLA ALEAANPQIS NPNRIYPGQV
IHIPGGSSGS AAPAPKPASH DYTVRSGDTL SGIAARNGVS LAALERANPQ ISNPNRISVG
QVIHVPGAGS TGGSTGPGPV QGSSGASGSK VVDLAKQFLG RNASDLKRSG QLPMESWVPS
DLCCANFVTA VLQKAGAINF HSNQVSEVAS KLQAQGWHKV DAAHAKPGDV CILNNGGHVE
LVASNNGGNV QLIGSNNSNA DGTQKVGYGH PYGGAWYLTP P
//
