(data stored in ACNUC10821 zone)

SWISSPROT: C8U2N9_ECO10

ID   C8U2N9_ECO10            Unreviewed;       165 AA.
AC   C8U2N9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 48.
DE   RecName: Full=Lysozyme {ECO:0000256|RuleBase:RU003788};
DE            EC=3.2.1.17 {ECO:0000256|RuleBase:RU003788};
GN   OrderedLocusNames=ECO103_0530 {ECO:0000313|EMBL:BAI29397.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29397.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29397.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-linkages between N-
CC         acetylmuramic acid and N-acetyl-D-glucosamine residues in a
CC         peptidoglycan and between N-acetyl-D-glucosamine residues in
CC         chitodextrins.; EC=3.2.1.17;
CC         Evidence={ECO:0000256|RuleBase:RU003788};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC       {ECO:0000256|RuleBase:RU003788}.
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DR   EMBL; AP010958; BAI29397.1; -; Genomic_DNA.
DR   RefSeq; WP_001135281.1; NC_013353.1.
DR   SMR; C8U2N9; -.
DR   CAZy; GH24; Glycoside Hydrolase Family 24.
DR   EnsemblBacteria; BAI29397; BAI29397; ECO103_0530.
DR   KEGG; eoh:ECO103_0530; -.
DR   HOGENOM; HOG000277068; -.
DR   KO; K01185; -.
DR   OMA; WIYADGQ; -.
DR   BioCyc; ECOL585395:ECO103_RS02765-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
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:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0044659; P:cytolysis by virus of host cell; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd00737; endolysin_autolysin; 1.
DR   InterPro; IPR033907; Endolysin_autolysin.
DR   InterPro; IPR002196; Glyco_hydro_24.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   Pfam; PF00959; Phage_lysozyme; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U2N9.
DR   SWISS-2DPAGE; C8U2N9.
KW   Antimicrobial {ECO:0000256|RuleBase:RU003788};
KW   Bacteriolytic enzyme {ECO:0000256|RuleBase:RU003788};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Glycosidase {ECO:0000256|RuleBase:RU003788};
KW   Hydrolase {ECO:0000256|RuleBase:RU003788}.
SQ   SEQUENCE   165 AA;  17972 MW;  370CECD5B419329B CRC64;
     MPPSLRKAVA AAIGGGAIAI ASVLITGPSG NDGLEGVSYI PYKDIVGVWT VCHGHTGKDI
     MLGKTYTKAE CKALLNKDLA TVARQINPYI KVDIPETTRG ALYSFVYNVG AGNFRTSTLL
     RKINQGDIKG ACDQLRRWTY AGGKQWKGLM TRREIEREVC LWGQQ
//

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