(data stored in SCRATCH zone)

SWISSPROT: B7ULT6_ECO27

ID   B7ULT6_ECO27            Unreviewed;       165 AA.
AC   B7ULT6;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 49.
DE   RecName: Full=Lysozyme {ECO:0000256|RuleBase:RU003788};
DE            EC=3.2.1.17 {ECO:0000256|RuleBase:RU003788};
GN   OrderedLocusNames=E2348C_0690 {ECO:0000313|EMBL:CAS08238.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08238.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08238.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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; FM180568; CAS08238.1; -; Genomic_DNA.
DR   RefSeq; WP_000075132.1; NC_011601.1.
DR   CAZy; GH24; Glycoside Hydrolase Family 24.
DR   EnsemblBacteria; CAS08238; CAS08238; E2348C_0690.
DR   KEGG; ecg:E2348C_0690; -.
DR   HOGENOM; HOG000277068; -.
DR   KO; K01185; -.
DR   OMA; HLENIAY; -.
DR   BioCyc; ECOL574521:E2348C_RS03705-MONOMER; -.
DR   Proteomes; UP000008205; 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; B7ULT6.
DR   SWISS-2DPAGE; B7ULT6.
KW   Antimicrobial {ECO:0000256|RuleBase:RU003788};
KW   Bacteriolytic enzyme {ECO:0000256|RuleBase:RU003788};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Glycosidase {ECO:0000256|RuleBase:RU003788};
KW   Hydrolase {ECO:0000256|RuleBase:RU003788}.
SQ   SEQUENCE   165 AA;  17889 MW;  D4314AA85D9D8CCA CRC64;
     MSPSLRKAVA AAIGGGAVAI ASVLITGPGG NDGLEGVSYI PYKDIVGVWT VCHGHTGKDI
     MPGKTYTEAE CKALLNKDLA TVARQINPYI NVDIPETTRG ALYSFVYNVG AGNFRTSTLL
     RKINQGDIKG ACDQLRRWTY AGGKQWKGLM TRREIEREVC LWGQQ
//

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