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Database: UniProt/TrEMBL
Entry: D5B6W5_YERPZ
LinkDB: D5B6W5_YERPZ
Original site: D5B6W5_YERPZ 
ID   D5B6W5_YERPZ            Unreviewed;       170 AA.
AC   D5B6W5;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   01-MAY-2013, entry version 20.
DE   RecName: Full=Lysozyme;
DE            EC=3.2.1.17;
GN   OrderedLocusNames=YPZ3_1736;
OS   Yersinia pestis (strain Z176003).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Yersinia.
OX   NCBI_TaxID=637386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Z176003;
RA   Hai R., Yu D., Xia L., Zhu X., Liang Y., Shen X., Zhang E., Zhang H.;
RT   "Complete genome sequence of Yersinia pestis from new plague natural
RT   foci in China.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z176003;
RX   PubMed=20453098; DOI=10.1128/JB.00340-10;
RA   Shen X., Wang Q., Xia L., Zhu X., Zhang Z., Liang Y., Cai H.,
RA   Zhang E., Wei J., Chen C., Song Z., Zhang H., Yu D., Hai R.;
RT   "Complete genome sequences of Yersinia pestis from natural foci in
RT   China.";
RL   J. Bacteriol. 192:3551-3552(2010).
CC   -!- CATALYTIC ACTIVITY: 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.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
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DR   EMBL; CP001593; ADE64646.1; -; Genomic_DNA.
DR   RefSeq; YP_003567908.1; NC_014029.1.
DR   ProteinModelPortal; D5B6W5; -.
DR   EnsemblBacteria; ADE64646; ADE64646; YPZ3_1736.
DR   GeneID; 8991657; -.
DR   KEGG; ypz:YPZ3_1736; -.
DR   PATRIC; 35471532; VBIYerPes97410_2476.
DR   HOGENOM; HOG000277068; -.
DR   KO; K01185; -.
DR   OMA; MAITEKQ; -.
DR   GO; GO:0003796; F:lysozyme activity; IEA: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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   Gene3D; 1.10.530.40; -; 1.
DR   InterPro; IPR002196; Glyco_hydro_24.
DR   InterPro; IPR023346; Lysozyme-like_dom.
DR   InterPro; IPR023347; Lysozyme_dom.
DR   Pfam; PF00959; Phage_lysozyme; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
PE   3: Inferred from homology;
KW   Antimicrobial; Bacteriolytic enzyme; Complete proteome; Glycosidase;
KW   Hydrolase.
SQ   SEQUENCE   170 AA;  18174 MW;  AD79B7CC8AA0828C CRC64;
     MATIKRIASG SACAVAVIIA IVISAGNVRT SERGLELIGN AESCRRDPYA CPAGVLTDGI
     GNTHGVKAGV IKTDTQIAED WEKNILDAER CVIRYANGNK LPPSAFDAAT SISFNAGCSL
     MQKSTMFKYF RAGNVTAACE QFPRWIYGGG KKLPGLVTRR EKEKALCLES
//
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