ID   LYSD_ECOLI              Reviewed;         165 AA.
AC   P78285; Q2MBM6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   24-JAN-2024, entry version 146.
DE   RecName: Full=Lysozyme RrrD;
DE            EC=3.2.1.17;
DE   AltName: Full=Endolysin;
DE   AltName: Full=Lysis protein;
DE   AltName: Full=Muramidase;
GN   Name=rrrD; Synonyms=arrD, ybcS; OrderedLocusNames=b0555, JW0544;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION AS A LYSIN.
RX   PubMed=17914239; DOI=10.1007/s12038-007-0097-x;
RA   Srividhya K.V., Krishnaswamy S.;
RT   "Subclassification and targeted characterization of prophage-encoded two-
RT   component cell lysis cassette.";
RL   J. Biosci. 32:979-990(2007).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / MG1655 / ATCC 47076 / PHL626;
RX   PubMed=21415116; DOI=10.1099/mic.0.045161-0;
RA   Toba F.A., Thompson M.G., Campbell B.R., Junker L.M., Rueggeberg K.G.,
RA   Hay A.G.;
RT   "Role of DLP12 lysis genes in Escherichia coli biofilm formation.";
RL   Microbiology 157:1640-1650(2011).
CC   -!- FUNCTION: Essential for lysis of bacterial cell wall, by showing cell
CC       wall hydrolyzing activity. Exhibits lytic activity against E.coli and
CC       S.typhi cell wall substrate. {ECO:0000269|PubMed:17914239}.
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;
CC   -!- DISRUPTION PHENOTYPE: Mutants are unable to form wild-type biofilms,
CC       which could be due to altered peptidoglycan metabolism.
CC       {ECO:0000269|PubMed:21415116}.
CC   -!- MISCELLANEOUS: Encoded by the cryptic lambdoid prophage DLP12.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family. {ECO:0000305}.
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DR   EMBL; U82598; AAB40751.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73656.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76330.1; -; Genomic_DNA.
DR   PIR; A64788; A64788.
DR   RefSeq; NP_415087.1; NC_000913.3.
DR   RefSeq; WP_001135281.1; NZ_JACEFS010000069.1.
DR   PDB; 4ZPU; X-ray; 2.40 A; A/B/C/D=1-165.
DR   PDBsum; 4ZPU; -.
DR   AlphaFoldDB; P78285; -.
DR   SMR; P78285; -.
DR   BioGRID; 4259885; 4.
DR   IntAct; P78285; 3.
DR   STRING; 511145.b0555; -.
DR   CAZy; GH24; Glycoside Hydrolase Family 24.
DR   PaxDb; 511145-b0555; -.
DR   EnsemblBacteria; AAC73656; AAC73656; b0555.
DR   GeneID; 947539; -.
DR   KEGG; ecj:JW0544; -.
DR   KEGG; eco:b0555; -.
DR   PATRIC; fig|1411691.4.peg.1720; -.
DR   EchoBASE; EB3399; -.
DR   eggNOG; COG3772; Bacteria.
DR   HOGENOM; CLU_091641_4_1_6; -.
DR   InParanoid; P78285; -.
DR   OMA; WIYADGQ; -.
DR   OrthoDB; 8141296at2; -.
DR   PhylomeDB; P78285; -.
DR   BioCyc; EcoCyc:G6310-MONOMER; -.
DR   BioCyc; MetaCyc:G6310-MONOMER; -.
DR   PRO; PR:P78285; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0003796; F:lysozyme activity; IDA:EcoCyc.
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:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   GO; GO:0044659; P:viral release from host cell by cytolysis; IMP:EcoCyc.
DR   CDD; cd16900; endolysin_R21-like; 1.
DR   Gene3D; 1.10.530.40; -; 1.
DR   HAMAP; MF_04110; ENDOLYSIN_T4; 1.
DR   HAMAP; MF_04136; SAR_ENDOLYSIN; 1.
DR   InterPro; IPR034690; Endolysin_T4_type.
DR   InterPro; IPR002196; Glyco_hydro_24.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR023347; Lysozyme_dom_sf.
DR   InterPro; IPR043688; SAR_endolysin-like.
DR   PANTHER; PTHR38107; -; 1.
DR   PANTHER; PTHR38107:SF3; LYSOZYME RRRD-RELATED; 1.
DR   Pfam; PF00959; Phage_lysozyme; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antimicrobial; Bacteriolytic enzyme; Glycosidase; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..165
FT                   /note="Lysozyme RrrD"
FT                   /id="PRO_0000218109"
FT   ACT_SITE        35
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        44
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   HELIX           3..11
FT                   /evidence="ECO:0007829|PDB:4ZPU"
FT   HELIX           13..15
FT                   /evidence="ECO:0007829|PDB:4ZPU"
FT   HELIX           16..26
FT                   /evidence="ECO:0007829|PDB:4ZPU"
FT   STRAND          30..35
FT                   /evidence="ECO:0007829|PDB:4ZPU"
FT   STRAND          38..43
FT                   /evidence="ECO:0007829|PDB:4ZPU"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:4ZPU"
FT   HELIX           68..86
FT                   /evidence="ECO:0007829|PDB:4ZPU"
FT   HELIX           87..89
FT                   /evidence="ECO:0007829|PDB:4ZPU"
FT   HELIX           96..109
FT                   /evidence="ECO:0007829|PDB:4ZPU"
FT   HELIX           111..115
FT                   /evidence="ECO:0007829|PDB:4ZPU"
FT   HELIX           118..124
FT                   /evidence="ECO:0007829|PDB:4ZPU"
FT   HELIX           128..134
FT                   /evidence="ECO:0007829|PDB:4ZPU"
FT   HELIX           135..137
FT                   /evidence="ECO:0007829|PDB:4ZPU"
FT   HELIX           147..160
FT                   /evidence="ECO:0007829|PDB:4ZPU"
FT   TURN            161..164
FT                   /evidence="ECO:0007829|PDB:4ZPU"
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
//