LYS_CLOAB
ID LYS_CLOAB Reviewed; 324 AA.
AC P34020;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Autolytic lysozyme;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase;
DE AltName: Full=Autolysin;
GN Name=lyc; OrderedLocusNames=CA_C0554;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=1916274; DOI=10.1016/0378-1119(91)90460-s;
RA Croux C., Garcia J.L.;
RT "Sequence of the lyc gene encoding the autolytic lysozyme of Clostridium
RT acetobutylicum ATCC824: comparison with other lytic enzymes.";
RL Gene 104:25-31(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
RN [3]
RP PROTEIN SEQUENCE OF 1-23, AND CHARACTERIZATION.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=1599233; DOI=10.1128/aem.58.4.1075-1081.1992;
RA Croux C., Canard B., Goma G., Soucaille P.;
RT "Purification and characterization of an extracellular muramidase of
RT Clostridium acetobutylicum ATCC 824 that acts on non-N-acetylated
RT peptidoglycan.";
RL Appl. Environ. Microbiol. 58:1075-1081(1992).
RN [4]
RP CHARACTERIZATION.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=1645127; DOI=10.1099/00221287-138-5-861;
RA Croux C., Canard B., Goma G., Soucaille P.;
RT "Autolysis of Clostridium acetobutylicum ATCC 824.";
RL J. Gen. Microbiol. 138:861-869(1992).
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 -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasm.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family. {ECO:0000305}.
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DR EMBL; M68865; AAA23250.1; -; Genomic_DNA.
DR EMBL; AE001437; AAK78533.1; -; Genomic_DNA.
DR PIR; B96968; B96968.
DR PIR; JH0441; JH0441.
DR RefSeq; NP_347193.1; NC_003030.1.
DR RefSeq; WP_010963875.1; NC_003030.1.
DR AlphaFoldDB; P34020; -.
DR SMR; P34020; -.
DR STRING; 272562.CA_C0554; -.
DR CAZy; GH25; Glycoside Hydrolase Family 25.
DR EnsemblBacteria; AAK78533; AAK78533; CA_C0554.
DR GeneID; 44997064; -.
DR KEGG; cac:CA_C0554; -.
DR PATRIC; fig|272562.8.peg.759; -.
DR eggNOG; COG3409; Bacteria.
DR eggNOG; COG3757; Bacteria.
DR HOGENOM; CLU_044973_2_0_9; -.
DR OMA; INNANGC; -.
DR OrthoDB; 1444566at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR Gene3D; 1.10.101.10; -; 2.
DR InterPro; IPR002053; Glyco_hydro_25.
DR InterPro; IPR008270; Glyco_hydro_25_AS.
DR InterPro; IPR018077; Glyco_hydro_fam25_subgr.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR Pfam; PF01183; Glyco_hydro_25; 1.
DR Pfam; PF01471; PG_binding_1; 2.
DR SMART; SM00641; Glyco_25; 2.
DR SUPFAM; SSF47090; SSF47090; 2.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00953; GLYCOSYL_HYDROL_F25_1; 1.
DR PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
PE 1: Evidence at protein level;
KW Antimicrobial; Bacteriolytic enzyme; Cytoplasm; Direct protein sequencing;
KW Glycosidase; Hydrolase; Reference proteome; Repeat; Secreted.
FT CHAIN 1..324
FT /note="Autolytic lysozyme"
FT /id="PRO_0000208264"
FT REPEAT 212..234
FT /note="1"
FT REPEAT 235..254
FT /note="2"
FT REPEAT 255..277
FT /note="3"
FT REPEAT 278..300
FT /note="4"
FT REPEAT 301..324
FT /note="5"
FT REGION 212..324
FT /note="5 X 23 AA tandem repeats"
FT ACT_SITE 5
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10065"
FT ACT_SITE 91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10065"
SQ SEQUENCE 324 AA; 34978 MW; 32F09D6D77D015E9 CRC64;
MKGIDIYSGQ GSVDFNAVKE SGVEVVYIKA TEGLTYTDST YKDFYDGAKN AGLKIGFYHY
LRANDPTSEA EHFFNTISGL SLDCKCAIDV EVTLGQSIDQ ISSNVRKFAD YLINKGLDVC
VYTYTNFYKD NLNSTVKDLP LWIAEYGVSK PNIDASYVGF QYSDSGSVNG ISGSADLDEF
SEGILVGGTV VIDPGQGGDD NIKAIQQDLN ILLKRGLEVD GIEGPETEAA IKDFQSIMGL
TVDGIWGTNT SGAAQQIFSR PLDGVAYPHY EYATRYIQYR VGASVDGTFG SGTKAKVAAW
QSNQGLMADG VVGSATWSKL LDEN
