LYS_BPB30
ID LYS_BPB30 Reviewed; 443 AA.
AC Q8HA43;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=D-alanyl-L-alanine endopeptidase {ECO:0000303|PubMed:17021237};
DE EC=3.4.22.- {ECO:0000269|PubMed:15256551, ECO:0000269|PubMed:17021237};
DE AltName: Full=1,4-N-acetylmuramidase {ECO:0000303|PubMed:17021237};
DE EC=3.2.1.17 {ECO:0000269|PubMed:17021237};
DE AltName: Full=B30 lysin {ECO:0000303|PubMed:17021237};
DE AltName: Full=Endoysin;
DE AltName: Full=Glycosidase;
OS Streptococcus phage B30 (Streptococcus agalactiae bacteriophage B30).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales.
OX NCBI_TaxID=209152;
OH NCBI_TaxID=1311; Streptococcus agalactiae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-26; CYS-34; CYS-44;
RP HIS-91; ASP-158 AND GLU-185, FUNCTION, AND DOMAIN.
RX PubMed=15256551; DOI=10.1099/mic.0.27063-0;
RA Pritchard D.G., Dong S., Baker J.R., Engler J.A.;
RT "The bifunctional peptidoglycan lysin of Streptococcus agalactiae
RT bacteriophage B30.";
RL Microbiology 150:2079-2087(2004).
RN [2]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=17021237; DOI=10.1128/aem.00829-06;
RA Baker J.R., Liu C., Dong S., Pritchard D.G.;
RT "Endopeptidase and glycosidase activities of the bacteriophage B30 lysin.";
RL Appl. Environ. Microbiol. 72:6825-6828(2006).
RN [3]
RP DOMAIN.
RX PubMed=16820517; DOI=10.1128/aem.03065-05;
RA Donovan D.M., Foster-Frey J., Dong S., Rousseau G.M., Moineau S.,
RA Pritchard D.G.;
RT "The cell lysis activity of the Streptococcus agalactiae bacteriophage B30
RT endolysin relies on the cysteine, histidine-dependent
RT amidohydrolase/peptidase domain.";
RL Appl. Environ. Microbiol. 72:5108-5112(2006).
CC -!- FUNCTION: The endopeptidase activity cleaves the bacterial
CC peptidoglycan between D-alanine and L-alanine (PubMed:15256551,
CC PubMed:17021237). The N-acetyl-muramidase activity cleaves between N-
CC acetylmuramic acid and N-acetylglucosamine bonds (PubMed:17021237).
CC {ECO:0000269|PubMed:15256551, ECO:0000269|PubMed:17021237}.
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; Evidence={ECO:0000269|PubMed:17021237};
CC -!- ACTIVITY REGULATION: Ca++ enhances the activity of the enzyme.
CC {ECO:0000269|PubMed:15256551}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5-6.0. {ECO:0000269|PubMed:15256551};
CC -!- DOMAIN: A CHAP domain is present at the N-terminus and is associated
CC with the endopeptidase activity (PubMed:15256551). The CHAP domain is
CC responsible for nearly all the cell lysis activity (PubMed:16820517).
CC An Acm glycosidase domain is located in the central part of the protein
CC and is associated with the muramidase activity (PubMed:15256551). The
CC Acm domain seems to require the SH3b domain for activity
CC (PubMed:16820517). {ECO:0000269|PubMed:15256551,
CC ECO:0000269|PubMed:16820517}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family. {ECO:0000305}.
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DR EMBL; AY149214; AAN28166.2; -; Genomic_DNA.
DR SMR; Q8HA43; -.
DR CAZy; GH25; Glycoside Hydrolase Family 25.
DR GO; GO:0003796; F:lysozyme activity; IDA:UniProtKB.
DR GO; GO:0061785; F:peptidoglycan endopeptidase activity; IDA:UniProtKB.
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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR007921; CHAP_dom.
DR InterPro; IPR002053; Glyco_hydro_25.
DR InterPro; IPR018077; Glyco_hydro_fam25_subgr.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF01183; Glyco_hydro_25; 1.
DR SMART; SM00641; Glyco_25; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS50911; CHAP; 1.
DR PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
PE 1: Evidence at protein level;
KW Antimicrobial; Bacteriolytic enzyme; Glycosidase; Hydrolase;
KW Multifunctional enzyme; Protease.
FT CHAIN 1..443
FT /note="D-alanyl-L-alanine endopeptidase"
FT /id="PRO_0000448054"
FT DOMAIN 1..131
FT /note="Peptidase C51"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00048"
FT DOMAIN 380..441
FT /note="SH3b"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
FT REGION 145..344
FT /note="Acm domain"
FT /evidence="ECO:0000269|PubMed:15256551"
FT ACT_SITE 26
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:15256551"
FT ACT_SITE 91
FT /note="Increases nucleophilicity of active site cys; for D-
FT alanyl-L-alanine endopeptidase activity"
FT /evidence="ECO:0000305|PubMed:15256551"
FT SITE 158
FT /note="Important for 1,4-N-acetylmuramidase activity"
FT /evidence="ECO:0000269|PubMed:15256551"
FT SITE 185
FT /note="Important for 1,4-N-acetylmuramidase activity"
FT /evidence="ECO:0000269|PubMed:15256551"
FT MUTAGEN 26
FT /note="C->S: No effect on glycosidase activity; complete
FT loss of endopeptidase activity."
FT /evidence="ECO:0000269|PubMed:15256551"
FT MUTAGEN 34
FT /note="C->S: Slight loss of glycosidase activity; 85% loss
FT of endopeptidase activity."
FT /evidence="ECO:0000269|PubMed:15256551"
FT MUTAGEN 44
FT /note="C->S: 30% loss of glycosidase activity; almost
FT complete loss of endopeptidase activity."
FT /evidence="ECO:0000269|PubMed:15256551"
FT MUTAGEN 91
FT /note="H->A: 40% loss of glycosidase activity; complete
FT loss of endopeptidase activity."
FT /evidence="ECO:0000269|PubMed:15256551"
FT MUTAGEN 158
FT /note="D->A: Almost 90% loss of glycosidase activity; no
FT effect on endopeptidase activity."
FT /evidence="ECO:0000269|PubMed:15256551"
FT MUTAGEN 185
FT /note="E->A: Major loss of glycosidase activity; no effect
FT on endopeptidase activity."
FT /evidence="ECO:0000269|PubMed:15256551"
SQ SEQUENCE 443 AA; 49672 MW; 2E39CC7A4050A9B7 CRC64;
MATYQEYKSR SNGNAYDIDG SFGAQCWDGY ADYCKYLGLP YANCTNTGYA RDIWEQRHEN
GILNYFDEVE VMQAGDVAIF MVVDGVTPYS HVAIFDSDAG GGYGWFLGQN QGGANGAYNL
VKIPYSATYP TAFRPKSFKN AVTVTDNTGL NKGDYFIDVS AYQQADLTTT CQQAGTTKTI
IKVSESIAWL SDRHQQQANT SDPIGYYHFG RFGGDSALAQ READLFLSNL PSKKVSYLVI
DYEDSASADK QANTNAVIAF MDKIASAGYK PIYYSYKPFT LNNIDYQKII AKYPNSIWIA
GYPDYEVRTE PLWEFFPSMD GVRWWQFTSV GVAGGLDKNI VLLADDSSKM DIPKVDKPQE
LTFYQKLATN TKLDNSNVPY YEATLSTDYY VESKPNASSA DKEFIKAGTR VRVYEKVNGW
SRINHPESAQ WVEDNYLVNA TDM
