LYSB_BPMD2
ID LYSB_BPMD2 Reviewed; 254 AA.
AC O64205;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 02-JUN-2021, entry version 62.
DE RecName: Full=Endolysin B {ECO:0000303|PubMed:19555454};
DE AltName: Full=Gene 12 protein {ECO:0000305};
DE AltName: Full=Gp12 {ECO:0000305};
DE AltName: Full=Mycolylarabinogalactan esterase {ECO:0000303|PubMed:19555454};
DE EC=3.1.-.- {ECO:0000269|PubMed:19555454};
GN Name=12;
OS Mycobacterium phage D29 (Mycobacteriophage D29).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Fromanvirus.
OX NCBI_TaxID=28369;
OH NCBI_TaxID=1763; Mycobacterium.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9636706; DOI=10.1006/jmbi.1997.1610;
RA Ford M.E., Sarkis G.J., Belanger A.E., Hendrix R.W., Hatfull G.F.;
RT "Genome structure of mycobacteriophage D29: implications for phage
RT evolution.";
RL J. Mol. Biol. 279:143-164(1998).
RN [2] {ECO:0007744|PDB:3HC7}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVE SITE, AND MUTAGENESIS OF SER-82.
RX PubMed=19555454; DOI=10.1111/j.1365-2958.2009.06775.x;
RA Payne K., Sun Q., Sacchettini J., Hatfull G.F.;
RT "Mycobacteriophage Lysin B is a novel mycolylarabinogalactan esterase.";
RL Mol. Microbiol. 73:367-381(2009).
CC -!- FUNCTION: Endolysin that degrades the junction between mycolic acid and
CC peptidoglycans in the host cell wall and participates with the holin
CC protein in the sequential events which lead to the programmed host cell
CC lysis releasing the mature viral particles. Once the holin has
CC permeabilized the host cell membrane, the endolysin can reach the
CC periplasm and break down the mycolic acid-rich outer membrane. Cleaves
CC the ester linkage joining the mycolic acid-rich outer membrane to
CC arabinogalactan, releasing free mycolic acids.
CC {ECO:0000269|PubMed:19555454}.
CC -!- SIMILARITY: Belongs to the L5likevirus endolysin B protein family.
CC {ECO:0000305}.
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DR EMBL; AF022214; AAC18452.1; -; Genomic_DNA.
DR PIR; A72801; A72801.
DR RefSeq; NP_046827.1; NC_001900.1.
DR PDB; 3HC7; X-ray; 2.00 A; A=1-254.
DR PDBsum; 3HC7; -.
DR SMR; O64205; -.
DR ESTHER; bpmd2-vg12; Lysin_B_C_ter.
DR GeneID; 1261627; -.
DR KEGG; vg:1261627; -.
DR EvolutionaryTrace; O64205; -.
DR Proteomes; UP000002131; Genome.
DR GO; GO:0016787; F:hydrolase activity; IDA:CACAO.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0044659; P:viral release from host cell by cytolysis; IDA:UniProtKB.
DR Gene3D; 1.10.10.1120; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000675; Cutinase/axe.
DR InterPro; IPR041855; Lysin_B_C_ter.
DR Pfam; PF01083; Cutinase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Bacteriolytic enzyme; Cytolysis;
KW Host cell lysis by virus; Hydrolase; Reference proteome;
KW Viral release from host cell.
FT CHAIN 1..254
FT /note="Endolysin B"
FT /id="PRO_0000164712"
FT ACT_SITE 82
FT /evidence="ECO:0000269|PubMed:19555454"
FT ACT_SITE 166
FT /evidence="ECO:0000305|PubMed:19555454"
FT ACT_SITE 240
FT /evidence="ECO:0000269|PubMed:19555454, ECO:0000305"
FT MUTAGEN 82
FT /note="S->A: Complete loss of mycolylarabinogalactan
FT esterase activity."
FT /evidence="ECO:0000269|PubMed:19555454"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:3HC7"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:3HC7"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:3HC7"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:3HC7"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:3HC7"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3HC7"
FT HELIX 50..70
FT /evidence="ECO:0007829|PDB:3HC7"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:3HC7"
FT HELIX 83..95
FT /evidence="ECO:0007829|PDB:3HC7"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:3HC7"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:3HC7"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:3HC7"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:3HC7"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:3HC7"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:3HC7"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:3HC7"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:3HC7"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:3HC7"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:3HC7"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:3HC7"
FT HELIX 212..230
FT /evidence="ECO:0007829|PDB:3HC7"
FT HELIX 245..251
FT /evidence="ECO:0007829|PDB:3HC7"
SQ SEQUENCE 254 AA; 28512 MW; 62CEF3CCD53E3379 CRC64;
MSKPWLFTVH GTGQPDPLGP GLPADTARDV LDIYRWQPIG NYPAAAFPMW PSVEKGVAEL
ILQIELKLDA DPYADFAMAG YSQGAIVVGQ VLKHHILPPT GRLHRFLHRL KKVIFWGNPM
RQKGFAHSDE WIHPVAAPDT LGILEDRLEN LEQYGFEVRD YAHDGDMYAS IKEDDLHEYE
VAIGRIVMKA SGFIGGRDSV VAQLIELGQR PITEGIALAG AIIDALTFFA RSRMGDKWPH
LYNRYPAVEF LRQI
