ID   VG13_BPB03              Reviewed;         365 AA.
AC   Q37894;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Morphogenesis protein 1;
DE   AltName: Full=Late protein GP13;
DE   Includes:
DE     RecName: Full=Lysozyme-like glycosidase;
DE              EC=3.2.1.-;
DE   Includes:
DE     RecName: Full=Probable metalloendopeptidase;
DE              EC=3.4.-.-;
GN   Name=13;
OS   Bacillus phage B103 (Bacteriophage B103).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Salasmaviridae; Picovirinae; Beecentumtrevirus.
OX   NCBI_TaxID=10778;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9358052; DOI=10.1016/s0378-1119(97)00363-6;
RA   Pecenkova T., Benes V., Paces J., Vlcek C., Paces V.;
RT   "Bacteriophage B103: complete DNA sequence of its genome and relationship
RT   to other Bacillus phages.";
RL   Gene 199:157-163(1997).
CC   -!- FUNCTION: Essential for tail assembly and the production of infectious
CC       particles (By similarity). Degrades the peptidoglycan layer of the host
CC       cell wall and thereby facilitates infection of host bacteria. Acts
CC       probably as multifunctional enzyme that degrades N-acetylglucosamine
CC       polymers (in vitro) and cleaves the peptide cross-links of the host
CC       cell wall (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Note=Located at the end of
CC       the tail structure. {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the glycosyl
CC       hydrolase 24 family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M23B
CC       family. {ECO:0000305}.
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DR   EMBL; X99260; CAA67661.1; -; Genomic_DNA.
DR   RefSeq; NP_690647.1; NC_004165.1.
DR   SMR; Q37894; -.
DR   MEROPS; M23.008; -.
DR   GeneID; 955363; -.
DR   KEGG; vg:955363; -.
DR   Proteomes; UP000000971; Genome.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.70.70.10; -; 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR041219; Phage_lysozyme2.
DR   Pfam; PF18013; Phage_lysozyme2; 1.
DR   SUPFAM; SSF51261; SSF51261; 1.
PE   3: Inferred from homology;
KW   Antimicrobial; Bacteriolytic enzyme; Cell wall biogenesis/degradation;
KW   Glycosidase; Hydrolase; Late protein; Metal-binding; Metalloprotease;
KW   Multifunctional enzyme; Protease; Virion; Zinc.
FT   CHAIN           1..365
FT                   /note="Morphogenesis protein 1"
FT                   /id="PRO_0000106594"
FT   REGION          1..159
FT                   /note="Lysozyme-like glycosidase"
FT                   /evidence="ECO:0000250"
FT   REGION          160..165
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          166..365
FT                   /note="Probable metalloendopeptidase"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        45
FT                   /note="For lysozyme-like glycosidase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         137..140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   365 AA;  41284 MW;  00FAFA4C72E3D22D CRC64;
     MFYSKNAYLS MKEMTVNAQY ILNYLLPRGW TKNAICGMLG NMQTESTINP GIWQNLDEGN
     TSLGFGLVQW TPATKYLNWA DRNGLKRDHM DSQLKRILWE VDNNEQWINL RNMTFKEFTK
     STKSANELAM IFLASYERPA NPNQPERGTQ AEYWFKTLTG KGSTGIQLAQ FPMDIINITQ
     GENGSFSHKG TLCIDFVGKH EKYPYYAPCD CTCVWRGDES AYLAWTSDKE VMCADGTVRY
     ITWVCVHDEN LLYNVGKKLK KGELMGHSGK GGRATGDHLH LNVIEGNKYQ GWVKKPDSAL
     AGTELHIYDV FAVNGVEIVN GLGYDWKTSD WVDGSDENNG DDKDKDKDET KNIVNLLLCG
     ALNGW