GP13_BPPZA
ID GP13_BPPZA Reviewed; 365 AA.
AC P07538;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Morphogenesis protein 1 {ECO:0000250|UniProtKB:P15132};
DE AltName: Full=Gene product 13 {ECO:0000250|UniProtKB:P15132};
DE Short=gp13 {ECO:0000250|UniProtKB:P15132};
DE AltName: Full=Protein p13 {ECO:0000250|UniProtKB:P15132};
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 PZA (Bacteriophage PZA).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Salasmaviridae; Picovirinae; Salasvirus; Bacillus virus PZA.
OX NCBI_TaxID=10757;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3095188; DOI=10.1016/0378-1119(86)90048-x;
RA Paces V., Vlcek C., Urbanek P.;
RT "Nucleotide sequence of the late region of Bacillus subtilis phage PZA, a
RT close relative of phi 29.";
RL Gene 44:107-114(1986).
CC -!- FUNCTION: May serve as a plug to restrain the highly pressurized
CC packaged genome and thus would be the first virion protein to contact
CC the host cell wall, degrading the peptidoglycan layer and thereby
CC facilitating viral genome entry into the host bacteria. Acts probably
CC as a multifunctional enzyme that degrades N-acetylglucosamine polymers
CC (in vitro) and cleaves the peptide cross-links of the host cell wall.
CC Essential for the tail assembly. {ECO:0000250|UniProtKB:P15132}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P15132};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P15132};
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P15132}.
CC Note=Located at the distal tip of the tail knob.
CC {ECO:0000250|UniProtKB:P15132}.
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; M11813; AAA88490.1; -; Genomic_DNA.
DR PIR; H24831; WMBP13.
DR SMR; P07538; -.
DR Proteomes; UP000000855; 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:0098932; P:disruption by virus of host cell wall peptidoglycan during virus entry; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0098003; P:viral tail assembly; 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 Degradation of host cell envelope components during virus entry;
KW Degradation of host peptidoglycans during virus entry; Glycosidase;
KW Hydrolase; Late protein; Metal-binding; Metalloprotease;
KW Multifunctional enzyme; Protease; Viral release from host cell;
KW Viral tail assembly; Virion; Virus entry into host cell; Zinc.
FT CHAIN 1..365
FT /note="Morphogenesis protein 1"
FT /id="PRO_0000106596"
FT REGION 1..159
FT /note="Lysozyme-like glycosidase"
FT /evidence="ECO:0000250|UniProtKB:P15132"
FT REGION 160..165
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:P15132"
FT REGION 166..365
FT /note="Probable metalloendopeptidase"
FT /evidence="ECO:0000250|UniProtKB:P15132"
FT ACT_SITE 45
FT /note="For lysozyme-like glycosidase activity"
FT /evidence="ECO:0000250|UniProtKB:P15132"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15132"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15132"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15132"
FT BINDING 137..140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15132"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15132"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15132"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15132"
SQ SEQUENCE 365 AA; 40919 MW; 2B9B7606A7498A5A CRC64;
MVYVSNKYLT MSEMKVNAQY ILNYLSNNGW TKQAICGMLG NMQSESTINP GLWQNLDEGN
TSLGFGLVQW TPASNYINWA NNQGIPYKNM DSELKRIIWE VNNNAQWNNL RDMTFKEYIK
STKTPRELAM IFLASYERPA NPNQPVRGDQ AEYWYKNLSG GGGGGLQLAQ FPMDIINITQ
GENGSFSHKG TLCIDFVGKT EKYPYYAPCD CTCVWRGDAS AYLAWTSDKE VMCADGSVRY
ITWVNVHESP LPFDVGKKLK KGDLMGHTGI GGNVTGDHWH FNVIDGKEYQ GWTKKPDSCL
AGTELHIYDV FAVNNVEIIN GNGYDWKTSD WQDGDGGDGG DDNENNKTKD LITLLLSDAL
HGWKA
