GP13_BPPH2
ID GP13_BPPH2 Reviewed; 365 AA.
AC P15132; B3VMP9;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Morphogenesis protein 1 {ECO:0000303|Ref.3};
DE AltName: Full=Gene product 13 {ECO:0000303|PubMed:18394643};
DE Short=gp13 {ECO:0000303|PubMed:18394643};
DE AltName: Full=Protein p13 {ECO:0000305};
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 phi29 (Bacteriophage phi-29).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Salasmaviridae; Picovirinae; Salasvirus.
OX NCBI_TaxID=10756;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3803926; DOI=10.1016/0378-1119(86)90406-3;
RA Vlcek C., Paces V.;
RT "Nucleotide sequence of the late region of Bacillus phage phi 29 completes
RT the 19,285-bp sequence of phi 29 genome. Comparison with the homologous
RT sequence of phage PZA.";
RL Gene 46:215-225(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 239-365.
RX PubMed=3027653; DOI=10.1093/nar/14.24.10001;
RA Garvey K.J., Saedi M.S., Ito J.;
RT "Nucleotide sequence of Bacillus phage phi 29 genes 14 and 15: homology of
RT gene 15 with other phage lysozymes.";
RL Nucleic Acids Res. 14:10001-10008(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Villegas A.P., Lingohr E.J., Ceyssens P.-J., Kropinski A.M.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18394643; DOI=10.1016/j.jmb.2008.02.068;
RA Cohen D.N., Erickson S.E., Xiang Y., Rossmann M.G., Anderson D.L.;
RT "Multifunctional roles of a bacteriophage phi 29 morphogenetic factor in
RT assembly and infection.";
RL J. Mol. Biol. 378:804-817(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.37 ANGSTROMS) OF 1-334 IN COMPLEXES WITH ZINC AND
RP N-ACETYLGLUCOSAMINE OLIGOMER, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18606992; DOI=10.1073/pnas.0803787105;
RA Xiang Y., Morais M.C., Cohen D.N., Bowman V.D., Anderson D.L.,
RA Rossmann M.G.;
RT "Crystal and cryoEM structural studies of a cell wall degrading enzyme in
RT the bacteriophage phi29 tail.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:9552-9557(2008).
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:0000305|PubMed:18394643,
CC ECO:0000305|PubMed:18606992}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:18606992};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:18606992};
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:18394643,
CC ECO:0000269|PubMed:18606992}. Note=Located at the distal tip of the
CC tail knob.
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; M14782; AAA32286.1; -; Genomic_DNA.
DR EMBL; X04962; CAA28630.1; -; Genomic_DNA.
DR EMBL; EU771092; ACE96036.1; -; Genomic_DNA.
DR PIR; H25816; WMBP23.
DR RefSeq; YP_002004542.1; NC_011048.1.
DR PDB; 3CSQ; X-ray; 1.80 A; A/B/C/D=1-334.
DR PDB; 3CSR; X-ray; 1.80 A; A=1-159.
DR PDB; 3CSZ; X-ray; 1.80 A; A=1-159.
DR PDB; 3CT0; X-ray; 1.77 A; A=1-159.
DR PDB; 3CT1; X-ray; 1.51 A; A=1-159.
DR PDB; 3CT5; X-ray; 1.37 A; A=1-159.
DR PDBsum; 3CSQ; -.
DR PDBsum; 3CSR; -.
DR PDBsum; 3CSZ; -.
DR PDBsum; 3CT0; -.
DR PDBsum; 3CT1; -.
DR PDBsum; 3CT5; -.
DR SMR; P15132; -.
DR MEROPS; M23.008; -.
DR GeneID; 6446506; -.
DR KEGG; vg:6446506; -.
DR EvolutionaryTrace; P15132; -.
DR Proteomes; UP000001207; Genome.
DR GO; GO:0098023; C:virus tail, tip; IDA:UniProtKB.
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:0099002; P:viral genome ejection through host cell envelope, short tail mechanism; IEA:UniProtKB-KW.
DR GO; GO:0098004; P:virus tail fiber assembly; IDA:CACAO.
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 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Bacteriolytic enzyme;
KW 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; Reference proteome;
KW Viral genome ejection through host cell envelope;
KW Viral penetration into host cytoplasm; Viral release from host cell;
KW Viral short tail ejection system; Viral tail assembly; Virion;
KW Virus entry into host cell; Zinc.
FT CHAIN 1..365
FT /note="Morphogenesis protein 1"
FT /id="PRO_0000106595"
FT REGION 1..159
FT /note="Lysozyme-like glycosidase"
FT REGION 160..165
FT /note="Linker"
FT REGION 166..365
FT /note="Probable metalloendopeptidase"
FT ACT_SITE 45
FT /note="For lysozyme-like glycosidase activity"
FT /evidence="ECO:0000305"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:3CSZ, ECO:0007744|PDB:3CT0,
FT ECO:0007744|PDB:3CT1, ECO:0007744|PDB:3CT5"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:3CSZ, ECO:0007744|PDB:3CT0,
FT ECO:0007744|PDB:3CT1, ECO:0007744|PDB:3CT5"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:3CSZ, ECO:0007744|PDB:3CT0,
FT ECO:0007744|PDB:3CT1, ECO:0007744|PDB:3CT5"
FT BINDING 137..140
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:3CSZ, ECO:0007744|PDB:3CT0,
FT ECO:0007744|PDB:3CT1, ECO:0007744|PDB:3CT5"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:3CSQ"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:3CSQ"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:3CSQ"
FT CONFLICT 89
FT /note="D -> N (in Ref. 3; ACE96036)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="Missing (in Ref. 3; ACE96036)"
FT /evidence="ECO:0000305"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:3CT5"
FT HELIX 11..26
FT /evidence="ECO:0007829|PDB:3CT5"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:3CT5"
FT HELIX 32..46
FT /evidence="ECO:0007829|PDB:3CT5"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:3CT5"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:3CT5"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:3CT5"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:3CT5"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:3CT5"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:3CT5"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:3CT5"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:3CT5"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:3CT5"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:3CT5"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:3CSQ"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:3CSQ"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:3CSQ"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:3CSQ"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:3CSQ"
FT STRAND 208..217
FT /evidence="ECO:0007829|PDB:3CSQ"
FT TURN 218..221
FT /evidence="ECO:0007829|PDB:3CSQ"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:3CSQ"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:3CSQ"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:3CSQ"
FT STRAND 278..287
FT /evidence="ECO:0007829|PDB:3CSQ"
FT STRAND 292..302
FT /evidence="ECO:0007829|PDB:3CSQ"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:3CSQ"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:3CSQ"
SQ SEQUENCE 365 AA; 40925 MW; 08EEA78F2CF8CB48 CRC64;
MVYVSNKYLT MSEMKVNAQY ILNYLSSNGW TKQAICGMLG NMQSESTINP GLWQNLDEGN
TSLGFGLVQW TPASNYINWA NSQGLPYKDM DSELKRIIWE VNNNAQWINL RDMTFKEYIK
STKTPRELAM IFLASYERPA NPNQPERGDQ AEYWYKNLSG GGGGGLQLAQ FPMDIINISQ
GENGSFSHKG TLCIDFVGKT EKYPYYAPCD CTCVWRGDAS AYLAWTSDKE VMCADGSVRY
ITWVNVHESP LPFDVGKKLK KGDLMGHTGI GGNVTGDHWH FNVIDGKEYQ GWTKKPDSCL
AGTELHIYDV FAVNNVEIIN GNGYDWKTSD WQDGDGGDGD DDNDNNKTKD LITLLLSDAL
HGWKA
