GP46_BPSP1
ID GP46_BPSP1 Reviewed; 77 AA.
AC O48400; B6V2I6;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Inhibitor of histone-like protein HU {ECO:0000305};
DE AltName: Full=Gene 46 protein {ECO:0000303|PubMed:35193978};
DE Short=Gp46 {ECO:0000303|PubMed:35193978};
DE AltName: Full=Gene product 46 {ECO:0000305};
GN Name=46 {ECO:0000312|EMBL:ACI90919.1};
GN ORFNames=SPO1_14 {ECO:0000312|EMBL:ACI90919.1};
OS Bacillus phage SP01 (Bacteriophage SP01).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Herelleviridae; Spounavirinae; Okubovirus.
OX NCBI_TaxID=10685 {ECO:0000312|Proteomes:UP000001590};
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1] {ECO:0000312|EMBL:AAC29015.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9657951; DOI=10.1006/viro.1998.9197;
RA Stewart C.R., Gaslightwala I., Hinata K., Krolikowski K.A., Needleman D.S.,
RA Peng A.S.-Y., Peterman M.A., Tobias A., Wei P.;
RT "Genes and regulatory sites of the 'host-takeover module' in the terminal
RT redundancy of Bacillus subtilis bacteriophage SPO1.";
RL Virology 246:329-340(1998).
RN [2] {ECO:0000312|EMBL:ACI90919.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19285085; DOI=10.1016/j.jmb.2009.03.009;
RA Stewart C.R., Casjens S.R., Cresawn S.G., Houtz J.M., Smith A.L.,
RA Ford M.E., Peebles C.L., Hatfull G.F., Hendrix R.W., Huang W.M.,
RA Pedulla M.L.;
RT "The genome of Bacillus subtilis bacteriophage SPO1.";
RL J. Mol. Biol. 388:48-70(2009).
RN [3] {ECO:0007744|PDB:7BY7}
RP STRUCTURE BY NMR, FUNCTION, INTERACTION WITH B.SUBTILIS HUPA, AND
RP MUTAGENESIS OF PHE-22 AND ASP-63.
RX PubMed=35193978; DOI=10.1073/pnas.2116278119;
RA Zhang P., Zhao X., Wang Y., Du K., Wang Z., Yu J., Chang G., Matthews S.,
RA Wang H., Liu B.;
RT "Bacteriophage protein Gp46 is a cross-species inhibitor of nucleoid-
RT associated HU proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 119:0-0(2022).
CC -!- FUNCTION: Acts as a host growth inhibitor by inhibiting DNA-binding of
CC microbial histone-like protein HU, thereby preventing chromosome
CC segregation and causing filamentous cell morphology and growth defects
CC in the host. {ECO:0000269|PubMed:35193978}.
CC -!- SUBUNIT: Interacts with host homodimeric histone-like protein (HU)
CC hupA; thereby replacing dsDNA from the HU-DNA complex.
CC {ECO:0000269|PubMed:35193978}.
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DR EMBL; AF031901; AAC29015.1; -; Genomic_DNA.
DR EMBL; FJ230960; ACI90919.1; -; Genomic_DNA.
DR RefSeq; YP_002300290.1; NC_011421.1.
DR PDB; 7BY7; NMR; -; A=1-77.
DR PDBsum; 7BY7; -.
DR SMR; O48400; -.
DR GeneID; 7009003; -.
DR KEGG; vg:7009003; -.
DR Proteomes; UP000001590; Genome.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Cell cycle; Growth arrest;
KW Host-virus interaction; Reference proteome.
FT CHAIN 1..77
FT /note="Inhibitor of histone-like protein HU"
FT /id="PRO_0000106152"
FT MUTAGEN 22
FT /note="F->A: Disrupts interaction with B.subtilis hupA.
FT Reduces host cell filamentation, nucleoid deformation and
FT inhibition of cell growth. No impact on B.subtilis growth
FT rate and morphology; when associated with Asn-63."
FT /evidence="ECO:0000269|PubMed:35193978"
FT MUTAGEN 63
FT /note="D->N: Weakens interaction with B.subtilis hupA.
FT Reduces host cell filamentation, nucleoid deformation and
FT inhibition of cell growth. No impact on B.subtilis growth
FT rate and morphology; when associated with Ala-22."
FT /evidence="ECO:0000269|PubMed:35193978"
FT MUTAGEN 63
FT /note="D->R: Abrogates tertiary structure folding."
FT /evidence="ECO:0000269|PubMed:35193978"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:7BY7"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:7BY7"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:7BY7"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:7BY7"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:7BY7"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:7BY7"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:7BY7"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:7BY7"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:7BY7"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:7BY7"
FT TURN 67..72
FT /evidence="ECO:0007829|PDB:7BY7"
SQ SEQUENCE 77 AA; 8989 MW; DFA3E89975061FAA CRC64;
MMTEDQKFKY LTKIEELEAG CFSDWTKEDI TGDLKYLKKG IIEESIELIR AVNGLTYSEE
LHDFTQEIIE ELDISPL
