VHLP_ASFB7
ID VHLP_ASFB7 Reviewed; 104 AA.
AC P68742; P43272;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Viral histone-like protein;
DE AltName: Full=DNA-binding protein pA104R {ECO:0000303|PubMed:30185597};
DE AltName: Full=pA104R;
GN OrderedLocusNames=BA71V-033; ORFNames=A104R;
OS African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10498;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA Rodriguez J.F., Vinuela E.;
RT "Analysis of the complete nucleotide sequence of African swine fever
RT virus.";
RL Virology 208:249-278(1995).
RN [2]
RP CHARACTERIZATION.
RX PubMed=12029148; DOI=10.1099/0022-1317-83-6-1331;
RA Kollnberger S.D., Gutierrez-Castaneda B., Foster-Cuevas M., Corteyn A.,
RA Parkhouse R.M.;
RT "Identification of the principal serological immunodeterminants of African
RT swine fever virus by screening a virus cDNA library with antibody.";
RL J. Gen. Virol. 83:1331-1342(2002).
RN [3]
RP HOST ANTIBODY RESPONSE.
RX PubMed=17698651; DOI=10.1099/vir.0.82857-0;
RA Reis A.L., Parkhouse R.M., Penedos A.R., Martins C., Leitao A.;
RT "Systematic analysis of longitudinal serological responses of pigs infected
RT experimentally with African swine fever virus.";
RL J. Gen. Virol. 88:2426-2434(2007).
RN [4]
RP DNA-BINDING, FUNCTION, MUTAGENESIS OF ARG-69 AND PRO-74, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=28381576; DOI=10.1128/jvi.02498-16;
RA Frouco G., Freitas F.B., Coelho J., Leitao A., Martins C., Ferreira F.;
RT "DNA-Binding properties of African swine fever virus pA104R, a histone-Like
RT protein involved in viral replication and transcription.";
RL J. Virol. 91:0-0(2017).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=30185597; DOI=10.1128/jvi.01293-18;
RA Alejo A., Matamoros T., Guerra M., Andres G.;
RT "A Proteomic Atlas of the African Swine Fever Virus Particle.";
RL J. Virol. 92:0-0(2018).
RN [6]
RP INDUCTION.
RX PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA Dixon L., Werner F.;
RT "The African Swine Fever Virus Transcriptome.";
RL J. Virol. 94:0-0(2020).
RN [7] {ECO:0007744|PDB:6LMH, ECO:0007744|PDB:6LMJ}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), DNA-BINDING, ACTIVITY REGULATION,
RP AND SUBUNIT.
RX PubMed=32358196; DOI=10.1073/pnas.1922523117;
RA Liu R., Sun Y., Chai Y., Li S., Li S., Wang L., Su J., Yu S., Yan J.,
RA Gao F., Zhang G., Qiu H.J., Gao G.F., Qi J., Wang H.;
RT "The structural basis of African swine fever virus pA104R binding to DNA
RT and its inhibition by stilbene derivatives.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:11000-11009(2020).
CC -!- FUNCTION: DNA-binding protein that plays a critical role in nucleoid
CC compaction, genome replication and DNA replication and transcription
CC (PubMed:28381576). Binds to both ssDNA and dsDNA with a binding site
CC covering about 15 nucleotides (PubMed:28381576). Displays DNA-
CC supercoiling activity only when associated with the viral DNA
CC topoisomerase 2 (PubMed:28381576). {ECO:0000269|PubMed:28381576}.
CC -!- ACTIVITY REGULATION: Stilbene derivatives SD1 and SD4 disrupt the
CC binding between pA104R and DNA and inhibit the viral replication in
CC primary alveolar macrophages. {ECO:0000269|PubMed:32358196}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:32358196}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:30185597}. Note=Found
CC in association with viral nucleoid. {ECO:0000269|PubMed:30185597}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000269|PubMed:28381576, ECO:0000269|PubMed:32075923}.
CC -!- DISRUPTION PHENOTYPE: Knockout of the viral histone-like protein leads
CC to reduced levels of the mRNA coding for the capsid protein and to a
CC reduced number of viral progeny. {ECO:0000269|PubMed:28381576}.
CC -!- MISCELLANEOUS: Host antibody response against A104R protein is higher
CC in asymptomatic than in chronically infected hosts.
CC {ECO:0000269|PubMed:17698651}.
CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family.
CC {ECO:0000305}.
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DR EMBL; U18466; AAA65264.1; -; Genomic_DNA.
DR RefSeq; NP_042728.1; NC_001659.2.
DR PDB; 6LMH; X-ray; 2.81 A; A/B=1-104.
DR PDB; 6LMJ; X-ray; 2.80 A; A/B=1-104.
DR PDBsum; 6LMH; -.
DR PDBsum; 6LMJ; -.
DR SMR; P68742; -.
DR GeneID; 22220416; -.
DR KEGG; vg:22220416; -.
DR Proteomes; UP000000624; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 4.10.520.10; -; 1.
DR InterPro; IPR000119; Hist_DNA-bd.
DR InterPro; IPR020816; Histone-like_DNA-bd_CS.
DR InterPro; IPR010992; IHF-like_DNA-bd_dom_sf.
DR PANTHER; PTHR33175; PTHR33175; 1.
DR Pfam; PF00216; Bac_DNA_binding; 1.
DR SMART; SM00411; BHL; 1.
DR SUPFAM; SSF47729; SSF47729; 1.
DR PROSITE; PS00045; HISTONE_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; Late protein;
KW Reference proteome; Virion.
FT CHAIN 1..104
FT /note="Viral histone-like protein"
FT /id="PRO_0000105083"
FT SITE 57
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:32358196"
FT SITE 69
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:28381576,
FT ECO:0000269|PubMed:32358196"
FT SITE 72
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:32358196"
FT SITE 74
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:32358196"
FT SITE 83
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:32358196"
FT SITE 85
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:32358196"
FT SITE 92
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:32358196"
FT SITE 94
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:32358196"
FT SITE 96
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:32358196"
FT SITE 97
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:32358196"
FT MUTAGEN 69
FT /note="R->A: Drastic loss of DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:28381576"
FT MUTAGEN 69
FT /note="R->K: No effect on DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:28381576"
FT MUTAGEN 74
FT /note="P->A: No effect on DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:28381576"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:6LMJ"
FT HELIX 26..45
FT /evidence="ECO:0007829|PDB:6LMJ"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:6LMJ"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:6LMJ"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:6LMJ"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6LMJ"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:6LMJ"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:6LMJ"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:6LMJ"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:6LMJ"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:6LMJ"
SQ SEQUENCE 104 AA; 11609 MW; 939515B48C793AF8 CRC64;
MSTKKKPTIT KQELYSLVAA DTQLNKALIE RIFTSQQKII QNALKHNQEV IIPPGIKFTV
VTVKAKPARQ GHNPATGEPI QIKAKPEHKA VKIRALKPVH DMLN
