VINT_BPP2
ID VINT_BPP2 Reviewed; 337 AA.
AC P36932;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 23-FEB-2022, entry version 97.
DE RecName: Full=Integrase;
DE EC=2.7.7.- {ECO:0000305|PubMed:18284484};
DE EC=3.1.-.- {ECO:0000305|PubMed:18284484};
GN Name=int;
OS Escherichia phage P2 (Bacteriophage P2).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Peduovirinae; Peduovirus.
OX NCBI_TaxID=10679;
OH NCBI_TaxID=543; Enterobacteriaceae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2676729; DOI=10.1016/0378-1119(89)90244-8;
RA Yu A., Bertani E.L., Haggaard-Ljungquist E.;
RT "Control of prophage integration and excision in bacteriophage P2:
RT nucleotide sequences of the int gene and att sites.";
RL Gene 80:1-12(1989).
RN [2]
RP SEQUENCE REVISION TO 246 AND 255.
RA Christie G.E., Haggard-Ljungquist E., Calendar R.;
RT "The complete genome of bacteriophage P2.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=18284484; DOI=10.1111/j.1365-2672.2008.03748.x;
RA Frumerie C., Sylwan L., Helleday T., Yu A., Haggaard-Ljungquist E.;
RT "Bacteriophage P2 integrase: another possible tool for site-specific
RT recombination in eukaryotic cells.";
RL J. Appl. Microbiol. 105:290-299(2008).
RN [4]
RP FUNCTION.
RX PubMed=20627350; DOI=10.1016/j.virol.2010.05.009;
RA Sylwan L., Frumerie C., Haggaard-Ljungquist E.;
RT "Identification of bases required for P2 integrase core binding and
RT recombination.";
RL Virology 404:240-245(2010).
CC -!- FUNCTION: Integrase is necessary for integration of the phage into the
CC host genome by site-specific recombination.
CC {ECO:0000269|PubMed:18284484, ECO:0000269|PubMed:20627350}.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. {ECO:0000305}.
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DR EMBL; AF063097; AAD03297.1; -; Genomic_DNA.
DR RefSeq; NP_046786.1; NC_001895.1.
DR PDB; 5C6K; X-ray; 1.90 A; A/B=46-337.
DR PDB; 5DOR; X-ray; 2.50 A; A/B/C/D=162-337.
DR PDBsum; 5C6K; -.
DR PDBsum; 5DOR; -.
DR SMR; P36932; -.
DR MINT; P36932; -.
DR GeneID; 1261534; -.
DR KEGG; vg:1261534; -.
DR Proteomes; UP000009092; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR DisProt; DP00850; -.
DR Gene3D; 1.10.443.10; -; 1.
DR InterPro; IPR044068; CB.
DR InterPro; IPR011010; DNA_brk_join_enz.
DR InterPro; IPR013762; Integrase-like_cat_sf.
DR InterPro; IPR002104; Integrase_catalytic.
DR Pfam; PF00589; Phage_integrase; 1.
DR SUPFAM; SSF56349; SSF56349; 1.
DR PROSITE; PS51900; CB; 1.
DR PROSITE; PS51898; TYR_RECOMBINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA integration; DNA recombination; DNA-binding; Hydrolase;
KW Reference proteome; Transferase; Viral genome integration;
KW Virus entry into host cell.
FT CHAIN 1..337
FT /note="Integrase"
FT /id="PRO_0000197506"
FT DOMAIN 59..138
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 160..317
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 304
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:5C6K"
FT HELIX 179..191
FT /evidence="ECO:0007829|PDB:5C6K"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:5C6K"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:5C6K"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:5C6K"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:5C6K"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:5C6K"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:5C6K"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:5C6K"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:5C6K"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:5C6K"
FT HELIX 270..281
FT /evidence="ECO:0007829|PDB:5C6K"
FT HELIX 286..293
FT /evidence="ECO:0007829|PDB:5C6K"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:5C6K"
FT HELIX 302..307
FT /evidence="ECO:0007829|PDB:5C6K"
FT HELIX 314..318
FT /evidence="ECO:0007829|PDB:5C6K"
FT TURN 320..323
FT /evidence="ECO:0007829|PDB:5C6K"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:5DOR"
SQ SEQUENCE 337 AA; 38332 MW; C6FC3F87FD6F79DD CRC64;
MAIKKLDDGR YEVDIRPTGR NGKRIRRKFD KKSEAVAFEK YTLYNHHNKE WLSKPTDKRR
LSELTQIWWD LKGKHEEHGK SNLGKIEIFT KITNDPCAFQ ITKSLISQYC ATRRSQGIKP
SSINRDLTCI SGMFTALIEA ELFFGEHPIR GTKRLKEEKP ETGYLTQEEI ALLLAALDGD
NKKIAILCLS TGARWGEAAR LKAENIIHNR VTFVKTKTNK PRTVPISEAV AKMIADNKRG
FLFPDADYPR FRRTMKAIKP DLPMGQATHA LRHSFATHFM INGGSIITLQ RILGHTRIEQ
TMVYAHFAPE YLQDAISLNP LRGGTEAESV HTVSTVE
