ID VINT_LAMBD Reviewed; 356 AA.
AC P03700;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 08-NOV-2023, entry version 146.
DE RecName: Full=Integrase;
DE EC=2.7.7.- {ECO:0000269|PubMed:15973401};
DE EC=3.1.-.- {ECO:0000269|PubMed:15973401};
GN Name=int;
OS Escherichia phage lambda (Bacteriophage lambda).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Lambdavirus; Lambdavirus lambda.
OX NCBI_TaxID=2681611;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6221115; DOI=10.1016/0022-2836(82)90546-0;
RA Sanger F., Coulson A.R., Hong G.F., Hill D.F., Petersen G.B.;
RT "Nucleotide sequence of bacteriophage lambda DNA.";
RL J. Mol. Biol. 162:729-773(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6446713; DOI=10.1073/pnas.77.5.2482;
RA Hoess R.H., Foeller C., Bidwell K., Landy A.;
RT "Site-specific recombination functions of bacteriophage lambda: DNA
RT sequence of regulatory regions and overlapping structural genes for Int and
RT Xis.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:2482-2486(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6253947; DOI=10.1093/nar/8.8.1765;
RA Davies R.W.;
RT "DNA sequence of the int-xis-Pi region of the bacteriophage lambda; overlap
RT of the int and xis genes.";
RL Nucleic Acids Res. 8:1765-1782(1980).
RN [4]
RP INTERACTION WITH THE EXCISIONASE, AND MUTAGENESIS OF GLU-47.
RX PubMed=12832614; DOI=10.1073/pnas.1033041100;
RA Warren D., Sam M.D., Manley K., Sarkar D., Lee S.Y., Abbani M.,
RA Wojciak J.M., Clubb R.T., Landy A.;
RT "Identification of the lambda integrase surface that interacts with Xis
RT reveals a residue that is also critical for Int dimer formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8176-8181(2003).
RN [5]
RP REVIEW, AND FUNCTION.
RX PubMed=16139195; DOI=10.1016/j.cub.2005.08.031;
RA Van Duyne G.D.;
RT "Lambda integrase: armed for recombination.";
RL Curr. Biol. 15:R658-R660(2005).
RN [6]
RP IDENTIFICATION IN THE EXCISION COMPLEX, AND SUBUNIT.
RX PubMed=25114241; DOI=10.1073/pnas.1413019111;
RA Seah N.E., Warren D., Tong W., Laxmikanthan G., Van Duyne G.D., Landy A.;
RT "Nucleoprotein architectures regulating the directionality of viral
RT integration and excision.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12372-12377(2014).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 177-356.
RX PubMed=9082984; DOI=10.1126/science.276.5309.126;
RA Kwon H.J., Tirumalai R., Landy A., Ellenberger T.;
RT "Flexibility in DNA recombination: structure of the lambda integrase
RT catalytic core.";
RL Science 276:126-131(1997).
RN [8]
RP STRUCTURE BY NMR OF 1-64.
RX PubMed=11904406; DOI=10.1073/pnas.052017999;
RA Wojciak J.M., Sarkar D., Landy A., Clubb R.T.;
RT "Arm-site binding by lambda-integrase: solution structure and functional
RT characterization of its amino-terminal domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:3434-3439(2002).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 74-356 IN COMPLEX WITH
RP PHOSPHOTYROSINE.
RX PubMed=12887904; DOI=10.1016/s1097-2765(03)00268-5;
RA Aihara H., Kwon H.J., Nunes-Duby S.E., Landy A., Ellenberger T.;
RT "A conformational switch controls the DNA cleavage activity of lambda
RT integrase.";
RL Mol. Cell 12:187-198(2003).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 74-356 IN COMPLEX WITH
RP PHOSPHOTYROSINE, AND ACTIVE SITE.
RX PubMed=15973401; DOI=10.1038/nature03657;
RA Biswas T., Aihara H., Radman-Livaja M., Filman D., Landy A.,
RA Ellenberger T.;
RT "A structural basis for allosteric control of DNA recombination by lambda
RT integrase.";
RL Nature 435:1059-1066(2005).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 75-176.
RX PubMed=18540053; DOI=10.1107/s174430910801381x;
RA Kamadurai H.B., Jain R., Foster M.P.;
RT "Crystallization and structure determination of the core-binding domain of
RT bacteriophage lambda integrase.";
RL Acta Crystallogr. F 64:470-473(2008).
RN [12]
RP STRUCTURE BY NMR OF 1-64.
RX PubMed=19324050; DOI=10.1016/j.jmb.2009.03.041;
RA Fadeev E.A., Sam M.D., Clubb R.T.;
RT "NMR structure of the amino-terminal domain of the lambda integrase protein
RT in complex with DNA: immobilization of a flexible tail facilitates beta-
RT sheet recognition of the major groove.";
RL J. Mol. Biol. 388:682-690(2009).
CC -!- FUNCTION: Integrase is necessary for integration of the phage into the
CC host genome by site-specific recombination. In conjunction with
CC excisionase, integrase is also necessary for excision of the prophage
CC from the host genome. {ECO:0000269|PubMed:15973401,
CC ECO:0000303|PubMed:16139195}.
CC -!- SUBUNIT: Homotetramer. Interacts (via N-terminus) with the excisionase
CC (via C-terminus) (PubMed:12832614). Part of the excision complex made
CC of the integrase tetramer, IHF, Fis and Xis.
CC {ECO:0000269|PubMed:12832614, ECO:0000269|PubMed:25114241}.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J02459; AAA96562.1; -; Genomic_DNA.
DR PIR; A04322; RSBPIL.
DR RefSeq; NP_040609.1; NC_001416.1.
DR PDB; 1AE9; X-ray; 1.90 A; A/B=177-355.
DR PDB; 1KJK; NMR; -; A=1-64.
DR PDB; 1P7D; X-ray; 2.95 A; A/B=74-356.
DR PDB; 1Z19; X-ray; 2.80 A; A/B=74-356.
DR PDB; 1Z1B; X-ray; 3.80 A; A/B=1-356.
DR PDB; 1Z1G; X-ray; 4.40 A; A/B/C/D=1-356.
DR PDB; 2OXO; X-ray; 2.00 A; A=75-176.
DR PDB; 2WCC; NMR; -; 3=1-64.
DR PDB; 5J0N; EM; 11.00 A; E/F/G/H=1-356.
DR PDBsum; 1AE9; -.
DR PDBsum; 1KJK; -.
DR PDBsum; 1P7D; -.
DR PDBsum; 1Z19; -.
DR PDBsum; 1Z1B; -.
DR PDBsum; 1Z1G; -.
DR PDBsum; 2OXO; -.
DR PDBsum; 2WCC; -.
DR PDBsum; 5J0N; -.
DR SMR; P03700; -.
DR DIP; DIP-41000N; -.
DR IntAct; P03700; 10.
DR GeneID; 2703464; -.
DR KEGG; vg:2703470; -.
DR OrthoDB; 3373at10239; -.
DR EvolutionaryTrace; P03700; -.
DR Proteomes; UP000001711; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008907; F:integrase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0015074; P:DNA integration; IDA:CACAO.
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:0032359; P:provirus excision; 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 CDD; cd00800; INT_Lambda_C; 1.
DR Gene3D; 1.10.150.130; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 1.10.443.10; Intergrase catalytic core; 1.
DR InterPro; IPR044068; CB.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR011010; DNA_brk_join_enz.
DR InterPro; IPR013762; Integrase-like_cat_sf.
DR InterPro; IPR002104; Integrase_catalytic.
DR InterPro; IPR015094; Integrase_lambda-typ_DNA-bd_N.
DR InterPro; IPR010998; Integrase_recombinase_N.
DR InterPro; IPR004107; Integrase_SAM-like_N.
DR PANTHER; PTHR30629; PROPHAGE INTEGRASE; 1.
DR PANTHER; PTHR30629:SF2; PROPHAGE INTEGRASE INTS-RELATED; 1.
DR Pfam; PF09003; Arm-DNA-bind_1; 1.
DR Pfam; PF02899; Phage_int_SAM_1; 1.
DR Pfam; PF00589; Phage_integrase; 1.
DR SUPFAM; SSF56349; DNA breaking-rejoining enzymes; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 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 excision;
KW Viral genome integration; Virus entry into host cell.
FT CHAIN 1..356
FT /note="Integrase"
FT /id="PRO_0000197527"
FT DOMAIN 74..155
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 175..355
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 342
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246,
FT ECO:0007744|PDB:1P7D, ECO:0007744|PDB:1Z19,
FT ECO:0007744|PDB:1Z1B"
FT MUTAGEN 47
FT /note="E->A: Complete loss of interaction with the
FT integrase."
FT /evidence="ECO:0000269|PubMed:12832614"
FT CONFLICT 118
FT /note="D -> V (in Ref. 3)"
FT /evidence="ECO:0000305"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:2WCC"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1KJK"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:1KJK"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:1KJK"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:1KJK"
FT HELIX 41..57
FT /evidence="ECO:0007829|PDB:1KJK"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:2OXO"
FT HELIX 94..110
FT /evidence="ECO:0007829|PDB:2OXO"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2OXO"
FT HELIX 121..133
FT /evidence="ECO:0007829|PDB:2OXO"
FT HELIX 137..156
FT /evidence="ECO:0007829|PDB:2OXO"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:1Z19"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:1AE9"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:1AE9"
FT HELIX 198..209
FT /evidence="ECO:0007829|PDB:1AE9"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:1AE9"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:1AE9"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:1AE9"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:1AE9"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:1AE9"
FT TURN 249..252
FT /evidence="ECO:0007829|PDB:1AE9"
FT HELIX 255..265
FT /evidence="ECO:0007829|PDB:1AE9"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:1AE9"
FT HELIX 282..296
FT /evidence="ECO:0007829|PDB:1AE9"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:1AE9"
FT HELIX 309..321
FT /evidence="ECO:0007829|PDB:1AE9"
FT HELIX 324..331
FT /evidence="ECO:0007829|PDB:1AE9"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:1Z19"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:1Z19"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:1AE9"
SQ SEQUENCE 356 AA; 40304 MW; 708D52B96E89209C CRC64;
MGRRRSHERR DLPPNLYIRN NGYYCYRDPR TGKEFGLGRD RRIAITEAIQ ANIELFSGHK
HKPLTARINS DNSVTLHSWL DRYEKILASR GIKQKTLINY MSKIKAIRRG LPDAPLEDIT
TKEIAAMLNG YIDEGKAASA KLIRSTLSDA FREAIAEGHI TTNHVAATRA AKSEVRRSRL
TADEYLKIYQ AAESSPCWLR LAMELAVVTG QRVGDLCEMK WSDIVDGYLY VEQSKTGVKI
AIPTALHIDA LGISMKETLD KCKEILGGET IIASTRREPL SSGTVSRYFM RARKASGLSF
EGDPPTFHEL RSLSARLYEK QISDKFAQHL LGHKSDTMAS QYRDDRGREW DKIEIK
//
