ID   VXIS_LAMBD              Reviewed;          72 AA.
AC   P03699;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   02-JUN-2021, entry version 106.
DE   RecName: Full=Excisionase;
GN   Name=xis;
OS   Escherichia phage lambda (Bacteriophage lambda).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Lambdavirus.
OX   NCBI_TaxID=10710;
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=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   [3]
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   [4]
RP   INTERACTION WITH THE INTEGRASE.
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   FUNCTION, AND IDENTIFICATION IN THE EXCISION COMPLEX.
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   [6] {ECO:0007744|PDB:1LX8}
RP   STRUCTURE BY NMR OF 1-55.
RX   PubMed=12460578; DOI=10.1016/s0022-2836(02)01150-6;
RA   Sam M.D., Papagiannis C.V., Connolly K.M., Corselli L., Iwahara J., Lee J.,
RA   Phillips M., Wojciak J.M., Johnson R.C., Clubb R.T.;
RT   "Regulation of directionality in bacteriophage lambda site-specific
RT   recombination: structure of the Xis protein.";
RL   J. Mol. Biol. 324:791-805(2002).
RN   [7] {ECO:0007744|PDB:1RH6}
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-55.
RX   PubMed=15066428; DOI=10.1016/j.jmb.2004.02.053;
RA   Sam M.D., Cascio D., Johnson R.C., Clubb R.T.;
RT   "Crystal structure of the excisionase-DNA complex from bacteriophage
RT   lambda.";
RL   J. Mol. Biol. 338:229-240(2004).
RN   [8] {ECO:0007744|PDB:2OG0}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-52.
RX   PubMed=17275024; DOI=10.1016/j.jmb.2006.12.071;
RA   Papagiannis C.V., Sam M.D., Abbani M.A., Yoo D., Cascio D., Clubb R.T.,
RA   Johnson R.C.;
RT   "Fis targets assembly of the Xis nucleoprotein filament to promote excisive
RT   recombination by phage lambda.";
RL   J. Mol. Biol. 367:328-343(2007).
RN   [9] {ECO:0007744|PDB:2IEF}
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-55.
RX   PubMed=17287355; DOI=10.1073/pnas.0607820104;
RA   Abbani M.A., Papagiannis C.V., Sam M.D., Cascio D., Johnson R.C.,
RA   Clubb R.T.;
RT   "Structure of the cooperative Xis-DNA complex reveals a micronucleoprotein
RT   filament that regulates phage lambda intasome assembly.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2109-2114(2007).
CC   -!- FUNCTION: Part of the excision complex necessary for the excision of
CC       prophage from the host genome by site-specific recombination at the att
CC       site. {ECO:0000269|PubMed:25114241}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with the integrase (via N-terminus)
CC       (PubMed:12832614). Part of the excision complex made of the integrase
CC       tetramer, IHF, Fis and Xis (PubMed:25114241).
CC       {ECO:0000269|PubMed:12832614, ECO:0000269|PubMed:25114241}.
CC   -!- INTERACTION:
CC       P03699; P03699: xis; NbExp=2; IntAct=EBI-4479236, EBI-4479236;
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DR   EMBL; J02459; AAA96563.1; -; Genomic_DNA.
DR   PIR; C94164; RSBPXL.
DR   RefSeq; NP_040610.1; NC_001416.1.
DR   PDB; 1LX8; NMR; -; A=1-55.
DR   PDB; 1RH6; X-ray; 1.70 A; A/B=1-55.
DR   PDB; 2IEF; X-ray; 2.60 A; A/B/C=1-55.
DR   PDB; 2OG0; X-ray; 1.90 A; A/B=1-52.
DR   PDB; 5J0N; EM; 11.00 A; M/N/O=1-55.
DR   PDB; 6P0S; X-ray; 2.70 A; E=1-55.
DR   PDB; 6P0T; X-ray; 3.60 A; E=1-55.
DR   PDB; 6P0U; X-ray; 3.30 A; E/F=1-55.
DR   PDBsum; 1LX8; -.
DR   PDBsum; 1RH6; -.
DR   PDBsum; 2IEF; -.
DR   PDBsum; 2OG0; -.
DR   PDBsum; 5J0N; -.
DR   PDBsum; 6P0S; -.
DR   PDBsum; 6P0T; -.
DR   PDBsum; 6P0U; -.
DR   BMRB; P03699; -.
DR   SMR; P03699; -.
DR   DIP; DIP-60872N; -.
DR   IntAct; P03699; 3.
DR   GeneID; 2703504; -.
DR   KEGG; vg:2703504; -.
DR   EvolutionaryTrace; P03699; -.
DR   Proteomes; UP000001711; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0032359; P:provirus excision; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1660.20; -; 1.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR012884; Excisionase-like.
DR   InterPro; IPR038137; Excisionase-like_sf.
DR   Pfam; PF07825; Exc; 1.
DR   SUPFAM; SSF46955; SSF46955; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA recombination; DNA-binding; Reference proteome;
KW   Viral genome excision.
FT   CHAIN           1..72
FT                   /note="Excisionase"
FT                   /id="PRO_0000077714"
FT   STRAND          2..4
FT                   /evidence="ECO:0007829|PDB:2OG0"
FT   HELIX           5..10
FT                   /evidence="ECO:0007829|PDB:1RH6"
FT   STRAND          12..14
FT                   /evidence="ECO:0007829|PDB:1RH6"
FT   HELIX           18..26
FT                   /evidence="ECO:0007829|PDB:1RH6"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:1RH6"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:1RH6"
FT   STRAND          40..44
FT                   /evidence="ECO:0007829|PDB:1RH6"
SQ   SEQUENCE   72 AA;  8605 MW;  0E6A4843502200AA CRC64;
     MYLTLQEWNA RQRRPRSLET VRRWVRECRI FPPPVKDGRE YLFHESAVKV DLNRPVTGGL
     LKRIRNGKKA KS