RECR_BPP1
ID RECR_BPP1 Reviewed; 343 AA.
AC P06956;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Recombinase cre;
GN Name=cre;
OS Escherichia phage P1 (Bacteriophage P1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Punavirus.
OX NCBI_TaxID=2886926;
OH NCBI_TaxID=543; Enterobacteriaceae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3486297; DOI=10.1016/0022-2836(86)90228-7;
RA Sternberg N., Sauer B., Hoess R., Abremski K.;
RT "Bacteriophage P1 cre gene and its regulatory region. Evidence for multiple
RT promoters and for regulation by DNA methylation.";
RL J. Mol. Biol. 187:197-212(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15489417; DOI=10.1128/jb.186.21.7032-7068.2004;
RA Lobocka M.B., Rose D.J., Plunkett G. III, Rusin M., Samojedny A.,
RA Lehnherr H., Yarmolinsky M.B., Blattner F.R.;
RT "Genome of bacteriophage P1.";
RL J. Bacteriol. 186:7032-7068(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=9288963; DOI=10.1038/37925;
RA Guo F., Gopaul D.N., van Duyne G.D.;
RT "Structure of Cre recombinase complexed with DNA in a site-specific
RT recombination synapse.";
RL Nature 389:40-46(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=9670032; DOI=10.1093/emboj/17.14.4175;
RA Gopaul D.N., Guo F., van Duyne G.D.;
RT "Structure of the Holliday junction intermediate in Cre-loxP site-specific
RT recombination.";
RL EMBO J. 17:4175-4187(1998).
CC -!- FUNCTION: Catalyzes site-specific recombination between two 34-base-
CC pair LOXP sites. Its role is to maintain the phage genome as a
CC monomeric unit-copy plasmid in the lysogenic state.
CC -!- SUBUNIT: Homotetramer when bound to DNA.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. {ECO:0000305}.
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DR EMBL; X03453; CAA27178.1; -; Genomic_DNA.
DR EMBL; AF234172; AAQ13978.1; -; Genomic_DNA.
DR PIR; B24836; RGBPP1.
DR RefSeq; YP_006472.1; NC_005856.1.
DR PDB; 1CRX; X-ray; 2.40 A; A/B=20-341.
DR PDB; 1DRG; X-ray; 2.55 A; A=21-343.
DR PDB; 1F44; X-ray; 2.05 A; A=20-343.
DR PDB; 1KBU; X-ray; 2.20 A; A/B=1-343.
DR PDB; 1MA7; X-ray; 2.30 A; A/B=1-343.
DR PDB; 1NZB; X-ray; 3.10 A; A/B/E/F=1-343.
DR PDB; 1OUQ; X-ray; 3.20 A; A/B/E/F=1-343.
DR PDB; 1PVP; X-ray; 2.35 A; A/B=2-343.
DR PDB; 1PVQ; X-ray; 2.75 A; A/B=2-343.
DR PDB; 1PVR; X-ray; 2.65 A; A/B=2-343.
DR PDB; 1Q3U; X-ray; 2.90 A; A/B/E/F=1-343.
DR PDB; 1Q3V; X-ray; 2.91 A; A/B/E/F=1-343.
DR PDB; 1XNS; X-ray; 2.80 A; A/B=20-343.
DR PDB; 1XO0; X-ray; 2.00 A; A/B=20-343.
DR PDB; 2CRX; X-ray; 2.50 A; A/B=1-343.
DR PDB; 2HOF; X-ray; 2.40 A; A/B=1-343.
DR PDB; 2HOI; X-ray; 2.60 A; A/B/G/H=1-343.
DR PDB; 3C28; X-ray; 2.60 A; A/B=20-341.
DR PDB; 3C29; X-ray; 2.20 A; A/B/G/H=20-341.
DR PDB; 3CRX; X-ray; 2.50 A; A/B=1-343.
DR PDB; 3MGV; X-ray; 2.29 A; A/B/C/D=1-343.
DR PDB; 4CRX; X-ray; 2.20 A; A/B=20-341.
DR PDB; 5CRX; X-ray; 2.70 A; A/B=1-343.
DR PDB; 7RHX; EM; 3.23 A; A/B/G/H=1-343.
DR PDB; 7RHY; EM; 3.91 A; A=1-343.
DR PDB; 7RHZ; EM; 4.48 A; A/B=1-343.
DR PDBsum; 1CRX; -.
DR PDBsum; 1DRG; -.
DR PDBsum; 1F44; -.
DR PDBsum; 1KBU; -.
DR PDBsum; 1MA7; -.
DR PDBsum; 1NZB; -.
DR PDBsum; 1OUQ; -.
DR PDBsum; 1PVP; -.
DR PDBsum; 1PVQ; -.
DR PDBsum; 1PVR; -.
DR PDBsum; 1Q3U; -.
DR PDBsum; 1Q3V; -.
DR PDBsum; 1XNS; -.
DR PDBsum; 1XO0; -.
DR PDBsum; 2CRX; -.
DR PDBsum; 2HOF; -.
DR PDBsum; 2HOI; -.
DR PDBsum; 3C28; -.
DR PDBsum; 3C29; -.
DR PDBsum; 3CRX; -.
DR PDBsum; 3MGV; -.
DR PDBsum; 4CRX; -.
DR PDBsum; 5CRX; -.
DR PDBsum; 7RHX; -.
DR PDBsum; 7RHY; -.
DR PDBsum; 7RHZ; -.
DR SMR; P06956; -.
DR DNASU; 2777477; -.
DR GeneID; 2777477; -.
DR KEGG; vg:2777477; -.
DR EvolutionaryTrace; P06956; -.
DR Proteomes; UP000008091; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.130; -; 1.
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 InterPro; IPR010998; Integrase_recombinase_N.
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;
KW Reference proteome.
FT CHAIN 1..343
FT /note="Recombinase cre"
FT /id="PRO_0000197529"
FT DOMAIN 18..103
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 130..338
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 324
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:1Q3U"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:1XO0"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1XO0"
FT HELIX 39..59
FT /evidence="ECO:0007829|PDB:1XO0"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:1F44"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:1XO0"
FT HELIX 85..102
FT /evidence="ECO:0007829|PDB:1XO0"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1XO0"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:1XO0"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:1XO0"
FT HELIX 155..170
FT /evidence="ECO:0007829|PDB:1XO0"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:1XO0"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1XO0"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:1XO0"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:1XO0"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:1XO0"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:1XO0"
FT HELIX 215..228
FT /evidence="ECO:0007829|PDB:1XO0"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:1XO0"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1PVQ"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:1XO0"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2CRX"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:2CRX"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:2CRX"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2CRX"
FT HELIX 258..273
FT /evidence="ECO:0007829|PDB:1XO0"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:1PVP"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:1KBU"
FT HELIX 290..301
FT /evidence="ECO:0007829|PDB:1XO0"
FT HELIX 306..313
FT /evidence="ECO:0007829|PDB:1XO0"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:1XO0"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:1XO0"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:1F44"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:1XO0"
FT HELIX 334..339
FT /evidence="ECO:0007829|PDB:1XO0"
SQ SEQUENCE 343 AA; 38540 MW; A05AC4300003FF34 CRC64;
MSNLLTVHQN LPALPVDATS DEVRKNLMDM FRDRQAFSEH TWKMLLSVCR SWAAWCKLNN
RKWFPAEPED VRDYLLYLQA RGLAVKTIQQ HLGQLNMLHR RSGLPRPSDS NAVSLVMRRI
RKENVDAGER AKQALAFERT DFDQVRSLME NSDRCQDIRN LAFLGIAYNT LLRIAEIARI
RVKDISRTDG GRMLIHIGRT KTLVSTAGVE KALSLGVTKL VERWISVSGV ADDPNNYLFC
RVRKNGVAAP SATSQLSTRA LEGIFEATHR LIYGAKDDSG QRYLAWSGHS ARVGAARDMA
RAGVSIPEIM QAGGWTNVNI VMNYIRNLDS ETGAMVRLLE DGD
