FLP_YEAST
ID FLP_YEAST Reviewed; 423 AA.
AC P03870;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Site-specific recombinase Flp;
DE Short=FLP;
DE AltName: Full=Protein Able;
GN Name=FLP1; OrderedLocusNames=R0010W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OG Plasmid 2-micron.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A364A D5;
RX PubMed=6251374; DOI=10.1038/286860a0;
RA Hartley J.L., Donelson J.E.;
RT "Nucleotide sequence of the yeast plasmid.";
RL Nature 286:860-864(1980).
RN [2]
RP PROTEIN SEQUENCE OF 1-12.
RX PubMed=2995370; DOI=10.1016/s0021-9258(17)39027-0;
RA Babineau D., Vetter D., Andrews B.J., Gronostajski R.M., Proteau G.A.,
RA Beatty L.G., Sadowski P.D.;
RT "The FLP protein of the 2-micron plasmid of yeast. Purification of the
RT protein from Escherichia coli cells expressing the cloned FLP gene.";
RL J. Biol. Chem. 260:12313-12319(1985).
RN [3]
RP PROTEIN SEQUENCE OF 1-7; 124-129 AND 148-153, AND FUNCTION.
RX PubMed=2040639; DOI=10.1016/s0021-9258(18)99169-6;
RA Pan H., Clary D., Sadowski P.D.;
RT "Identification of the DNA-binding domain of the FLP recombinase.";
RL J. Biol. Chem. 266:11347-11354(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 250-423.
RX PubMed=386282; DOI=10.1093/nar/7.2.361;
RA Hindley J., Phear G.A.;
RT "Sequence of 1019 nucleotides encompassing one of the inverted repeats from
RT the yeast 2 micrometer plasmid.";
RL Nucleic Acids Res. 7:361-375(1979).
RN [5]
RP INDUCTION.
RX PubMed=2832156; DOI=10.1002/j.1460-2075.1987.tb02768.x;
RA Murray J.A.H., Scarpa M., Rossi N., Cesareni G.;
RT "Antagonistic controls regulate copy number of the yeast 2 micron
RT plasmid.";
RL EMBO J. 6:4205-4212(1987).
RN [6]
RP FUNCTION.
RX PubMed=3316982; DOI=10.1128/mcb.7.10.3566-3573.1987;
RA Reynolds A.E., Murray A.W.H., Szostak J.W.;
RT "Roles of the 2 microns gene products in stable maintenance of the 2
RT microns plasmid of Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 7:3566-3573(1987).
RN [7]
RP MUTAGENESIS OF TYR-343.
RX PubMed=3104911; DOI=10.1073/pnas.84.8.2189;
RA Prasad P.V., Young L.J., Jayaram M.;
RT "Mutations in the 2-microns circle site-specific recombinase that abolish
RT recombination without affecting substrate recognition.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:2189-2193(1987).
RN [8]
RP MUTAGENESIS OF HIS-305 AND ARG-308.
RX PubMed=2974924; DOI=10.1128/mcb.8.8.3303-3310.1988;
RA Parsons R.L., Prasad P.V., Harshey R.M., Jayaram M.;
RT "Step-arrest mutants of FLP recombinase: implications for the catalytic
RT mechanism of DNA recombination.";
RL Mol. Cell. Biol. 8:3303-3310(1988).
RN [9]
RP FUNCTION.
RX PubMed=2254930; DOI=10.1016/s0022-2836(05)80320-1;
RA Schwartz C.J., Sadowski P.D.;
RT "FLP protein of 2 mu circle plasmid of yeast induces multiple bends in the
RT FLP recognition target site.";
RL J. Mol. Biol. 216:289-298(1990).
RN [10]
RP ACTIVE SITE.
RX PubMed=2211714; DOI=10.1016/s0021-9258(17)44780-6;
RA Evans B.R., Chen J.W., Parsons R.L., Bauer T.K., Teplow D.B., Jayaram M.;
RT "Identification of the active site tyrosine of Flp recombinase. Possible
RT relevance of its location to the mechanism of recombination.";
RL J. Biol. Chem. 265:18504-18510(1990).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH DNA, AND SUBUNIT.
RX PubMed=11090626; DOI=10.1016/s1097-2765(05)00088-2;
RA Chen Y., Narendra U., Iype L.E., Cox M.M., Rice P.A.;
RT "Crystal structure of a Flp recombinase-Holliday junction complex: assembly
RT of an active oligomer by helix swapping.";
RL Mol. Cell 6:885-897(2000).
CC -!- FUNCTION: Part of the plasmid amplification system, which corrects any
CC decrease in copy number caused by a rare missegregation event.
CC Catalyzes the recombination between the large inverted repetitions of
CC the 2-micron plasmid during plasmid replication. This recombination
CC event changes the direction of one of the two replication forks in the
CC bidirectionally replicating molecule, effectively resulting in multiple
CC rounds of replication from a single initiation event. Binds
CC specifically to the FLP recognition target (FRT) site where it induces
CC DNA to bend. Three types of bend exist. Type I is approximately 60
CC degrees and results from 1 FLP molecule binding to 1 symmetry element.
CC Type II is >144 degrees and results from FLP molecules binding to
CC symmetry elements a and b. Type III is approximately 65 degrees and
CC results from FLP molecules binding to symmetry elements b and c.
CC {ECO:0000269|PubMed:2040639, ECO:0000269|PubMed:2254930,
CC ECO:0000269|PubMed:3316982}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11090626}.
CC -!- INDUCTION: Repressed by the negative regulatory complex REP1-REP2.
CC {ECO:0000269|PubMed:2832156}.
CC -!- MISCELLANEOUS: The plasmid 2-micron circle is a extrachromosomal
CC element that resides in the nucleus and propagates itself stably in
CC host cell populations. It provides no obvious advantage to the host but
CC imposes no significant disadvantage either at its steady-state copy
CC number of 40-60 molecules/cell.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. {ECO:0000305}.
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DR EMBL; J01347; AAB59340.1; -; Genomic_DNA.
DR PIR; A04502; PDBYA.
DR PDB; 1FLO; X-ray; 2.65 A; A/B/C/D=2-423.
DR PDB; 1M6X; X-ray; 2.80 A; A/B/C/D=1-423.
DR PDB; 1P4E; X-ray; 2.70 A; A/B=2-423, C/D=2-422.
DR PDBsum; 1FLO; -.
DR PDBsum; 1M6X; -.
DR PDBsum; 1P4E; -.
DR AlphaFoldDB; P03870; -.
DR SMR; P03870; -.
DR iPTMnet; P03870; -.
DR PRIDE; P03870; -.
DR SGD; S000029654; FLP1.
DR InParanoid; P03870; -.
DR EvolutionaryTrace; P03870; -.
DR PRO; PR:P03870; -.
DR Proteomes; UP000002311; Plasmid 2-micron.
DR RNAct; P03870; protein.
DR GO; GO:0008301; F:DNA binding, bending; IMP:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0009009; F:site-specific recombinase activity; IDA:SGD.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0042150; P:plasmid recombination; IDA:SGD.
DR Gene3D; 1.10.443.10; -; 1.
DR InterPro; IPR011010; DNA_brk_join_enz.
DR InterPro; IPR013762; Integrase-like_cat_sf.
DR InterPro; IPR005626; Recombinase_Flp_C.
DR InterPro; IPR022647; Recombinase_Flp_N.
DR Pfam; PF05202; Flp_C; 1.
DR Pfam; PF03930; Flp_N; 1.
DR SUPFAM; SSF56349; SSF56349; 1.
DR PROSITE; PS51899; TYR_RECOMBINASE_FLP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA integration;
KW DNA recombination; DNA-binding; Plasmid; Reference proteome.
FT CHAIN 1..423
FT /note="Site-specific recombinase Flp"
FT /id="PRO_0000197567"
FT DOMAIN 136..422
FT /note="Tyr recombinase Flp-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01247"
FT ACT_SITE 343
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01247,
FT ECO:0000269|PubMed:2211714"
FT MUTAGEN 305
FT /note="H->L,P: Inactive and weakened DNA binding."
FT /evidence="ECO:0000269|PubMed:2974924"
FT MUTAGEN 305
FT /note="H->Q: Reduced activity."
FT /evidence="ECO:0000269|PubMed:2974924"
FT MUTAGEN 308
FT /note="R->G: Inactive and weakened DNA binding."
FT /evidence="ECO:0000269|PubMed:2974924"
FT MUTAGEN 343
FT /note="Y->F,S: No strand cleavage or recombination."
FT /evidence="ECO:0000269|PubMed:3104911"
FT CONFLICT 5
FT /note="G -> D (in Ref. 2; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:1FLO"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:1FLO"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1FLO"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:1FLO"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:1FLO"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 116..128
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:1FLO"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1M6X"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:1FLO"
FT TURN 164..168
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 172..188
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:1FLO"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:1FLO"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:1FLO"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:1FLO"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:1FLO"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 241..251
FT /evidence="ECO:0007829|PDB:1FLO"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:1P4E"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 279..290
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 306..317
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 324..328
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 337..340
FT /evidence="ECO:0007829|PDB:1FLO"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:1P4E"
FT HELIX 352..358
FT /evidence="ECO:0007829|PDB:1FLO"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:1FLO"
FT TURN 366..369
FT /evidence="ECO:0007829|PDB:1FLO"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 380..389
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 395..399
FT /evidence="ECO:0007829|PDB:1FLO"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:1FLO"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:1P4E"
FT HELIX 409..420
FT /evidence="ECO:0007829|PDB:1FLO"
SQ SEQUENCE 423 AA; 48620 MW; B9C3DE95AB253BC3 CRC64;
MPQFGILCKT PPKVLVRQFV ERFERPSGEK IALCAAELTY LCWMITHNGT AIKRATFMSY
NTIISNSLSF DIVNKSLQFK YKTQKATILE ASLKKLIPAW EFTIIPYYGQ KHQSDITDIV
SSLQLQFESS EEADKGNSHS KKMLKALLSE GESIWEITEK ILNSFEYTSR FTKTKTLYQF
LFLATFINCG RFSDIKNVDP KSFKLVQNKY LGVIIQCLVT ETKTSVSRHI YFFSARGRID
PLVYLDEFLR NSEPVLKRVN RTGNSSSNKQ EYQLLKDNLV RSYNKALKKN APYSIFAIKN
GPKSHIGRHL MTSFLSMKGL TELTNVVGNW SDKRASAVAR TTYTHQITAI PDHYFALVSR
YYAYDPISKE MIALKDETNP IEEWQHIEQL KGSAEGSIRY PAWNGIISQE VLDYLSSYIN
RRI
