Site-specific recombinase Flp - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P03870 (FLP_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 98. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Site-specific recombinase Flp
Short name=FLP

Alternative name(s):
Protein Able

Gene names

Name:	FLP1
Ordered Locus Names:	R0010W

Encoded on

Plasmid 2-micron

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	423 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Part of the plasmid amplification system, which corrects any decrease in copy number caused by a rare missegregation event. Catalyzes the recombination between the large inverted repetitions of the 2-micron plasmid during plasmid replication. This recombination event changes the direction of one of the two replication forks in the bidirectionally replicating molecule, effectively resulting in multiple rounds of replication from a single initiation event. Binds specifically to the FLP recognition target (FRT) site where it induces DNA to bend. Three types of bend exist. Type I is approximately 60 degrees and results from 1 FLP molecule binding to 1 symmetry element. Type II is >144 degrees and results from FLP molecules binding to symmetry elements a and b. Type III is approximately 65 degrees and results from FLP molecules binding to symmetry elements b and c. Ref.3 Ref.6 Ref.9
Subunit structure	Homotetramer. Ref.11
Induction	Repressed by the negative regulatory complex REP1-REP2. Ref.5
Miscellaneous	The plasmid 2-micron circle is a extrachromosomal element that resides in the nucleus and propagates itself stably in host cell populations. It provides no obvious advantage to the host but imposes no significant disadvantage either at its steady-state copy number of 40-60 molecules/cell.
Sequence similarities	Belongs to the 'phage' integrase family.

Ontologies

Keywords
Biological process	DNA integration DNA recombination
Ligand	DNA-binding
Technical term	3D-structure Complete proteome Direct protein sequencing Plasmid Reference proteome
Gene Ontology (GO)
Biological_process	DNA integration Inferred from electronic annotation. Source: UniProtKB-KW plasmid recombination Inferred from direct assay PubMed 6308608. Source: SGD
Molecular_function	DNA binding, bending Inferred from mutant phenotype PubMed 2648010. Source: SGD double-stranded DNA binding Inferred from direct assay PubMed 2427927. Source: SGD single-stranded DNA binding Inferred from direct assay PubMed 9469845. Source: SGD site-specific recombinase activity Inferred from direct assay PubMed 6286142. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 423

423

Site-specific recombinase Flp

PRO_0000197567

Sites

Active site

343

O-(3'-phospho-DNA)-tyrosine intermediate Ref.10

Experimental info

Mutagenesis

305

H → L or P: Inactive and weakened DNA binding. Ref.8

Mutagenesis

305

H → Q: Reduced activity. Ref.8

Mutagenesis

308

R → G: Inactive and weakened DNA binding. Ref.8

Mutagenesis

343

Y → F or S: No strand cleavage or recombination. Ref.7

Sequence conflict

G → D AA sequence Ref.2

Sequence conflict

G → D AA sequence Ref.3

Secondary structure

423

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P03870 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: B9C3DE95AB253BC3
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FASTA

423

48,620

        10         20         30         40         50         60 
MPQFGILCKT PPKVLVRQFV ERFERPSGEK IALCAAELTY LCWMITHNGT AIKRATFMSY 

        70         80         90        100        110        120 
NTIISNSLSF DIVNKSLQFK YKTQKATILE ASLKKLIPAW EFTIIPYYGQ KHQSDITDIV 

       130        140        150        160        170        180 
SSLQLQFESS EEADKGNSHS KKMLKALLSE GESIWEITEK ILNSFEYTSR FTKTKTLYQF 

       190        200        210        220        230        240 
LFLATFINCG RFSDIKNVDP KSFKLVQNKY LGVIIQCLVT ETKTSVSRHI YFFSARGRID 

       250        260        270        280        290        300 
PLVYLDEFLR NSEPVLKRVN RTGNSSSNKQ EYQLLKDNLV RSYNKALKKN APYSIFAIKN 

       310        320        330        340        350        360 
GPKSHIGRHL MTSFLSMKGL TELTNVVGNW SDKRASAVAR TTYTHQITAI PDHYFALVSR 

       370        380        390        400        410        420 
YYAYDPISKE MIALKDETNP IEEWQHIEQL KGSAEGSIRY PAWNGIISQE VLDYLSSYIN 


RRI

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References

[1]	"Nucleotide sequence of the yeast plasmid." Hartley J.L., Donelson J.E. Nature 286:860-864(1980) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: A364A D5.
[2]	"The FLP protein of the 2-micron plasmid of yeast. Purification of the protein from Escherichia coli cells expressing the cloned FLP gene." Babineau D., Vetter D., Andrews B.J., Gronostajski R.M., Proteau G.A., Beatty L.G., Sadowski P.D. J. Biol. Chem. 260:12313-12319(1985) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-12.
[3]	"Identification of the DNA-binding domain of the FLP recombinase." Pan H., Clary D., Sadowski P.D. J. Biol. Chem. 266:11347-11354(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-7; 124-129 AND 148-153, FUNCTION.
[4]	"Sequence of 1019 nucleotides encompassing one of the inverted repeats from the yeast 2 micrometer plasmid." Hindley J., Phear G.A. Nucleic Acids Res. 7:361-375(1979) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 250-423.
[5]	"Antagonistic controls regulate copy number of the yeast 2 micron plasmid." Murray J.A.H., Scarpa M., Rossi N., Cesareni G. EMBO J. 6:4205-4212(1987) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[6]	"Roles of the 2 microns gene products in stable maintenance of the 2 microns plasmid of Saccharomyces cerevisiae." Reynolds A.E., Murray A.W.H., Szostak J.W. Mol. Cell. Biol. 7:3566-3573(1987) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Mutations in the 2-microns circle site-specific recombinase that abolish recombination without affecting substrate recognition." Prasad P.V., Young L.J., Jayaram M. Proc. Natl. Acad. Sci. U.S.A. 84:2189-2193(1987) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF TYR-343.
[8]	"Step-arrest mutants of FLP recombinase: implications for the catalytic mechanism of DNA recombination." Parsons R.L., Prasad P.V., Harshey R.M., Jayaram M. Mol. Cell. Biol. 8:3303-3310(1988) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-305 AND ARG-308.
[9]	"FLP protein of 2 mu circle plasmid of yeast induces multiple bends in the FLP recognition target site." Schwartz C.J., Sadowski P.D. J. Mol. Biol. 216:289-298(1990) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Identification of the active site tyrosine of Flp recombinase. Possible relevance of its location to the mechanism of recombination." Evans B.R., Chen J.W., Parsons R.L., Bauer T.K., Teplow D.B., Jayaram M. J. Biol. Chem. 265:18504-18510(1990) [PubMed] [Europe PMC] [Abstract] Cited for: ACTIVE SITE.
[11]	"Crystal structure of a Flp recombinase-Holliday junction complex: assembly of an active oligomer by helix swapping." Chen Y., Narendra U., Iype L.E., Cox M.M., Rice P.A. Mol. Cell 6:885-897(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH DNA, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J01347 Genomic DNA. Translation: AAB59340.1.

PIR

PDBYA. A04502.

RefSeq

NP_040488.1. NC_001398.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FLO	X-ray	2.65	A/B/C/D	2-423	[»]
1M6X	X-ray	2.80	A/B/C/D	3-423	[»]
1P4E	X-ray	2.70	A/B	3-423	[»]
			C/D	3-422	[»]

ProteinModelPortal

P03870.

SMR

P03870. Positions 2-422.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Organism-specific databases

CYGD

R0010w.

SGD

S000029654. FLP1.

Phylogenomic databases

eggNOG

NOG255844.

Gene expression databases

Genevestigator

P03870.

Family and domain databases

Gene3D

1.10.443.10. 1 hit.

InterPro

IPR011010. DNA_brk_join_enz.
IPR013762. Integrase-like_cat-core.
IPR010998. Integrase_Lambda-type_N.
IPR005626. Recombinase_Flp.
IPR022647. Recombinase_Flp_N.
[Graphical view]

Pfam

PF05202. Flp_C. 1 hit.
PF03930. Flp_N. 1 hit.
[Graphical view]

SUPFAM

SSF56349. DNA_brk_join_enz. 1 hit.
SSF47823. L_intgrse_like_N. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P03870.

Entry information

Entry name

FLP_YEAST

Accession

Primary (citable) accession number: P03870

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents