Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Transposon gamma-delta resolvase

Gene

tnpR

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

This protein catalyzes the site-specific recombination of the transposon and also regulates its frequency of transposition.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei10 – 101O-(5'-phospho-DNA)-serine intermediatePROSITE-ProRule annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi161 – 18020H-T-H motifSequence AnalysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA integration, DNA recombination

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Transposon gamma-delta resolvase
Alternative name(s):
Transposon Tn1000 resolvase
Gene namesi
Name:tnpR
Ordered Locus Names:ECOK12F009
Encoded oniPlasmid F1 Publication
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 183183Transposon gamma-delta resolvasePRO_0000196367Add
BLAST

Proteomic databases

PRIDEiP03012.

Expressioni

Gene expression databases

GenevestigatoriP03012.

Interactioni

Protein-protein interaction databases

DIPiDIP-61217N.

Structurei

Secondary structure

1
183
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Helixi13 – 2513Combined sources
Helixi30 – 323Combined sources
Beta strandi33 – 375Combined sources
Beta strandi41 – 433Combined sources
Helixi46 – 549Combined sources
Beta strandi60 – 656Combined sources
Helixi66 – 683Combined sources
Beta strandi69 – 724Combined sources
Helixi73 – 8513Combined sources
Beta strandi89 – 924Combined sources
Turni93 – 964Combined sources
Helixi102 – 12726Combined sources
Turni135 – 1373Combined sources
Beta strandi143 – 1453Combined sources
Helixi148 – 1569Combined sources
Helixi161 – 1688Combined sources
Helixi172 – 1809Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GDRX-ray3.50A1-140[»]
1GDTX-ray3.00A/B1-183[»]
1GHTNMR-A1-105[»]
1HX7NMR-A1-105[»]
1RESNMR-A141-183[»]
1RETNMR-A141-183[»]
1ZR2X-ray3.90A/B1-183[»]
1ZR4X-ray3.40A/B/D/E1-183[»]
2GM4X-ray3.50A/B1-183[»]
2GM5X-ray2.10A/B/C/D2-134[»]
2RSLX-ray2.30A/B/C1-140[»]
ProteinModelPortaliP03012.
SMRiP03012. Positions 1-183.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03012.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 137136Resolvase/invertase-type recombinase catalyticPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 resolvase/invertase-type recombinase catalytic domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000275578.
OMAiMGVAIRF.
PhylomeDBiP03012.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.40.50.1390. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR006118. Recombinase_CS.
IPR006119. Resolv_N.
IPR006120. Resolvase_HTH_dom.
[Graphical view]
PfamiPF02796. HTH_7. 1 hit.
PF00239. Resolvase. 1 hit.
[Graphical view]
SMARTiSM00857. Resolvase. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF53041. SSF53041. 1 hit.
PROSITEiPS00397. RECOMBINASES_1. 1 hit.
PS00398. RECOMBINASES_2. 1 hit.
PS51736. RECOMBINASES_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P03012-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLFGYARVS TSQQSLDIQV RALKDAGVKA NRIFTDKASG SSSDRKGLDL
60 70 80 90 100
LRMKVEEGDV ILVKKLDRLG RDTADMIQLI KEFDAQGVSI RFIDDGISTD
110 120 130 140 150
GEMGKMVVTI LSAVAQAERQ RILERTNEGR QEAMAKGVVF GRKRKIDRDA
160 170 180
VLNMWQQGLG ASHISKTMNI ARSTVYKVIN ESN
Length:183
Mass (Da):20,362
Last modified:July 21, 1986 - v1
Checksum:iB2EBA6037F926FAB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01844 Genomic DNA. No translation available.
X60200 Genomic DNA. Translation: CAA42759.1.
D16449 Genomic DNA. Translation: BAA03915.1.
AP001918 Genomic DNA. Translation: BAA97879.1.
PIRiA03542. RPECTG.
RefSeqiNP_061388.1. NC_002483.1.
WP_001235704.1. NC_002483.1.

Genome annotation databases

GeneIDi1263577.
KEGGipg:1263577.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01844 Genomic DNA. No translation available.
X60200 Genomic DNA. Translation: CAA42759.1.
D16449 Genomic DNA. Translation: BAA03915.1.
AP001918 Genomic DNA. Translation: BAA97879.1.
PIRiA03542. RPECTG.
RefSeqiNP_061388.1. NC_002483.1.
WP_001235704.1. NC_002483.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GDRX-ray3.50A1-140[»]
1GDTX-ray3.00A/B1-183[»]
1GHTNMR-A1-105[»]
1HX7NMR-A1-105[»]
1RESNMR-A141-183[»]
1RETNMR-A141-183[»]
1ZR2X-ray3.90A/B1-183[»]
1ZR4X-ray3.40A/B/D/E1-183[»]
2GM4X-ray3.50A/B1-183[»]
2GM5X-ray2.10A/B/C/D2-134[»]
2RSLX-ray2.30A/B/C1-140[»]
ProteinModelPortaliP03012.
SMRiP03012. Positions 1-183.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61217N.

Proteomic databases

PRIDEiP03012.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1263577.
KEGGipg:1263577.

Phylogenomic databases

HOGENOMiHOG000275578.
OMAiMGVAIRF.
PhylomeDBiP03012.

Miscellaneous databases

EvolutionaryTraceiP03012.
PROiP03012.

Gene expression databases

GenevestigatoriP03012.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.40.50.1390. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR006118. Recombinase_CS.
IPR006119. Resolv_N.
IPR006120. Resolvase_HTH_dom.
[Graphical view]
PfamiPF02796. HTH_7. 1 hit.
PF00239. Resolvase. 1 hit.
[Graphical view]
SMARTiSM00857. Resolvase. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF53041. SSF53041. 1 hit.
PROSITEiPS00397. RECOMBINASES_1. 1 hit.
PS00398. RECOMBINASES_2. 1 hit.
PS51736. RECOMBINASES_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of gamma delta resolvase gene and demonstration that its gene product acts as a repressor of transcription."
    Reed R.R., Shibuya G.I., Steitz J.A.
    Nature 300:381-383(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Identification of the region that determines the specificity of binding of the transposases encoded by Tn3 and gamma delta to the terminal inverted repeat sequences."
    Maekawa T., Ohtsubo E.
    Jpn. J. Genet. 69:269-285(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Sequence of a transposon identified as Tn1000 (gamma delta)."
    Broom J.E., Hill D.F., Hughes G., Jones W.A., McNaughton J.C., Stockwell P.A., Petersen G.B.
    DNA Seq. 5:185-189(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete nucleotide sequence of the F plasmid: its implications for organization and diversification of plasmid genomes."
    Shimizu H., Saitoh Y., Suda Y., Uehara K., Sampei G., Mizobuchi K.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / CR63.
    Plasmid: F
  5. "Resolvase-mediated recombination intermediates contain a serine residue covalently linked to DNA."
    Reed R.R., Moser C.D.
    Cold Spring Harb. Symp. Quant. Biol. 49:245-249(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE SER-10.
  6. "Mutants of the gamma delta resolvase: a genetic analysis of the recombination function."
    Newman B.J., Grindley N.D.F.
    Cell 38:463-469(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  7. "The crystal structure of the catalytic domain of the site-specific recombination enzyme gamma delta resolvase at 2.7-A resolution."
    Sanderson M.R., Freemont P.S., Rice P.A., Goldman A., Hatfull G.F., Grindley N.D.F., Steitz T.A.
    Cell 63:1323-1329(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-140.
  8. "Crystal structure of the site-specific recombinase gamma delta resolvase complexed with a 34 bp cleavage site."
    Yang W., Steitz T.A.
    Cell 82:193-207(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  9. "Determination of the structure of the DNA binding domain of gamma delta resolvase in solution."
    Liu T., Derose E.F., Mullen G.P.
    Protein Sci. 3:1286-1295(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 141-183.

Entry informationi

Entry nameiTNR1_ECOLI
AccessioniPrimary (citable) accession number: P03012
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 27, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Plasmid, Transposable element

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.