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P03015 (GIN_BPMU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine recombinase gin

EC=3.1.22.-
EC=6.5.1.-
Alternative name(s):
G-segment invertase
Short name=Gin
Gene product 53
Short name=gp53
Gene names
Name:gin
Ordered Locus Names:Mup53
OrganismEnterobacteria phage Mu (Bacteriophage Mu) [Reference proteome]
Taxonomic identifier10677 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeMulikevirus
Virus hostEnterobacteriaceae [TaxID: 543]

Protein attributes

Sequence length193 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Performs inversion of a viral 3 kp segment (G-segment) that encodes two alternate pairs of tail fiber proteins thereby modifying the host specificity of the virus. Binds as a dimer to the viral gix sites which are 34-bp palindromic sequences that flank the invertible G-segment. Catalyzes site-specific recombination in the presence of the host factor Fis. Gin dimers bound to each of the gix sites and host factor Fis bound to the enhancer come together to form the synaptic complex. Each Gin monomer introduces a nick and becomes covalently attached to the 5'-phosphate of the DNA, resulting in double-stranded staggered breaks at both recombination sites. A 180 degrees rotation of one of the two Gin dimers followed by religation of the DNA leads to the inversion of the G-segment (G+ or G- orientation). Ref.5 Ref.6 Ref.7 Ref.11

Subunit structure

Homodimer. During inversion, two dimers associate to form a homotetramer. Ref.10 Ref.11

Subcellular location

Host cytoplasm Probable.

Induction

Expressed in the late phase of the viral replicative cycle. Expression of late genes is activated by the viral late transcription activator C. Ref.9

Domain

The dimerization region is in the N-terminus.

Miscellaneous

The orientation of the G segment is defined as G+ and G-. G+ orientation provides S-U fibers whereas G- provides S'-U' fibers. S-U and S'-U' dont have the same host range (e.g. respectively E.coli and C.freundii).

Sequence similarities

Belongs to the site-specific recombinase resolvase family.

Caution

Translation initiates from a non-canonical start codon (GUG).

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 193193Serine recombinase gin
PRO_0000196354

Regions

DNA binding138 – 18346H-T-H motif Ref.4 Ref.8 Ref.11

Sites

Active site91O-(5'-phospho-DNA)-serine intermediate Ref.4

Experimental info

Mutagenesis91S → A, L or T: Recombination deficient. Ref.4
Sequence conflict481A → D no nucleotide entry Ref.1

Sequences

Sequence LengthMass (Da)Tools
P03015 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 86ED5D1C6ADD17DB

FASTA19321,766
        10         20         30         40         50         60 
MLIGYVRVST NDQNTDLQRN ALVCAGCEQI FEDKLSGTRT DRPGLKRALK RLQKGDTLVV 

        70         80         90        100        110        120 
WKLDRLGRSM KHLISLVGEL RERGINFRSL TDSIDTSSPM GRFFFHVMGA LAEMERELII 

       130        140        150        160        170        180 
ERTMAGLAAA RNKGRIGGRP PKLTKAEWEQ AGRLLAQGIP RKQVALIYDV ALSTLYKKHP 

       190 
AKRAHIENDD RIN 

« Hide

References

« Hide 'large scale' references
[1]"DNA inversions in the chromosome of Escherichia coli and in bacteriophage Mu: relationship to other site-specific recombination systems."
Plasterk R.H.A., Brinkman A., van de Putte P.
Proc. Natl. Acad. Sci. U.S.A. 80:5355-5358(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Bacteriophage Mu genome sequence: analysis and comparison with Mu-like prophages in Haemophilus, Neisseria and Deinococcus."
Morgan G.J., Hatfull G.F., Casjens S., Hendrix R.W.
J. Mol. Biol. 317:337-359(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Methylation regulates the expression of a DNA-modification function encoded by bacteriophage Mu."
Kahmann R.
Cold Spring Harb. Symp. Quant. Biol. 47:639-646(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 173-193.
[4]"The DNA invertase Gin of phage Mu: formation of a covalent complex with DNA via a phosphoserine at amino acid position 9."
Klippel A., Mertens G., Patschinsky T., Kahmann R.
EMBO J. 7:1229-1237(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16, COVALENT COMPLEX WITH DNA, DNA-BINDING, ACTIVE SITE, MUTAGENESIS OF SER-9.
[5]"A genetic switch in vitro: DNA inversion by Gin protein of phage Mu."
Plasterk R.H., Kanaar R., van de Putte P.
Proc. Natl. Acad. Sci. U.S.A. 81:2689-2692(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"G inversion in bacteriophage Mu DNA is stimulated by a site within the invertase gene and a host factor."
Kahmann R., Rudt F., Koch C., Mertens G.
Cell 41:771-780(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Isolation and characterization of unusual gin mutants."
Klippel A., Cloppenborg K., Kahmann R.
EMBO J. 7:3983-3989(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF MUTANTS.
[8]"Site-specific recombination in bacteriophage Mu: characterization of binding sites for the DNA invertase Gin."
Mertens G., Klippel A., Fuss H., Blocker H., Frank R., Kahmann R.
EMBO J. 7:1219-1227(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING.
[9]"Mutational analysis of a C-dependent late promoter of bacteriophage Mu."
Chiang L.W., Howe M.M.
Genetics 135:619-629(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[10]"Gin invertase of bacteriophage Mu is a dimer in solution, with the domain for dimerization in the N-terminal part of the protein."
Spaeny-Dekking L., van Hemert M., van de Putte P., Goosen N.
Biochemistry 34:1779-1786(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, REGION OF DIMERIZATION.
[11]"Crystal structure of an intermediate of rotating dimers within the synaptic tetramer of the G-segment invertase."
Ritacco C.J., Kamtekar S., Wang J., Steitz T.A.
Nucleic Acids Res. 41:2673-2682(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF VAL-114 MUTANT, DNA-BINDING, SUBUNIT, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF083977 Genomic DNA. Translation: AAF01129.1.
V01463 Genomic DNA. Translation: CAA24708.1.
PIRJWBPU. S02705.
RefSeqNP_050655.1. NC_000929.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UJ3X-ray3.80X1-193[»]
4M6FX-ray4.99A1-193[»]
ProteinModelPortalP03015.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2636258.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
3.40.50.1390. 1 hit.
InterProIPR009057. Homeodomain-like.
IPR006118. Recombinase_CS.
IPR006119. Resolv_N.
IPR006120. Resolvase_HTH_dom.
[Graphical view]
PfamPF02796. HTH_7. 1 hit.
PF00239. Resolvase. 1 hit.
[Graphical view]
SMARTSM00857. Resolvase. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
SSF53041. SSF53041. 1 hit.
PROSITEPS00397. RECOMBINASES_1. 1 hit.
PS00398. RECOMBINASES_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGIN_BPMU
AccessionPrimary (citable) accession number: P03015
Secondary accession number(s): Q9T1U8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references