GIN_BPMU
ID GIN_BPMU Reviewed; 193 AA.
AC P03015; Q9T1U8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 23-FEB-2022, entry version 114.
DE RecName: Full=Serine recombinase gin;
DE EC=3.1.22.-;
DE EC=6.5.1.-;
DE AltName: Full=G-segment invertase;
DE Short=Gin;
DE AltName: Full=Gene product 53;
DE Short=gp53;
GN Name=gin; OrderedLocusNames=Mup53;
OS Escherichia phage Mu (Bacteriophage Mu).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Muvirus.
OX NCBI_TaxID=10677;
OH NCBI_TaxID=543; Enterobacteriaceae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6310572; DOI=10.1073/pnas.80.17.5355;
RA Plasterk R.H.A., Brinkman A., van de Putte P.;
RT "DNA inversions in the chromosome of Escherichia coli and in bacteriophage
RT Mu: relationship to other site-specific recombination systems.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:5355-5358(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11922669; DOI=10.1006/jmbi.2002.5437;
RA Morgan G.J., Hatfull G.F., Casjens S., Hendrix R.W.;
RT "Bacteriophage Mu genome sequence: analysis and comparison with Mu-like
RT prophages in Haemophilus, Neisseria and Deinococcus.";
RL J. Mol. Biol. 317:337-359(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 173-193.
RX PubMed=6345072; DOI=10.1101/sqb.1983.047.01.075;
RA Kahmann R.;
RT "Methylation regulates the expression of a DNA-modification function
RT encoded by bacteriophage Mu.";
RL Cold Spring Harb. Symp. Quant. Biol. 47:639-646(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16, COVALENT COMPLEX WITH DNA,
RP DNA-BINDING, ACTIVE SITE, AND MUTAGENESIS OF SER-9.
RX PubMed=3042382; DOI=10.1002/j.1460-2075.1988.tb02935.x;
RA Klippel A., Mertens G., Patschinsky T., Kahmann R.;
RT "The DNA invertase Gin of phage Mu: formation of a covalent complex with
RT DNA via a phosphoserine at amino acid position 9.";
RL EMBO J. 7:1229-1237(1988).
RN [5]
RP FUNCTION.
RX PubMed=6232613; DOI=10.1073/pnas.81.9.2689;
RA Plasterk R.H., Kanaar R., van de Putte P.;
RT "A genetic switch in vitro: DNA inversion by Gin protein of phage Mu.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:2689-2692(1984).
RN [6]
RP FUNCTION.
RX PubMed=3159478; DOI=10.1016/s0092-8674(85)80058-1;
RA Kahmann R., Rudt F., Koch C., Mertens G.;
RT "G inversion in bacteriophage Mu DNA is stimulated by a site within the
RT invertase gene and a host factor.";
RL Cell 41:771-780(1985).
RN [7]
RP FUNCTION OF MUTANTS.
RX PubMed=2974801; DOI=10.1002/j.1460-2075.1988.tb03286.x;
RA Klippel A., Cloppenborg K., Kahmann R.;
RT "Isolation and characterization of unusual gin mutants.";
RL EMBO J. 7:3983-3989(1988).
RN [8]
RP DNA-BINDING.
RX PubMed=3042381; DOI=10.1002/j.1460-2075.1988.tb02934.x;
RA Mertens G., Klippel A., Fuss H., Blocker H., Frank R., Kahmann R.;
RT "Site-specific recombination in bacteriophage Mu: characterization of
RT binding sites for the DNA invertase Gin.";
RL EMBO J. 7:1219-1227(1988).
RN [9]
RP INDUCTION.
RX PubMed=8293968; DOI=10.1093/genetics/135.3.619;
RA Chiang L.W., Howe M.M.;
RT "Mutational analysis of a C-dependent late promoter of bacteriophage Mu.";
RL Genetics 135:619-629(1993).
RN [10]
RP SUBUNIT, AND REGION OF DIMERIZATION.
RX PubMed=7849038; DOI=10.1021/bi00005a035;
RA Spaeny-Dekking L., van Hemert M., van de Putte P., Goosen N.;
RT "Gin invertase of bacteriophage Mu is a dimer in solution, with the domain
RT for dimerization in the N-terminal part of the protein.";
RL Biochemistry 34:1779-1786(1995).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF VAL-114 MUTANT, DNA-BINDING,
RP SUBUNIT, AND FUNCTION.
RX PubMed=23275567; DOI=10.1093/nar/gks1303;
RA Ritacco C.J., Kamtekar S., Wang J., Steitz T.A.;
RT "Crystal structure of an intermediate of rotating dimers within the
RT synaptic tetramer of the G-segment invertase.";
RL Nucleic Acids Res. 41:2673-2682(2013).
CC -!- FUNCTION: Performs inversion of a viral 3 kp segment (G-segment) that
CC encodes two alternate pairs of tail fiber proteins thereby modifying
CC the host specificity of the virus. Binds as a dimer to the viral gix
CC sites which are 34-bp palindromic sequences that flank the invertible
CC G-segment. Catalyzes site-specific recombination in the presence of the
CC host factor Fis. Gin dimers bound to each of the gix sites and host
CC factor Fis bound to the enhancer come together to form the synaptic
CC complex. Each Gin monomer introduces a nick and becomes covalently
CC attached to the 5'-phosphate of the DNA, resulting in double-stranded
CC staggered breaks at both recombination sites. A 180 degrees rotation of
CC one of the two Gin dimers followed by religation of the DNA leads to
CC the inversion of the G-segment (G+ or G- orientation).
CC {ECO:0000269|PubMed:23275567, ECO:0000269|PubMed:2974801,
CC ECO:0000269|PubMed:3159478, ECO:0000269|PubMed:6232613}.
CC -!- SUBUNIT: Homodimer. During inversion, two dimers associate to form a
CC homotetramer. {ECO:0000269|PubMed:23275567,
CC ECO:0000269|PubMed:7849038}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC Expression of late genes is activated by the viral late transcription
CC activator C. {ECO:0000269|PubMed:8293968}.
CC -!- DOMAIN: The dimerization region is in the N-terminus.
CC -!- MISCELLANEOUS: The orientation of the G segment is defined as G+ and
CC G-. G+ orientation provides S-U fibers whereas G- provides S'-U'
CC fibers. S-U and S'-U' dont have the same host range (e.g. respectively
CC E.coli and C.freundii).
CC -!- SIMILARITY: Belongs to the site-specific recombinase resolvase family.
CC {ECO:0000305}.
CC -!- CAUTION: Translation initiates from a non-canonical start codon (GUG).
CC {ECO:0000305}.
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DR EMBL; AF083977; AAF01129.1; -; Genomic_DNA.
DR EMBL; V01463; CAA24708.1; -; Genomic_DNA.
DR PIR; S02705; JWBPU.
DR RefSeq; NP_050655.1; NC_000929.1.
DR PDB; 3UJ3; X-ray; 3.80 A; X=1-193.
DR PDB; 4M6F; X-ray; 4.99 A; A=1-193.
DR PDBsum; 3UJ3; -.
DR PDBsum; 4M6F; -.
DR SMR; P03015; -.
DR GeneID; 2636258; -.
DR KEGG; vg:2636258; -.
DR Proteomes; UP000002611; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000150; F:DNA strand exchange activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0098678; P:viral tropism switching; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1390; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR006118; Recombinase_CS.
DR InterPro; IPR006119; Resolv_N.
DR InterPro; IPR036162; Resolvase-like_N_sf.
DR InterPro; IPR006120; Resolvase_HTH_dom.
DR Pfam; PF02796; HTH_7; 1.
DR Pfam; PF00239; Resolvase; 1.
DR SMART; SM00857; Resolvase; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF53041; SSF53041; 1.
DR PROSITE; PS00397; RECOMBINASES_1; 1.
DR PROSITE; PS00398; RECOMBINASES_2; 1.
DR PROSITE; PS51736; RECOMBINASES_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA integration; DNA invertase; DNA recombination;
KW DNA-binding; Host cytoplasm; Hydrolase; Late protein; Ligase;
KW Reference proteome; Viral receptor tropism switching;
KW Virus entry into host cell.
FT CHAIN 1..193
FT /note="Serine recombinase gin"
FT /id="PRO_0000196354"
FT DOMAIN 1..134
FT /note="Resolvase/invertase-type recombinase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01072"
FT DNA_BIND 138..183
FT /note="H-T-H motif"
FT ACT_SITE 9
FT /note="O-(5'-phospho-DNA)-serine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01072,
FT ECO:0000269|PubMed:3042382"
FT MUTAGEN 9
FT /note="S->A,L,T: Recombination deficient."
FT /evidence="ECO:0000269|PubMed:3042382"
FT CONFLICT 48
FT /note="A -> D (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 193 AA; 21766 MW; 86ED5D1C6ADD17DB CRC64;
MLIGYVRVST NDQNTDLQRN ALVCAGCEQI FEDKLSGTRT DRPGLKRALK RLQKGDTLVV
WKLDRLGRSM KHLISLVGEL RERGINFRSL TDSIDTSSPM GRFFFHVMGA LAEMERELII
ERTMAGLAAA RNKGRIGGRP PKLTKAEWEQ AGRLLAQGIP RKQVALIYDV ALSTLYKKHP
AKRAHIENDD RIN
