GIN_BPD10
ID GIN_BPD10 Reviewed; 197 AA.
AC Q38199; C9DGR2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 2.
DT 29-SEP-2021, entry version 76.
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;
GN Name=gin;
OS Escherichia phage D108 (Bacteriophage D108).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Muvirus; unclassified Muvirus.
OX NCBI_TaxID=665033;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kropinski A.M., Villegas A., Lingohr E.J.;
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 175-197.
RX PubMed=2957646; DOI=10.1093/nar/15.16.6691;
RA Szatmari G.B., Lapointe M., Dubow M.S.;
RT "The right end of transposable bacteriophage D108 contains a 520 base pair
RT protein-encoding sequence not present in bacteriophage Mu.";
RL Nucleic Acids Res. 15:6691-6704(1987).
CC -!- FUNCTION: Performs inversion of a viral 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. During inversion, two dimers associate to form a
CC homotetramer (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
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.
CC -!- DOMAIN: The dimerization region is in the N-terminus. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the site-specific recombinase resolvase family.
CC {ECO:0000305}.
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DR EMBL; X05926; CAA29365.1; -; Genomic_DNA.
DR EMBL; GQ357916; ACV50313.1; -; Genomic_DNA.
DR PIR; S07394; S07394.
DR RefSeq; YP_003335802.1; NC_013594.1.
DR SMR; Q38199; -.
DR GeneID; 8658865; -.
DR KEGG; vg:8658865; -.
DR Proteomes; UP000000320; 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 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 2: Evidence at transcript level;
KW DNA integration; DNA invertase; DNA recombination; DNA-binding;
KW Host cytoplasm; Hydrolase; Late protein; Ligase; Reference proteome.
FT CHAIN 1..197
FT /note="Serine recombinase gin"
FT /id="PRO_0000196355"
FT DOMAIN 1..134
FT /note="Resolvase/invertase-type recombinase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01072"
FT DNA_BIND 138..181
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"
SQ SEQUENCE 197 AA; 22309 MW; 204F4FF666FD5C1C CRC64;
MLIGYVRVST NDQNTDLQRN ALVCAGCEQI FEDKLSGTRT DRPGLKRALK RLQKGDTLVV
WKLDRLGRSM KHLISLVGEL RERGINFRSL TDSIDTSSPM GRFFFHVMGA LAEMERELII
ERTMAGLAAA RNKGRIGGRP PKLTKAEWEQ AGRLLAQGIP RKQVALIYDV ALSTLYKKHP
AKRTHIENDD RINQIDR