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Database: UniProt
Entry: Q1IMN9_KORVE
LinkDB: Q1IMN9_KORVE
Original site: Q1IMN9_KORVE 
ID   Q1IMN9_KORVE            Unreviewed;       300 AA.
AC   Q1IMN9;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Tyrosine recombinase XerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN   Name=xerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN   OrderedLocusNames=Acid345_2860 {ECO:0000313|EMBL:ABF41861.1};
OS   Koribacter versatilis (strain Ellin345).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Koribacter.
OX   NCBI_TaxID=204669 {ECO:0000313|EMBL:ABF41861.1, ECO:0000313|Proteomes:UP000002432};
RN   [1] {ECO:0000313|EMBL:ABF41861.1, ECO:0000313|Proteomes:UP000002432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin345 {ECO:0000313|EMBL:ABF41861.1,
RC   ECO:0000313|Proteomes:UP000002432};
RX   PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
CC   -!- FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing
CC       the cutting and rejoining of the recombining DNA molecules. The XerC-
CC       XerD complex is essential to convert dimers of the bacterial chromosome
CC       into monomers to permit their segregation at cell division. It also
CC       contributes to the segregational stability of plasmids.
CC       {ECO:0000256|HAMAP-Rule:MF_01808}.
CC   -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two
CC       molecules of XerC and two molecules of XerD. {ECO:0000256|HAMAP-
CC       Rule:MF_01808}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01808}.
CC   -!- SIMILARITY: Belongs to the 'phage' integrase family. XerC subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01808}.
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DR   EMBL; CP000360; ABF41861.1; -; Genomic_DNA.
DR   RefSeq; WP_011523662.1; NC_008009.1.
DR   AlphaFoldDB; Q1IMN9; -.
DR   STRING; 204669.Acid345_2860; -.
DR   EnsemblBacteria; ABF41861; ABF41861; Acid345_2860.
DR   KEGG; aba:Acid345_2860; -.
DR   eggNOG; COG4974; Bacteria.
DR   HOGENOM; CLU_027562_9_0_0; -.
DR   OrthoDB; 9801717at2; -.
DR   Proteomes; UP000002432; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009037; F:tyrosine-based site-specific recombinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006313; P:DNA transposition; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.150.130; -; 1.
DR   Gene3D; 1.10.443.10; Intergrase catalytic core; 1.
DR   HAMAP; MF_01808; Recomb_XerC_XerD; 1.
DR   InterPro; IPR044068; CB.
DR   InterPro; IPR011010; DNA_brk_join_enz.
DR   InterPro; IPR013762; Integrase-like_cat_sf.
DR   InterPro; IPR002104; Integrase_catalytic.
DR   InterPro; IPR010998; Integrase_recombinase_N.
DR   InterPro; IPR004107; Integrase_SAM-like_N.
DR   InterPro; IPR023009; Tyrosine_recombinase_XerC/XerD.
DR   PANTHER; PTHR30349:SF41; INTEGRASE_RECOMBINASE HI_1414-RELATED; 1.
DR   PANTHER; PTHR30349; PHAGE INTEGRASE-RELATED; 1.
DR   Pfam; PF02899; Phage_int_SAM_1; 1.
DR   Pfam; PF00589; Phage_integrase; 1.
DR   SUPFAM; SSF56349; DNA breaking-rejoining enzymes; 1.
DR   PROSITE; PS51900; CB; 1.
DR   PROSITE; PS51898; TYR_RECOMBINASE; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_01808};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_01808};
KW   Chromosome partition {ECO:0000256|ARBA:ARBA00022829, ECO:0000256|HAMAP-
KW   Rule:MF_01808};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01808};
KW   DNA integration {ECO:0000256|ARBA:ARBA00022908, ECO:0000256|HAMAP-
KW   Rule:MF_01808};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW   Rule:MF_01808};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01808}; Reference proteome {ECO:0000313|Proteomes:UP000002432}.
FT   DOMAIN          4..86
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000259|PROSITE:PS51900"
FT   DOMAIN          107..293
FT                   /note="Tyr recombinase"
FT                   /evidence="ECO:0000259|PROSITE:PS51898"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        248
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        271
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        280
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
SQ   SEQUENCE   300 AA;  33729 MW;  440D5853CC38B560 CRC64;
     MSVSQVEKGV AQFLRSLKEK NSSVHTIKAY TTDLEEFSAF LGPAKWDDID HVRIRGFLSH
     LYDKGLSKPS VARALAALRS LYKWLAREGF VEQNPAALVA TPKLPKKLPR VPTMEELNTV
     MDAEMPEAAS FPERDALIFE LLYGCGIRNS ELTGINLDDI RWSNEAILIR GKGKKERFVP
     FGDAAAVAAK VYLKKRQDIL AERHKSTNAL LINLRDVQRL TSRSVGRIVK KIAVARGLPA
     DVHPHTLRHA FGTHLLEEGA DLRAIQELLG HERLATTQRY TQLSTRHVLE VYDKTHPRAK
//
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