XERC_HERA2
ID XERC_HERA2 Reviewed; 306 AA.
AC A9B1E0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=Haur_4696;
OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC Herpetosiphon.
OX NCBI_TaxID=316274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23779 / DSM 785 / 114-95;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_01808}.
CC -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two
CC molecules of XerC and two molecules of XerD. {ECO:0000255|HAMAP-
CC Rule:MF_01808}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01808}.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01808}.
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DR EMBL; CP000875; ABX07327.1; -; Genomic_DNA.
DR AlphaFoldDB; A9B1E0; -.
DR SMR; A9B1E0; -.
DR STRING; 316274.Haur_4696; -.
DR EnsemblBacteria; ABX07327; ABX07327; Haur_4696.
DR KEGG; hau:Haur_4696; -.
DR eggNOG; COG4974; Bacteria.
DR HOGENOM; CLU_027562_9_6_0; -.
DR OMA; HSFASHM; -.
DR Proteomes; UP000000787; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009037; F:tyrosine-based site-specific recombinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
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:transposition, DNA-mediated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.150.130; -; 1.
DR Gene3D; 1.10.443.10; -; 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 Pfam; PF02899; Phage_int_SAM_1; 1.
DR Pfam; PF00589; Phage_integrase; 1.
DR SUPFAM; SSF56349; SSF56349; 1.
DR PROSITE; PS51900; CB; 1.
DR PROSITE; PS51898; TYR_RECOMBINASE; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW DNA integration; DNA recombination; DNA-binding; Reference proteome.
FT CHAIN 1..306
FT /note="Tyrosine recombinase XerC"
FT /id="PRO_1000187600"
FT DOMAIN 1..85
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 106..289
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 147
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 171
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 241
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 244
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 267
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 276
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ SEQUENCE 306 AA; 34204 MW; 9A5F3F1B0156A9F4 CRC64;
MQQQLEQFLA YLTVERGLTG NTIAAYRTDL DQFVNFIVER NTGSWSNVSR DDLLAFLLFL
KEKRYATSTI ARRTAAIKSF FEYLQGQHSI TTNPTENLDS PKVDRFLPKA ITVAQVDELL
ELPLTTSGPE GLRDKAMLEV LYATGMRVSE LVALDVGDVD LAIHQIRCLG KANKERNLPI
VGSASTALEE YLDIARGQIS RNGGDPALFL NHRGKRLTRQ GFWLILKGYA ERLGLSDLTP
HTLRHSFATH MLNRGKDLRE VQELLGHASI STTQIYTHVS NDRAVKYDQA AQRPTVANAA
EVEFSA