XERC_SHESW
ID XERC_SHESW Reviewed; 302 AA.
AC A1RPD0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN OrderedLocusNames=Sputw3181_3719;
OS Shewanella sp. (strain W3-18-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=351745;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W3-18-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella sp. W3-18-1.";
RL Submitted (DEC-2006) 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; CP000503; ABM26525.1; -; Genomic_DNA.
DR RefSeq; WP_011790956.1; NC_008750.1.
DR AlphaFoldDB; A1RPD0; -.
DR SMR; A1RPD0; -.
DR GeneID; 45044074; -.
DR KEGG; shw:Sputw3181_3719; -.
DR HOGENOM; CLU_027562_9_0_6; -.
DR OMA; HSFASHM; -.
DR Proteomes; UP000002597; 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; IPR011931; Recomb_XerC.
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 TIGRFAMs; TIGR02224; recomb_XerC; 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.
FT CHAIN 1..302
FT /note="Tyrosine recombinase XerC"
FT /id="PRO_1000070038"
FT DOMAIN 6..90
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 111..290
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 150
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 174
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 242
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 245
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 268
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 277
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ SEQUENCE 302 AA; 34208 MW; B637A9BD6BE017B9 CRC64;
MGDMSDLEVT CLQDYERYLH SERQLSAHTV HNYLYELNRV STLLPKDVTL LNVGREHWQQ
VLAKLHRKGL SPRSLSLCLS AIKQWGEFLL REGMIAVNPA KGLSAPKQAK PLPKNMDVDS
LTHLLEIEGT DPLTLRDKAM MELFYSSGLR LAELAALNLS SVQYDLREVR VLGKGNKERI
VPVGSYAIKA LEAWLVCRQQ IPCEDCALFV TGKGRRLSHR SIQSRMAKWG QEQALSVRVH
PHKLRHSFAT HMLESSADLR AVQELLGHAN LSTTQIYTSL DFQHLAKVYD SAHPRAKKQQ
DK