XER_CLOAB
ID XER_CLOAB Reviewed; 292 AA.
AC Q97HE5;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Putative tyrosine recombinase CA_C2066 {ECO:0000305};
GN OrderedLocusNames=CA_C2066;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
CC -!- FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing
CC the cutting and rejoining of the recombining DNA molecules.
CC {ECO:0000250|UniProtKB:P0A8P8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Although strongly related to XerD, it lacks the Arg-His
CC residues of the Arg-His-Arg-His (R-H-R-H) sandwich residues that are
CC clustered with it. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. {ECO:0000305}.
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DR EMBL; AE001437; AAK80025.1; -; Genomic_DNA.
DR PIR; F97154; F97154.
DR RefSeq; NP_348685.1; NC_003030.1.
DR RefSeq; WP_010965366.1; NC_003030.1.
DR AlphaFoldDB; Q97HE5; -.
DR SMR; Q97HE5; -.
DR STRING; 272562.CA_C2066; -.
DR EnsemblBacteria; AAK80025; AAK80025; CA_C2066.
DR GeneID; 44998550; -.
DR KEGG; cac:CA_C2066; -.
DR PATRIC; fig|272562.8.peg.2272; -.
DR eggNOG; COG4974; Bacteria.
DR HOGENOM; CLU_027562_9_6_9; -.
DR OMA; HSFASHM; -.
DR OrthoDB; 745068at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009009; F:site-specific recombinase activity; IEA:InterPro.
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-KW.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.130; -; 1.
DR Gene3D; 1.10.443.10; -; 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; IPR011932; Recomb_XerD.
DR Pfam; PF02899; Phage_int_SAM_1; 1.
DR Pfam; PF00589; Phage_integrase; 1.
DR SUPFAM; SSF56349; SSF56349; 1.
DR TIGRFAMs; TIGR02225; recomb_XerD; 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..292
FT /note="Putative tyrosine recombinase CA_C2066"
FT /id="PRO_0000095383"
FT DOMAIN 1..83
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 104..286
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 263
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 272
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
SQ SEQUENCE 292 AA; 34248 MW; F6A88B2FFA9892C6 CRC64;
MDNLIEQYFA EIRKKNLSLN TIDAYRRDIK KFHEFLDEKG EKLREVDVIT IMSYVQYLQK
NGRANSSIVR NIVSIRNFFK YLEIKGIMDD NPVTQYEMPK IRRNFPDILT IEEVEKLLMG
PDGNTDKGIR DKAMLEIMYA TGMKVTELLN LTIYDINLKL SYIKCRGIKN KERIIPMGSY
AVKCLEIYLK VRTKLNVQNI DYLFFNLQGD KMTRQGFWKI IKQYAQESGI KKKINAYTLR
HSFAVHLLQN GADIKTIQEL LGHSDMATTQ IYSGMYRKTR IAEVYKKTHP RA