XERC_HAEIN
ID XERC_HAEIN Reviewed; 295 AA.
AC P44818;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Tyrosine recombinase XerC;
GN Name=xerC; OrderedLocusNames=HI_0676;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP CHARACTERIZATION, FUNCTION, AND MUTAGENESIS OF TYR-272.
RX PubMed=10048034; DOI=10.1046/j.1365-2958.1999.01231.x;
RA Neilson L., Blakely G., Sherratt D.J.;
RT "Site-specific recombination at dif by Haemophilus influenzae XerC.";
RL Mol. Microbiol. 31:915-926(1999).
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:0000269|PubMed:10048034}.
CC -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two
CC molecules of XerC and two molecules of XerD. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerC subfamily.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC22336.1; -; Genomic_DNA.
DR PIR; F64085; F64085.
DR RefSeq; NP_438836.1; NC_000907.1.
DR RefSeq; WP_005692390.1; NC_000907.1.
DR AlphaFoldDB; P44818; -.
DR SMR; P44818; -.
DR STRING; 71421.HI_0676; -.
DR EnsemblBacteria; AAC22336; AAC22336; HI_0676.
DR KEGG; hin:HI_0676; -.
DR PATRIC; fig|71421.8.peg.706; -.
DR eggNOG; COG4973; Bacteria.
DR HOGENOM; CLU_027562_9_0_6; -.
DR OMA; HSFASHM; -.
DR PhylomeDB; P44818; -.
DR BioCyc; HINF71421:G1GJ1-711-MON; -.
DR Proteomes; UP000000579; 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 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW DNA integration; DNA recombination; DNA-binding; Reference proteome.
FT CHAIN 1..295
FT /note="Tyrosine recombinase XerC"
FT /id="PRO_0000095298"
FT DOMAIN 1..85
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 106..285
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 237
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"
FT MUTAGEN 272
FT /note="Y->F: Abolishes DNA cleavage activity."
FT /evidence="ECO:0000269|PubMed:10048034"
SQ SEQUENCE 295 AA; 33935 MW; CF59B475F0DA25AE CRC64;
MLTALNRYWD YLRIERQMSP HTITNYQHQL DATIKILAQQ DIHSWTQVTP SVVRFILAES
KKQGLKEKSL ALRLSALRRF LSFLVQQGEL KVNPATGISA PKQGRHLPKN MDGEQVQQLL
ANDSKEPIDI RDRAILELMY SSGLRLSELQ GLDLNSINTR VREVRVIGKG NKERVVPFGR
YASHAIQEWL KVRALFNPKD EALFVSQLGN RISHRAIQKR LETWGIRQGL NSHLNPHKLR
HSFATHMLEA SSDLRAVQEL LGHSNLSTTQ IYTHLNFQHL AEVYDQAHPR AKRKK