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XERC_RALPJ
ID   XERC_RALPJ              Reviewed;         328 AA.
AC   B2U7W2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN   Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=Rpic_3697;
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) 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; CP001068; ACD28815.1; -; Genomic_DNA.
DR   RefSeq; WP_004628279.1; NC_010682.1.
DR   AlphaFoldDB; B2U7W2; -.
DR   SMR; B2U7W2; -.
DR   STRING; 402626.Rpic_3697; -.
DR   EnsemblBacteria; ACD28815; ACD28815; Rpic_3697.
DR   KEGG; rpi:Rpic_3697; -.
DR   eggNOG; COG4973; Bacteria.
DR   HOGENOM; CLU_027562_9_0_4; -.
DR   OMA; HSFASHM; -.
DR   OrthoDB; 745068at2; -.
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..328
FT                   /note="Tyrosine recombinase XerC"
FT                   /id="PRO_1000187611"
FT   DOMAIN          13..100
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT   DOMAIN          122..319
FT                   /note="Tyr recombinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        197
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        271
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        274
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        297
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        306
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ   SEQUENCE   328 AA;  36119 MW;  329171134BE864F3 CRC64;
     MPQSASVDDH GAQAPHPQIA AYLDALKFER QLSPHTLQSY TRELAVLQRL GAQHAANIDL
     TQLQSHHIRR MMAQLHGDGL SGRSIARALS AWRGWFKWMA LRDAAVTANP VDGVRAPKSP
     KRLPKALSVE QAVALMEQLP GDDAETIRDR AVNELFYSCG LRLSELVSLD MRHVKAGAYE
     SASWLDLEAR EVQVLGKGSK RRTVPVGTKA TEALAAWLAV RAQLAKSDAA PEDAHALFLS
     PRGKRLAQRQ IQLRMKRNAI AAGVPADVHP HVLRHSFATH MLQSSGDLRA VQELLGHASI
     ASTQVYTSLD FQHLAKIYDQ AHPRAKKK
 
 
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