XERC_CHLTA
ID XERC_CHLTA Reviewed; 315 AA.
AC Q3KM11;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=CTA_0376;
OS Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=315277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT genitotropic strains.";
RL Infect. Immun. 73:6407-6418(2005).
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; CP000051; AAX50611.1; -; Genomic_DNA.
DR RefSeq; WP_009872581.1; NC_007429.1.
DR AlphaFoldDB; Q3KM11; -.
DR SMR; Q3KM11; -.
DR EnsemblBacteria; AAX50611; AAX50611; CTA_0376.
DR KEGG; cta:CTA_0376; -.
DR HOGENOM; CLU_027562_9_0_0; -.
DR OMA; QAFWYLI; -.
DR Proteomes; UP000002532; 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..315
FT /note="Tyrosine recombinase XerC"
FT /id="PRO_1000069996"
FT DOMAIN 1..103
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 124..306
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 164
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 188
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 258
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 261
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 284
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT ACT_SITE 293
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ SEQUENCE 315 AA; 36572 MW; 5416E390FE5C2CE1 CRC64;
MITSFYAFLD YLKNMKASSL HTLRNYCMDL SSLKCFLEKK SDLSPTPPLS LHDNTYDYPP
LSFSLFTKDN IRLYLLEQIQ THHSKRTVRR RLSAIKSFAR FCVKNQLIPE NPAEMIRGPR
LPQELPSPLT YEQVLALMAA PELDKVTGFR DRCLLELFYS SGLRISEITA LNRADIDFQS
HLLHIRGKGK KERIVPMTKV AVQWLQDYLN HPDRASVEQD HQACFLNRFG KRLSTRSIDR
KFQQYLLKTG LSGSITPHTI RHTIATHWLE RGMDLKTIQL LLGHTSLETT TIYTHVSMKL
KKQIHDETHP HNLEE