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Database: UniProt
Entry: A0A1H2DSJ5_9BACT
LinkDB: A0A1H2DSJ5_9BACT
Original site: A0A1H2DSJ5_9BACT 
ID   A0A1H2DSJ5_9BACT        Unreviewed;       323 AA.
AC   A0A1H2DSJ5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Tyrosine recombinase XerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN   Name=xerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN   ORFNames=SAMN05444156_0063 {ECO:0000313|EMBL:SDT85860.1};
OS   Verrucomicrobium sp. GAS474.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC   Verrucomicrobiaceae; Verrucomicrobium.
OX   NCBI_TaxID=1882831 {ECO:0000313|EMBL:SDT85860.1, ECO:0000313|Proteomes:UP000198591};
RN   [1] {ECO:0000313|EMBL:SDT85860.1, ECO:0000313|Proteomes:UP000198591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAS474 {ECO:0000313|EMBL:SDT85860.1,
RC   ECO:0000313|Proteomes:UP000198591};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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:0000256|HAMAP-Rule:MF_01808}.
CC   -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two
CC       molecules of XerC and two molecules of XerD. {ECO:0000256|HAMAP-
CC       Rule:MF_01808}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01808}.
CC   -!- SIMILARITY: Belongs to the 'phage' integrase family. XerC subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01808}.
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DR   EMBL; LT629781; SDT85860.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2DSJ5; -.
DR   STRING; 1882831.SAMN05444156_0063; -.
DR   OrthoDB; 9801717at2; -.
DR   Proteomes; UP000198591; Chromosome i.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009037; F:tyrosine-based site-specific recombinase activity; IEA:UniProtKB-UniRule.
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:DNA transposition; IEA:UniProtKB-UniRule.
DR   CDD; cd00798; INT_XerDC_C; 1.
DR   Gene3D; 1.10.150.130; -; 1.
DR   Gene3D; 1.10.443.10; Intergrase catalytic core; 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; IPR023009; Tyrosine_recombinase_XerC/XerD.
DR   PANTHER; PTHR30349:SF41; INTEGRASE_RECOMBINASE HI_1414-RELATED; 1.
DR   PANTHER; PTHR30349; PHAGE INTEGRASE-RELATED; 1.
DR   Pfam; PF00589; Phage_integrase; 1.
DR   SUPFAM; SSF56349; DNA breaking-rejoining enzymes; 1.
DR   SUPFAM; SSF47823; lambda integrase-like, N-terminal domain; 1.
DR   PROSITE; PS51900; CB; 1.
DR   PROSITE; PS51898; TYR_RECOMBINASE; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_01808};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_01808};
KW   Chromosome partition {ECO:0000256|HAMAP-Rule:MF_01808};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01808};
KW   DNA integration {ECO:0000256|ARBA:ARBA00022908, ECO:0000256|HAMAP-
KW   Rule:MF_01808};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW   Rule:MF_01808};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01808}; Reference proteome {ECO:0000313|Proteomes:UP000198591}.
FT   DOMAIN          11..99
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000259|PROSITE:PS51900"
FT   DOMAIN          120..312
FT                   /note="Tyr recombinase"
FT                   /evidence="ECO:0000259|PROSITE:PS51898"
FT   ACT_SITE        160
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        267
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        299
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
SQ   SEQUENCE   323 AA;  35675 MW;  C5A16857348EDAD4 CRC64;
     MGTPVAPALP PLWELEIEDC LAFLATERNH ATNSQLINHT ALLAFGAWMR RNLGEVGPEA
     VDVETVVRFL REERLARELS PASIKVHVVA LRHFFRRLHA SGRIPRDPTE TLDIPKIGRF
     LPECLSEDDV GKLLSVPFPE GHLGLRDRAI LEIFYGSGLR LAELTTLRIE SVIREPEDNG
     GGKGMALLRI IGKGNKERVV PLGSKALAAL DAYLDNARLY LATGKSGGEI FLGRNGTALT
     RARVWQIVKA CALRAGFAKN VFPHLLRHSF ATHLLENGAD LRVIQELLGH ASIATTQIYT
     HVDAARLRDV HRSHHPRSRL PSA
//
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