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Database: UniProt
Entry: A0A2D0KTU0_9GAMM
LinkDB: A0A2D0KTU0_9GAMM
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ID   A0A2D0KTU0_9GAMM        Unreviewed;       304 AA.
AC   A0A2D0KTU0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Tyrosine recombinase XerC {ECO:0000256|ARBA:ARBA00015804, ECO:0000256|HAMAP-Rule:MF_01808};
GN   Name=xerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN   ORFNames=Xsto_00805 {ECO:0000313|EMBL:PHM66788.1};
OS   Xenorhabdus stockiae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351614 {ECO:0000313|EMBL:PHM66788.1, ECO:0000313|Proteomes:UP000222366};
RN   [1] {ECO:0000313|EMBL:PHM66788.1, ECO:0000313|Proteomes:UP000222366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17904 {ECO:0000313|EMBL:PHM66788.1,
RC   ECO:0000313|Proteomes:UP000222366};
RX   PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA   Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA   Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA   Ebersberger I., Bode H.B.;
RT   "Natural product diversity associated with the nematode symbionts
RT   Photorhabdus and Xenorhabdus.";
RL   Nat. Microbiol. 2:1676-1685(2017).
CC   -!- FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing
CC       the cutting and rejoining of the recombining DNA molecules. Binds
CC       cooperatively to specific DNA consensus sequences that are separated
CC       from XerD binding sites by a short central region, forming the
CC       heterotetrameric XerC-XerD complex that recombines DNA substrates. The
CC       complex is essential to convert dimers of the bacterial chromosome into
CC       monomers to permit their segregation at cell division. It also
CC       contributes to the segregational stability of plasmids. In the complex
CC       XerC specifically exchanges the top DNA strands. {ECO:0000256|HAMAP-
CC       Rule:MF_01808}.
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|ARBA:ARBA00037721}.
CC   -!- ACTIVITY REGULATION: FtsK may regulate the catalytic switch between
CC       XerC and XerD in the heterotetrameric complex during the two steps of
CC       the recombination process. {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, in which XerC interacts
CC       with XerD via its C-terminal region, XerD interacts with XerC via its
CC       C-terminal region and so on. {ECO:0000256|ARBA:ARBA00011483,
CC       ECO:0000256|HAMAP-Rule:MF_01808}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01808}.
CC   -!- SIMILARITY: Belongs to the 'phage' integrase family. XerC subfamily.
CC       {ECO:0000256|ARBA:ARBA00006657, ECO:0000256|HAMAP-Rule:MF_01808}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PHM66788.1}.
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DR   EMBL; NJAJ01000006; PHM66788.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D0KTU0; -.
DR   Proteomes; UP000222366; Unassembled WGS sequence.
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; IPR004107; Integrase_SAM-like_N.
DR   InterPro; IPR011931; Recomb_XerC.
DR   InterPro; IPR023009; Tyrosine_recombinase_XerC/XerD.
DR   NCBIfam; TIGR02224; recomb_XerC; 1.
DR   PANTHER; PTHR30629; PROPHAGE INTEGRASE; 1.
DR   PANTHER; PTHR30629:SF2; PROPHAGE INTEGRASE INTS-RELATED; 1.
DR   Pfam; PF02899; Phage_int_SAM_1; 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|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_01808};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_01808};
KW   Chromosome partition {ECO:0000256|ARBA:ARBA00022829, ECO:0000256|HAMAP-
KW   Rule:MF_01808};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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}.
FT   DOMAIN          6..92
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000259|PROSITE:PS51900"
FT   DOMAIN          113..293
FT                   /note="Tyr recombinase"
FT                   /evidence="ECO:0000259|PROSITE:PS51898"
FT   ACT_SITE        152
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        248
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        271
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        280
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
SQ   SEQUENCE   304 AA;  35004 MW;  85B0F658F6F02DD5 CRC64;
     MSQPIDSLLE PVEAFLHYLR VERRLSPITI INYRRHLAVL VEMSLEMGIT EWQALDVTKV
     RMFATRSRRA GLQSASLALR LSSLRSFLDW MVTQGKMEAN PAKVVSTPRK KQHLPKNMDV
     DEVNQLLNID LNDPLSVRDR TMMEVMYGAG LRLSELVGLD CRHLDLENGE VWVYGKGSKE
     RKVPVGRIAL EWLQRWLVMR ELFEPEDNAV FISTQSGKRM STRNVQKRFE QWGIRQGVNS
     HIHPHKLRHS FATHILESSG DLRAVQELLG HANLSTTQIY THLDFQHLAK VYDVAHPRAK
     RGKS
//
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