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
//