ID A0A1W6P0H6_9RHOB Unreviewed; 307 AA.
AC A0A1W6P0H6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000256|HAMAP-Rule:MF_01808,
GN ECO:0000313|EMBL:ARO14830.1};
GN ORFNames=BVG79_01484 {ECO:0000313|EMBL:ARO14830.1};
OS Ketogulonicigenium robustum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ketogulonicigenium.
OX NCBI_TaxID=92947 {ECO:0000313|EMBL:ARO14830.1, ECO:0000313|Proteomes:UP000242447};
RN [1] {ECO:0000313|EMBL:ARO14830.1, ECO:0000313|Proteomes:UP000242447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPU_B003 {ECO:0000313|EMBL:ARO14830.1,
RC ECO:0000313|Proteomes:UP000242447};
RA Li Y., Liu L., Wang C., Zhang M., Zhang T., Zhang Y.;
RT "Ketogulonicigenium robustum SPU B003 Genome sequencing and assembly.";
RL Submitted (FEB-2017) 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|ARBA:ARBA00004496,
CC 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; CP019937; ARO14830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6P0H6; -.
DR STRING; 92947.BVG79_01484; -.
DR KEGG; kro:BVG79_01484; -.
DR Proteomes; UP000242447; Chromosome.
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 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; IPR023009; Tyrosine_recombinase_XerC/XerD.
DR PANTHER; PTHR30349; PHAGE INTEGRASE-RELATED; 1.
DR PANTHER; PTHR30349:SF85; TYROSINE RECOMBINASE XERC; 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}; Reference proteome {ECO:0000313|Proteomes:UP000242447}.
FT DOMAIN 5..96
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000259|PROSITE:PS51900"
FT DOMAIN 117..299
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 183
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 251
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 254
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 277
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 286
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
SQ SEQUENCE 307 AA; 33022 MW; 8F059672FC4BA0F9 CRC64;
MILSPALEDA LARWLIYRSA IGGAADATVT AYRHDVAAFL AFMTQHNGAP QGLAAISRIT
VSDMRAWMAH ARADGLSSRS LARALSAVKS FYGWLAQREG FEATAVLAAR APRFQRNLPR
PLEPDDAKAL LSRVEVQAKE PWVAARDLAV VTLLYGCGLR ISEALSLQGA DHPLPDVLRI
TGKGGKQRVV PVLPAARKAV ADYVRLYPAD LPADGPLFRG VRGGALNPRL IQKTVEQVRM
QLGLPASATP HALRHSFATH LLAAGGDLRS IQELLGHASL STTQAYTAVD AAHLMDIYDR
AHPKARS
//
