ID A0A290QBD0_9BACT Unreviewed; 329 AA.
AC A0A290QBD0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN ORFNames=CMV30_18360 {ECO:0000313|EMBL:ATC65753.1};
OS Nibricoccus aquaticus.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC Nibricoccus.
OX NCBI_TaxID=2576891 {ECO:0000313|EMBL:ATC65753.1, ECO:0000313|Proteomes:UP000217265};
RN [1] {ECO:0000313|EMBL:ATC65753.1, ECO:0000313|Proteomes:UP000217265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ-65 {ECO:0000313|EMBL:ATC65753.1,
RC ECO:0000313|Proteomes:UP000217265};
RA Choi A.;
RT "Complete genome sequence of Verrucomicrobial strain HZ-65, isolated from
RT freshwater.";
RL Submitted (SEP-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; CP023344; ATC65753.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A290QBD0; -.
DR KEGG; vbh:CMV30_18360; -.
DR OrthoDB; 9801717at2; -.
DR Proteomes; UP000217265; 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 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; IPR023009; Tyrosine_recombinase_XerC/XerD.
DR PANTHER; PTHR30349; PHAGE INTEGRASE-RELATED; 1.
DR PANTHER; PTHR30349:SF87; PROPHAGE INTEGRASE INTD-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}; Reference proteome {ECO:0000313|Proteomes:UP000217265}.
FT DOMAIN 30..116
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000259|PROSITE:PS51900"
FT DOMAIN 137..321
FT /note="Tyr recombinase"
FT /evidence="ECO:0000259|PROSITE:PS51898"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 177
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 273
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 276
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 299
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 308
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
SQ SEQUENCE 329 AA; 36152 MW; 3F113B4D7D7A6B7C CRC64;
MARSKQRKRQ EKVGRKSADT ITLQDSRAPG DFSGEIDDFI GYLKLERGLS IHTQSSYQSD
LDQCATFLSK RGVKNWSTVS ADEVTAWIHS LGSGDLSLAS LARKRTAVRM LARYLVSEEK
RPDDFTALLE GPKLARRIPG TLSVDDVAKL LAAPTGGDAI AIRDRAILEL FYSSGLRVSE
LSGVMIQQLD LENGFLRVFG KGSKERVVPV GGRALDAVQT YLTAARGHFV KPKKTGSALF
LSERGTAISR KMLWVLVKKY AARSGITKAV KPHLLRHSFA THLLGGGADL RAIQDMLGHA
NLATTQIYTA VDEKRLAGEH AKFHPRNRR
//
