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Entry: A0A1D8URN5_9PROT
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ID   A0A1D8URN5_9PROT        Unreviewed;       309 AA.
AC   A0A1D8URN5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Tyrosine recombinase XerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN   Name=xerD {ECO:0000313|EMBL:GEL63647.1};
GN   Synonyms=xerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN   ORFNames=A0U89_03235 {ECO:0000313|EMBL:AOX16298.1}, KBA01_09330
GN   {ECO:0000313|EMBL:GEL63647.1};
OS   Kozakia baliensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Kozakia.
OX   NCBI_TaxID=153496 {ECO:0000313|EMBL:AOX16298.1, ECO:0000313|Proteomes:UP000179145};
RN   [1] {ECO:0000313|EMBL:AOX16298.1, ECO:0000313|Proteomes:UP000179145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14400 {ECO:0000313|EMBL:AOX16298.1,
RC   ECO:0000313|Proteomes:UP000179145};
RX   PubMed=27716345;
RA   Brandt J.U., Jakob F., Behr J., Geissler A.J., Vogel R.F.;
RT   "Dissection of exopolysaccharide biosynthesis in Kozakia baliensis.";
RL   Microb. Cell Fact. 15:170-170(2016).
RN   [2] {ECO:0000313|EMBL:AOX16298.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 14400 {ECO:0000313|EMBL:AOX16298.1};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:GEL63647.1, ECO:0000313|Proteomes:UP000321177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 16664 {ECO:0000313|EMBL:GEL63647.1,
RC   ECO:0000313|Proteomes:UP000321177};
RA   Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT   "Whole genome shotgun sequence of Kozakia baliensis NBRC 16664.";
RL   Submitted (JUL-2019) 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; CP014674; AOX16298.1; -; Genomic_DNA.
DR   EMBL; BJVW01000002; GEL63647.1; -; Genomic_DNA.
DR   RefSeq; WP_070402087.1; NZ_CP014674.1.
DR   AlphaFoldDB; A0A1D8URN5; -.
DR   STRING; 153496.A0U89_03235; -.
DR   KEGG; kba:A0U89_03235; -.
DR   eggNOG; COG4974; Bacteria.
DR   OrthoDB; 9801717at2; -.
DR   Proteomes; UP000179145; Chromosome.
DR   Proteomes; UP000321177; 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   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   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:UP000179145}.
FT   DOMAIN          4..93
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000259|PROSITE:PS51900"
FT   DOMAIN          114..297
FT                   /note="Tyr recombinase"
FT                   /evidence="ECO:0000259|PROSITE:PS51898"
FT   ACT_SITE        157
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        181
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        249
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        252
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        275
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT   ACT_SITE        284
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
SQ   SEQUENCE   309 AA;  34338 MW;  C7DE0A311451C14A CRC64;
     MTRTTSSRYI ESFLEMLAAE RNAAARTRHA YFSDLADFES HCRQRGVAGP DVLINADAAC
     VQSYIAALSS SGMAARTSAR RLSCLRQFYR FLAREAIRPD DPTEREISPK LPASLPKLLS
     EQEVKRLLEE GVRGHADERR NYVAQAALEL LYTTGLRISE LLSLPSVLPL NNAPMVTVRG
     KGGRERLVPI SEKARQAALA LRHYDRDLDS PYLFPGRDPA KPLTRQGFDK ILHQAALNAG
     LDPERISPHV LRHSFASHLL AHGADLRALQ MLLGHADIAT TQIYTHVLSE RLRQLVQAHH
     PLASESADC
//
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