ID A0A060VEM3_KLEPN Unreviewed; 298 AA. AC A0A060VEM3; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 01-APR-2015, entry version 8. DE SubName: Full=Site-specific tyrosine recombinase {ECO:0000313|EMBL:CED77671.1}; DE SubName: Full=Site-specific tyrosine recombinase XerD {ECO:0000313|EMBL:KII07241.1}; DE SubName: Full=XerD protein {ECO:0000313|EMBL:CDQ52864.1}; GN Name=xerD {ECO:0000256|HAMAP-Rule:MF_01807, GN ECO:0000313|EMBL:CDQ52864.1}; GN ORFNames=KPLM21_90091 {ECO:0000313|EMBL:CED77671.1}, KpST82_3931 GN {ECO:0000313|EMBL:CDQ52864.1}, LS45_08105 GN {ECO:0000313|EMBL:KII07241.1}, SE21_11025 GN {ECO:0000313|EMBL:KII58014.1}; OS Klebsiella pneumoniae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=573 {ECO:0000313|EMBL:CDQ52864.1}; RN [1] {ECO:0000313|EMBL:CDQ52864.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SB3193 {ECO:0000313|EMBL:CDQ52864.1}; RA Genoscope - CEA; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CED77671.1} RP NUCLEOTIDE SEQUENCE. RA Khater Fida, Forestier Christiane; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:KII07241.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UMNturkey9 {ECO:0000313|EMBL:KII07241.1}; RA Lang K., Dorn K., Danzeisen J., Johnson T.; RT "Plasmid movement, recombination, and chromosomal integration amongst RT multidrug resistant commensal Escherichia coli clones within a single RT commercial turkey flock."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:KII58014.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1kgm {ECO:0000313|EMBL:KII58014.1}; RA Goh S.Y., Chan K.G.; RT "Genome Sequencing of Klebsiella pneumoniae 1kgm."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Site-specific tyrosine recombinase, which acts by CC catalyzing the cutting and rejoining of the recombining DNA CC molecules. Binds cooperatively to specific DNA consensus sequences CC that are separated from XerC binding sites by a short central CC region, forming the heterotetrameric XerC-XerD complex that CC recombines DNA substrates. The complex is essential to convert CC dimers of the bacterial chromosome into monomers to permit their CC segregation at cell division. It also contributes to the CC segregational stability of plasmids. In the complex XerD CC specifically exchanges the bottom DNA strands. {ECO:0000256|HAMAP- CC Rule:MF_01807}. CC -!- ENZYME REGULATION: FtsK may regulate the catalytic switch between CC XerC and XerD in the heterotetrameric complex during the two steps CC of the recombination process. {ECO:0000256|HAMAP-Rule:MF_01807}. CC -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two CC molecules of XerC and two molecules of XerD, in which XerC CC interacts with XerD via its C-terminal region, XerD interacts with CC XerC via its C-terminal region and so on. {ECO:0000256|HAMAP- CC Rule:MF_01807}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01807, CC ECO:0000256|SAAS:SAAS00019473}. CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerD CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01807}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LK022715; CDQ52864.1; -; Genomic_DNA. DR EMBL; CCVM01000144; CED77671.1; -; Genomic_DNA. DR EMBL; JRRF01000004; KII07241.1; -; Genomic_DNA. DR EMBL; JXBI01000009; KII58014.1; -; Genomic_DNA. DR ProteinModelPortal; A0A060VEM3; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009037; F:tyrosine-based site-specific recombinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-HAMAP. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.150.130; -; 1. DR Gene3D; 1.10.443.10; -; 1. DR HAMAP; MF_01807; Recomb_XerD; 1. DR HAMAP; MF_01808; Recomb_XerC; 1. DR InterPro; IPR011010; DNA_brk_join_enz. DR InterPro; IPR013762; Integrase-like_cat-core. DR InterPro; IPR002104; Integrase_catalytic. DR InterPro; IPR023109; Integrase_recombinase_N. DR InterPro; IPR004107; Integrase_SAM-like_N. DR InterPro; IPR011932; Recomb_XerD. DR InterPro; IPR023009; Tyrosine_recombinase_XerC/XerD. DR Pfam; PF02899; Phage_int_SAM_1; 1. DR Pfam; PF00589; Phage_integrase; 1. DR SUPFAM; SSF56349; SSF56349; 1. DR TIGRFAMs; TIGR02225; recomb_XerD; 1. PE 3: Inferred from homology; KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_01807, KW ECO:0000256|SAAS:SAAS00055632}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_01807, KW ECO:0000256|SAAS:SAAS00055628}; KW Chromosome partition {ECO:0000256|HAMAP-Rule:MF_01807, KW ECO:0000256|SAAS:SAAS00055605}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01807, KW ECO:0000256|SAAS:SAAS00019482}; KW DNA integration {ECO:0000256|HAMAP-Rule:MF_01807, KW ECO:0000256|SAAS:SAAS00094378}; KW DNA recombination {ECO:0000256|HAMAP-Rule:MF_01807, KW ECO:0000256|SAAS:SAAS00059574}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01807, KW ECO:0000256|SAAS:SAAS00019121}. FT ACT_SITE 148 148 {ECO:0000256|HAMAP-Rule:MF_01807}. FT ACT_SITE 172 172 {ECO:0000256|HAMAP-Rule:MF_01807}. FT ACT_SITE 244 244 {ECO:0000256|HAMAP-Rule:MF_01807}. FT ACT_SITE 247 247 {ECO:0000256|HAMAP-Rule:MF_01807}. FT ACT_SITE 270 270 {ECO:0000256|HAMAP-Rule:MF_01807}. FT ACT_SITE 279 279 O-(3'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01807}. SQ SEQUENCE 298 AA; 33967 MW; DF893A2E8C2D2B88 CRC64; MKQDLALIEQ FLDALWLERN LAENTLSAYR RDLTMLVEWL HHRGLSLASV GSDDLQALLA ERQSGGYKAT STARLLSAVR RFFQHLYREK IRPDDPSALL ASPKLPQRLP KDLSEAQVER LLQAPLVEQP LELRDKAMLE VLYATGLRVS ELVGLTMSDI SLRQGVLRVV GKGNKERLVP LGEEAVLWVE NYLEYGRPWL LNGVASDVLF PSQRAQQMTR QTFWHRIKHY AVLAGIDSEK LSPHVLRHAF ATHLLNHGAD LRVVQMLLGH SDLSTTQIYT HVATERLRQL HQQHHPRA //