ID A0A060VEM3_KLEPN Unreviewed; 298 AA. AC A0A060VEM3; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 24-JUN-2015, entry version 11. DE RecName: Full=Tyrosine recombinase XerD {ECO:0000256|HAMAP-Rule:MF_01807}; GN Name=xerD {ECO:0000256|HAMAP-Rule:MF_01807, GN ECO:0000313|EMBL:CDQ52864.1}; GN Synonyms=xerD_1 {ECO:0000313|EMBL:AIT00307.1}; GN ORFNames=JT12_26865 {ECO:0000313|EMBL:KJL06999.1}, JT13_26485 GN {ECO:0000313|EMBL:KJL07526.1}, JT14_26570 GN {ECO:0000313|EMBL:KGJ38036.1}, JT15_26520 GN {ECO:0000313|EMBL:KGJ37646.1}, KPLM21_90091 GN {ECO:0000313|EMBL:CED77671.1}, KPOL2_01260 GN {ECO:0000313|EMBL:CEN65736.1}, KPST15NDM1_01461 GN {ECO:0000313|EMBL:CEO85281.1}, KpST82_3931 GN {ECO:0000313|EMBL:CDQ52864.1}, PMK1_00810 GN {ECO:0000313|EMBL:AIT00307.1}; 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:AIT00307.1, ECO:0000313|Proteomes:UP000029666} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PMK1 {ECO:0000313|EMBL:AIT00307.1}; RX PubMed=25267672; RA Stoesser N., Giess A., Batty E.M., Sheppard A.E., Walker A.S., RA Wilson D.J., Didelot X., Bashir A., Sebra R., Kasarskis A., RA Sthapit B., Shakya M., Kelly D., Pollard A.J., Peto T.E., Crook D.W., RA Donnelly P., Thorson S., Amatya P., Joshi S.; RT "Genome Sequencing of an Extended Series of NDM-Producing Klebsiella RT pneumoniae Isolates from Neonatal Infections in a Nepali Hospital RT Characterizes the Extent of Community- versus Hospital-Associated RT Transmission in an Endemic Setting."; RL Antimicrob. Agents Chemother. 58:7347-7357(2014). RN [2] {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 [3] {ECO:0000313|EMBL:AIT00307.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PMK1 {ECO:0000313|EMBL:AIT00307.1}; RA Giess A.P.; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:KGJ37646.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CDPH3020 {ECO:0000313|EMBL:KJL06999.1}, CDPH3707 RC {ECO:0000313|EMBL:KJL07526.1}, CDPH3823 {ECO:0000313|EMBL:KGJ38036.1}, RC and CDPH5262 {ECO:0000313|EMBL:KGJ37646.1}; RA Greninger A.L., Chorny I., Knowles S., Chaturverdi V.; RT "Draft Genome Sequences from Four Isolates of NDM-producing Klebsiella RT pneumoniae from Three Patients in Northern California (Strains RT CDPH3020, CDPH3707, CDPH3823, CDPH5262)."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:CED77671.1} RP NUCLEOTIDE SEQUENCE. RA Khater Fida, Forestier Christiane; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:CEN65736.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Novel ST outbreak lineage 2 {ECO:0000313|EMBL:CEN65736.1}, and RC ST15 NDM-1 {ECO:0000313|EMBL:CEO85281.1}; RA Aslett A.Martin., De Silva Nishadi; 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:SAAS00202384}. 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; CP008929; AIT00307.1; -; Genomic_DNA. DR EMBL; LK022715; CDQ52864.1; -; Genomic_DNA. DR EMBL; CCVM01000144; CED77671.1; -; Genomic_DNA. DR EMBL; CDPE01000025; CEN65736.1; -; Genomic_DNA. DR EMBL; CDQG01000036; CEO85281.1; -; Genomic_DNA. DR EMBL; JQDY01000038; KGJ37646.1; -; Genomic_DNA. DR EMBL; JQDX01000035; KGJ38036.1; -; Genomic_DNA. DR EMBL; JQCW01000037; KJL06999.1; -; Genomic_DNA. DR EMBL; JQCX01000036; KJL07526.1; -; Genomic_DNA. DR RefSeq; WP_004144729.1; NZ_KN046818.1. DR EnsemblBacteria; AIJ41524; AIJ41524; FH42_12590. DR EnsemblBacteria; AIT00307; AIT00307; PMK1_00810. DR EnsemblBacteria; AIW98088; AIW98088; LQ47_02900. DR EnsemblBacteria; AJB56067; AJB56067; KU54_004475. DR EnsemblBacteria; AJB74524; AJB74524; LI86_04480. DR EnsemblBacteria; KEG36558; KEG36558; EQ82_23785. DR EnsemblBacteria; KEP96627; KEP96627; FP68_17045. DR EnsemblBacteria; KFC44073; KFC44073; ER51_23940. DR EnsemblBacteria; KFG23866; KFG23866; IA58_02105. DR EnsemblBacteria; KFG24014; KFG24014; HZ19_02115. DR EnsemblBacteria; KFJ76366; KFJ76366; DR88_2513. DR EnsemblBacteria; KGB16646; KGB16646; KPPR1_21890. DR EnsemblBacteria; KGK52392; KGK52392; EU63_07255. DR EnsemblBacteria; KGY31042; KGY31042; MC75_05110. DR EnsemblBacteria; KHF62927; KHF62927; LV59_04958. DR EnsemblBacteria; KHQ38044; KHQ38044; LI83_11485. DR EnsemblBacteria; KHQ44511; KHQ44511; LI84_04495. DR Proteomes; UP000029666; Chromosome. 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 Complete proteome {ECO:0000313|Proteomes:UP000029666}; 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 //