ID A0A060VEI2_KLEPN Unreviewed; 1178 AA. AC A0A060VEI2; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 14-OCT-2015, entry version 14. DE RecName: Full=RecBCD enzyme subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485}; DE EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01485}; DE AltName: Full=Exonuclease V subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485}; DE AltName: Full=Helicase/nuclease RecBCD subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485}; GN Name=recB {ECO:0000256|HAMAP-Rule:MF_01485, GN ECO:0000313|EMBL:CDQ52794.1}; GN ORFNames=KpST82_3861 {ECO:0000313|EMBL:CDQ52794.1}, SL19_03012 GN {ECO:0000313|EMBL:KLZ65660.1}, SL33_03369 GN {ECO:0000313|EMBL:KMA25585.1}, SL56_02656 GN {ECO:0000313|EMBL:KMB42843.1}, SL69_00289 GN {ECO:0000313|EMBL:KMD13508.1}, SM57_03455 GN {ECO:0000313|EMBL:KMW85428.1}, SM59_03084 GN {ECO:0000313|EMBL:KMG72983.1}, SM63_03982 GN {ECO:0000313|EMBL:KMG96656.1}, SM64_03375 GN {ECO:0000313|EMBL:KMG96156.1}, SM76_03398 GN {ECO:0000313|EMBL:KMH65702.1}, SM83_03357 GN {ECO:0000313|EMBL:KMI02818.1}, SM84_02761 GN {ECO:0000313|EMBL:KMI08581.1}, SM92_03492 GN {ECO:0000313|EMBL:KMI44139.1}, SM94_03269 GN {ECO:0000313|EMBL:KMI56822.1}; OS Klebsiella pneumoniae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=573 {ECO:0000313|EMBL:CDQ52794.1}; RN [1] {ECO:0000313|EMBL:CDQ52794.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SB3193 {ECO:0000313|EMBL:CDQ52794.1}; RA Genoscope - CEA; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KMW85428.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MGH83 {ECO:0000313|EMBL:KMW85428.1}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A.M., Onderdonk A.B., Kirby J., Ferraro M.J., Huang S., RA Spencer M., Fodor A., Hooper D., Dekker J., O'Brien T., Quan V., RA Gombosev A., Delaney M., Dubois A., Ernst C., Kim D.S., Rossman W., RA Gohs F., Petruso H., Nozar T., Mougeot F., Manson-Mcguire A., RA Young S., Abouelleil A., Cao P., Chapman S.B., Griggs A., Priest M., RA Shea T., Wortman I., Wortman J.R., Nusbaum C., Birren B.; RT "The Genome Sequence of None."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:KLZ65660.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BIDMC85 {ECO:0000313|EMBL:KMI02818.1}, BIDMC86 RC {ECO:0000313|EMBL:KMI08581.1}, CHS107 {ECO:0000313|EMBL:KLZ65660.1}, RC CHS121 {ECO:0000313|EMBL:KMA25585.1}, CHS145 RC {ECO:0000313|EMBL:KMB42843.1}, CHS159 {ECO:0000313|EMBL:KMD13508.1}, RC MGH116 {ECO:0000313|EMBL:KMH65702.1}, MGH89 RC {ECO:0000313|EMBL:KMG72983.1}, MGH93 {ECO:0000313|EMBL:KMG96656.1}, RC MGH94 {ECO:0000313|EMBL:KMG96156.1}, UCI70 RC {ECO:0000313|EMBL:KMI44139.1}, and UCI76 RC {ECO:0000313|EMBL:KMI56822.1}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Earl A.M., Onderdonk A.B., Kirby J., Ferraro M.J., Huang S., RA Spencer M., Fodor A., Hooper D., Dekker J., O'Brien T., Quan V., RA Gombosev A., Delaney M., DuBois A., Ernst C., Kim D.S., Rossman W., RA Gohs F., Petruso H., Nozar T., Mougeot F., Manson-McGuire A., RA Young S., Abouelleil A., Cao P., Chapman S.B., Griggs A., Priest M., RA Shea T., Wortman I., Wortman J.R., Nusbaum C., Birren B.; RT "The Genome Sequence of None."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for CC recombinational DNA repair. Binds to DSBs and unwinds DNA via a CC highly rapid and processive ATP-dependent bidirectional helicase CC activity. Degrades ssDNA until it encounters a chi (crossover CC hotspot instigator) sequence from the 3' direction. Cuts DNA near CC or within the chi site, which attenuates 3'- but not 5'- CC exonuclease activity. The altered holoenzyme produces a long 3'- CC ssDNA overhang and facilitates RecA-binding to the ssDNA for CC homologous DNA recombination and repair. Holoenzyme degrades CC foreign DNA, contributing to antiviral protection. This subunit CC has DNA-dependent ATPase activity, exo- and endonuclease activity, CC 3'-5' helicase activity and loads RecA onto ssDNA. CC {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage (in the presence of CC ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'- CC phosphooligonucleotides. {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01485}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01485}; CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits CC contribute to DNA-binding. Interacts with RecA. CC {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- DOMAIN: The C-terminal domain has nuclease activity and interacts CC with RecD. It interacts with RecA, facilitating its loading onto CC ssDNA. {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- DOMAIN: The N-terminal DNA-binding domain is a ssDNA-dependent CC ATPase and has ATP-dependent 3'-5' helicase function. This domain CC interacts with RecC. {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- SIMILARITY: Contains 1 uvrD-like helicase ATP-binding domain. CC {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- SIMILARITY: Contains 1 uvrD-like helicase C-terminal domain. CC {ECO:0000256|HAMAP-Rule:MF_01485}. 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; CDQ52794.1; -; Genomic_DNA. DR EMBL; LEVR01000010; KLZ65660.1; -; Genomic_DNA. DR EMBL; LEWC01000017; KMA25585.1; -; Genomic_DNA. DR EMBL; LEWW01000025; KMB42843.1; -; Genomic_DNA. DR EMBL; LEXJ01000001; KMD13508.1; -; Genomic_DNA. DR EMBL; LFAA01000006; KMG72983.1; -; Genomic_DNA. DR EMBL; LFAF01000006; KMG96156.1; -; Genomic_DNA. DR EMBL; LFAE01000025; KMG96656.1; -; Genomic_DNA. DR EMBL; LFAR01000014; KMH65702.1; -; Genomic_DNA. DR EMBL; LFAY01000065; KMI02818.1; -; Genomic_DNA. DR EMBL; LFAZ01000002; KMI08581.1; -; Genomic_DNA. DR EMBL; LFBG01000013; KMI44139.1; -; Genomic_DNA. DR EMBL; LFBI01000010; KMI56822.1; -; Genomic_DNA. DR EMBL; LGJJ01000012; KMW85428.1; -; Genomic_DNA. DR RefSeq; WP_015875135.1; NZ_LK022715.1. DR STRING; 272620.KPN_03229; -. DR EnsemblBacteria; KGB16514; KGB16514; KPPR1_21210. DR EnsemblBacteria; KHQ21480; KHQ21480; KU56_07395. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 5. DR Gene3D; 3.90.320.10; -; 1. DR HAMAP; MF_01485; RecB; 1. DR InterPro; IPR014017; DNA_helicase_UvrD-like_C. DR InterPro; IPR000212; DNA_helicase_UvrD/REP. DR InterPro; IPR011604; Exonuc_phg/RecB_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004586; RecB. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR014016; UvrD-like_ATP-bd. DR PANTHER; PTHR11070; PTHR11070; 1. DR Pfam; PF00580; UvrD-helicase; 1. DR Pfam; PF13361; UvrD_C; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR SUPFAM; SSF52980; SSF52980; 1. DR TIGRFAMs; TIGR00609; recB; 1. DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1. DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1. PE 3: Inferred from homology; KW Antiviral defense {ECO:0000256|HAMAP-Rule:MF_01485}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00146071}; Coiled coil {ECO:0000256|SAM:Coils}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00048487}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00048304}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00048455}; KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_01485}; KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00289199}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00146013}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00146062}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01485}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01485}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00289189}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00145996}. FT DOMAIN 2 450 UvrD-like helicase ATP-binding. FT {ECO:0000256|HAMAP-Rule:MF_01485}. FT DOMAIN 480 746 UvrD-like helicase C-terminal. FT {ECO:0000256|HAMAP-Rule:MF_01485}. FT NP_BIND 23 30 ATP. {ECO:0000256|HAMAP-Rule:MF_01485}. FT REGION 1 852 DNA-binding and helicase activity, FT interacts with RecC. {ECO:0000256|HAMAP- FT Rule:MF_01485}. FT REGION 897 1178 Nuclease activity, interacts with RecD FT and RecA. {ECO:0000256|HAMAP-Rule: FT MF_01485}. FT COILED 215 235 {ECO:0000256|SAM:Coils}. FT COILED 782 809 {ECO:0000256|SAM:Coils}. FT METAL 953 953 Magnesium; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01485}. FT METAL 1064 1064 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01485}. FT METAL 1077 1077 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01485}. SQ SEQUENCE 1178 AA; 132874 MW; 7F6AB8858C3A7161 CRC64; MTDTAESLDP LRLPLIGERL IEASAGTGKT FTIAALYLRL LLGLGGEAAY PRAISVEELL VVTFTEAATE ELRGRIRSNI HELRIACLRG ESDNPLYSAL LAEIADKDDA AKTLLLAERQ MDEAAVFTIH GFCQRMLSLN AFESGMLFEQ QLIEDESRLR YQACADFWRR HCYPLTRDIA AVIHDVWKGP RDLLKSLDRW LQGEAPQLKS PPAPNETLAE RHQQIIARID SLKQQWREQV GEIEGVLENS GLDRRKFNRG NQGKWMEKVN AWAQEETLSY QLPDALEKFA QSFLLERTKA GGEPPVHPLF SAVESLLASS LTLTDLVLAR AMVEIRDAVA REKRRRGELG FDDMLSRLDE ALRGDSGETL ASAIRQRFPV AMIDEFQDTD PQQYRIFRRI WRRQPETALL LIGDPKQAIY AFRGADIFTY MKARGDVAAH YTLDTNWRSS PGMVGSVNRL FSLSDNPFMF HEIPFLPVKA AAKNKGLRFT VDAADVPAMN VWLMPGDTVG SGDYQTFMAQ LCATQIRDWL SAGQQGRALL WRGETSRPVQ ASDITVLVRN RLEAAQVREA LQTLGIPSVY LSNRDSVFET LEAQELLWLL QAVLAPEREN TLRSALATSM FGLTALDIEN LNQDEQAWDA LVEEFSEYRQ IWRQRGVMPM LRALMTARHI AENLLATRGG ERRLTDILHI SELLQEAASQ LESEHALVRW LAQHIAEPDS NAASQQMRLE SDKHLVQIVT IHKSKGLEYP LVWLPFIARF RKQDQAFYHD RETFAAVLDL GQDEASLELA EAERLAEDLR LLYVALTRAV WHCSLGVAPL SSRKSGNSDF HLSALGRLLQ AGEAMDAAGL AARLADFCHG DIALQIPGEL DLTPWQAPAA TIPRLSAREL QRRIADDWRV TSYSGLQQHG FSGGQDLLPR LDVDAAGVGE VVEEPQLTPH QFPRGAAPGT FLHSLFEELD FTQPVPEGWM AEKLQLSGFD AQWAPVLTDW LGGVLKTRLP GPDIALNQLA ARDKQVEMAF YLPIAQLLTA ERLDALIRQY DPLSADTPPL DFRQVRGMLK GFIDLVFRHE GRYYLLDYKS NWLGEDREAY TRPAMEQAMR AHRYDLQYQL YSLALHRYLR HRLADYDYDR HFGGVIYLFL RGMDGQEGGQ GIFTTRPVRP LIDGLDQLFA GETQEEAS //