ID A0A060VEI2_KLEPN Unreviewed; 1178 AA. AC A0A060VEI2; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 07-JUN-2017, entry version 32. 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 Short=ExoV 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}, SM57_03455 GN {ECO:0000313|EMBL:KMW85428.1}; OS Klebsiella pneumoniae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=573 {ECO:0000313|EMBL:CDQ52794.1, ECO:0000313|Proteomes:UP000053587}; RN [1] {ECO:0000313|EMBL:CDQ52794.1, ECO:0000313|Proteomes:UP000053587} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB3193 {ECO:0000313|EMBL:CDQ52794.1, RC ECO:0000313|Proteomes:UP000053587}; RA Genoscope - CEA; RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KMW85428.1, ECO:0000313|Proteomes:UP000037134} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGH83 {ECO:0000313|EMBL:KMW85428.1, RC ECO:0000313|Proteomes:UP000037134}; 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. Unwinds dsDNA until it encounters a Chi (crossover CC hotspot instigator) sequence from the 3' direction. Cuts ssDNA a CC few nucleotides 3' to the Chi site. The properties and activities CC of the enzyme are changed at Chi. The Chi-altered holoenzyme CC produces a long 3'-ssDNA overhang and facilitates RecA-binding to CC the ssDNA for homologous DNA recombination and repair. Holoenzyme CC degrades any linearized DNA that is unable to undergo homologous CC recombination. In the holoenzyme this subunit contributes ATPase, CC 3'-5' helicase, exonuclease 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, ECO:0000256|SAAS:SAAS00597767}. 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; LGJJ01000012; KMW85428.1; -; Genomic_DNA. DR RefSeq; WP_015875135.1; NZ_MPCK01000001.1. DR RefSeq; WP_015875135.1; NZ_MPYL01000018.1. DR STRING; 272620.KPN_03229; -. DR PATRIC; fig|573.1355.peg.4322; -. DR eggNOG; ENOG4107QKA; Bacteria. DR eggNOG; COG1074; LUCA. DR Proteomes; UP000037134; Unassembled WGS sequence. DR Proteomes; UP000053587; Unassembled WGS sequence. 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:UniProtKB-EC. 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; 3.90.320.10; -; 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 InterPro; IPR034739; UvrD/AddA_N. DR PANTHER; PTHR11070; PTHR11070; 1. DR PANTHER; PTHR11070:SF29; PTHR11070:SF29; 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 ATP-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00753523}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000037134, KW ECO:0000313|Proteomes:UP000053587}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00753507}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00753512}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00627189}; KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00753531}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00493105}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00753525}; 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:SAAS00753541}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00753533}. FT DOMAIN 2 450 UvrD-like helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51198}. FT DOMAIN 480 746 UvrD-like helicase C-terminal. FT {ECO:0000259|PROSITE:PS51217}. FT REGION 1 846 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 782 809 {ECO:0000256|SAM:Coils}. FT ACT_SITE 1077 1077 For nuclease activity. FT {ECO:0000256|HAMAP-Rule:MF_01485}. 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 //