ID A0A060VEI2_KLEPN Unreviewed; 1178 AA. AC A0A060VEI2; A0A4V6LY54; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 27-NOV-2024, entry version 82. 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 EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_01485}; DE AltName: Full=DNA 3'-5' helicase subunit RecB {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:SSK22687.1}; GN ORFNames=B5L96_03585 {ECO:0000313|EMBL:OVF77140.1}, EXT45_08840 GN {ECO:0000313|EMBL:RZG38558.1}, SAMEA3649615_02629 GN {ECO:0000313|EMBL:SYU71173.1}, SAMEA4364603_01010 GN {ECO:0000313|EMBL:SSK22687.1}, SAMEA4873632_03212 GN {ECO:0000313|EMBL:VGK96966.1}; OS Klebsiella pneumoniae. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella. OX NCBI_TaxID=573 {ECO:0000313|EMBL:SSK22687.1, ECO:0000313|Proteomes:UP000252603}; RN [1] {ECO:0000313|EMBL:OVF77140.1, ECO:0000313|Proteomes:UP000196447} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=39383 {ECO:0000313|EMBL:OVF77140.1, RC ECO:0000313|Proteomes:UP000196447}; RA Fouts D., Stalin M.J., Chen L., Wright M., Sutton G., Nguyen K., RA Vanduin D., Rojas L., Hujer A., Hujer K., Bonomo R., Kreiswirth B., RA Adams M.; RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:SSK22687.1, ECO:0000313|Proteomes:UP000252603} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4300STDY6470422 {ECO:0000313|EMBL:SSK22687.1, RC ECO:0000313|Proteomes:UP000252603}, 5012STDY7626430 RC {ECO:0000313|EMBL:VGK96966.1, ECO:0000313|Proteomes:UP000376235}, and RC EuSCAPE_ES277 {ECO:0000313|EMBL:SYU71173.1, RC ECO:0000313|Proteomes:UP000259417}; RG Pathogen Informatics; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:RZG38558.1, ECO:0000313|Proteomes:UP000293472} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=53 {ECO:0000313|EMBL:RZG38558.1, RC ECO:0000313|Proteomes:UP000293472}; RA Newire E., Aydin A., Juma S., Enne V., Roberts A.P.; RT "Identification of a Type IV CRISPR-Cas system located exclusively on RT IncHI1B/ IncFIB plasmids in Enterobacteriaceae."; RL Submitted (FEB-2019) 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 highly CC rapid and processive ATP-dependent bidirectional helicase activity. CC Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) CC sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the CC Chi site. The properties and activities of the enzyme are changed at CC Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and CC facilitates RecA-binding to the ssDNA for homologous DNA recombination CC and repair. Holoenzyme degrades any linearized DNA that is unable to CC undergo homologous recombination. In the holoenzyme this subunit CC contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA CC onto ssDNA. {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4; CC Evidence={ECO:0000256|ARBA:ARBA00034618, ECO:0000256|HAMAP- CC Rule:MF_01485}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by CC translocating in the 3'-5' direction.; EC=5.6.2.4; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01485}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Exonucleolytic cleavage (in the presence of ATP) in either CC 5'- to 3'- or 3'- to 5'-direction to yield 5'- CC phosphooligonucleotides.; EC=3.1.11.5; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01485}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01485}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01485}; CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute CC to DNA-binding. Interacts with RecA. {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- DOMAIN: The C-terminal domain has nuclease activity and interacts with CC RecD. It interacts with RecA, facilitating its loading onto ssDNA. CC {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- DOMAIN: The N-terminal DNA-binding domain is a ssDNA-dependent ATPase CC and has ATP-dependent 3'-5' helicase function. This domain interacts CC with RecC. {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- MISCELLANEOUS: In the RecBCD complex, RecB has a slow 3'-5' helicase, CC an exonuclease activity and loads RecA onto ssDNA, RecD has a fast 5'- CC 3' helicase activity, while RecC stimulates the ATPase and processivity CC of the RecB helicase and contributes to recognition of the Chi site. CC {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily. 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; NDBK01000017; OVF77140.1; -; Genomic_DNA. DR EMBL; SGOL01000007; RZG38558.1; -; Genomic_DNA. DR EMBL; UFEU01000002; SSK22687.1; -; Genomic_DNA. DR EMBL; ULET01000005; SYU71173.1; -; Genomic_DNA. DR EMBL; CAAHCC010000005; VGK96966.1; -; Genomic_DNA. DR RefSeq; WP_015875135.1; NZ_WYAM01000010.1. DR Proteomes; UP000196447; Unassembled WGS sequence. DR Proteomes; UP000252603; Unassembled WGS sequence. DR Proteomes; UP000259417; Unassembled WGS sequence. DR Proteomes; UP000293472; Unassembled WGS sequence. DR Proteomes; UP000376235; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:TreeGrafter. DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule. DR CDD; cd22352; RecB_C-like; 1. DR CDD; cd18807; SF1_C_UvrD; 1. DR FunFam; 3.90.320.10:FF:000003; RecBCD enzyme subunit RecB; 1. DR Gene3D; 3.90.320.10; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR Gene3D; 1.10.3170.10; Recbcd, chain B, domain 2; 1. DR HAMAP; MF_01485; RecB; 1. DR InterPro; IPR014017; DNA_helicase_UvrD-like_C. DR InterPro; IPR000212; DNA_helicase_UvrD/REP. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011604; PDDEXK-like_dom_sf. DR InterPro; IPR038726; PDDEXK_AddAB-type. DR InterPro; IPR004586; RecB. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR014016; UvrD-like_ATP-bd. DR NCBIfam; TIGR00609; recB; 1. DR PANTHER; PTHR11070:SF23; RECBCD ENZYME SUBUNIT RECB; 1. DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1. DR Pfam; PF12705; PDDEXK_1; 1. DR Pfam; PF00580; UvrD-helicase; 1. DR Pfam; PF13361; UvrD_C; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF52980; Restriction endonuclease-like; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01485}; Coiled coil {ECO:0000256|SAM:Coils}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP- KW Rule:MF_01485}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP- KW Rule:MF_01485}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_01485}; KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP- KW Rule:MF_01485}; KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01485}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01485}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01485}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01485}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01485}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01485}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01485}. FT DOMAIN 2..450 FT /note="UvrD-like helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51198" FT DOMAIN 480..746 FT /note="UvrD-like helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51217" FT REGION 1..844 FT /note="DNA-binding and helicase activity, interacts with FT RecC" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT REGION 897..1178 FT /note="Nuclease activity, interacts with RecD and RecA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT COILED 782..809 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 1077 FT /note="For nuclease activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT BINDING 23..30 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560" FT BINDING 953 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT BINDING 1064 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT BINDING 1077 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule: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 //