ID A0A060VEI2_KLEPN Unreviewed; 1178 AA. AC A0A060VEI2; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 26-FEB-2020, entry version 58. 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:SSK22687.1}; GN ORFNames=B4U61_15930 {ECO:0000313|EMBL:TEB00300.1}, BANRA_03656 GN {ECO:0000313|EMBL:VCZ45015.1}, C2D59_04600 GN {ECO:0000313|EMBL:QFY32358.1}, C2D61_04805 GN {ECO:0000313|EMBL:QFY26942.1}, C4Y50_023875 GN {ECO:0000313|EMBL:ROG81646.1}, C7V41_04760 GN {ECO:0000313|EMBL:PWF60258.1}, EQH51_25195 GN {ECO:0000313|EMBL:QFU72834.1}, EXT45_08840 GN {ECO:0000313|EMBL:RZG38558.1}, FNY87_16825 GN {ECO:0000313|EMBL:TRW04050.1}, FOB38_25720 GN {ECO:0000313|EMBL:QET11489.1}, SAMEA4364603_01010 GN {ECO:0000313|EMBL:SSK22687.1}; OS Klebsiella pneumoniae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=573 {ECO:0000313|EMBL:SSK22687.1, ECO:0000313|Proteomes:UP000252603}; RN [1] {ECO:0000313|EMBL:TEB00300.1, ECO:0000313|Proteomes:UP000297943} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MEC097 {ECO:0000313|EMBL:TEB00300.1, RC ECO:0000313|Proteomes:UP000297943}; RA Arya A.S.; RT "Isolation of Levoglucosan Utilizing Bacteria."; RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QFY26942.1, ECO:0000313|Proteomes:UP000325416, ECO:0000313|Proteomes:UP000326098} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=11420 {ECO:0000313|EMBL:QFY32358.1, RC ECO:0000313|Proteomes:UP000325416}, and 13190 RC {ECO:0000313|EMBL:QFY26942.1, ECO:0000313|Proteomes:UP000326098}; RA Jia X., Ma G., Zhan Z., Zhou D., Chen F.; RT "Hypervirulent and multidrug-resistant Klebsiella pneumoniae."; RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:PWF60258.1, ECO:0000313|Proteomes:UP000245017} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KPL0.2 {ECO:0000313|EMBL:PWF60258.1, RC ECO:0000313|Proteomes:UP000245017}; RA Le Guern R., Grandjean T., Bauduin M., Loquet A., Faure K., Kipnis E., RA Dessein R.; RT "A murine model of gut colonization with Klebsiella pneumoniae NDM."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. RN [4] {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}; RG Pathogen Informatics; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:ROG81646.1, ECO:0000313|Proteomes:UP000286610} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CRK0390 {ECO:0000313|EMBL:ROG81646.1, RC ECO:0000313|Proteomes:UP000286610}; RA Vanduin D., Fouts D., Sutton G., Nguyen K., Hujer A., Hujer K., Bonomo R.; RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:VCZ45015.1, ECO:0000313|Proteomes:UP000269373} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Kpneu037 {ECO:0000313|EMBL:VCZ45015.1}; RA Noll B N.; RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:QFU72834.1, ECO:0000313|Proteomes:UP000326148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TH164 {ECO:0000313|EMBL:QFU72834.1, RC ECO:0000313|Proteomes:UP000326148}; RA Hadjadj L., Rolain J.-M.; RT "Genome of KpTH164."; RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases. RN [8] {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. RN [9] {ECO:0000313|EMBL:TRW04050.1, ECO:0000313|Proteomes:UP000317393} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCPM-O-B-8658 {ECO:0000313|EMBL:TRW04050.1}, and SCPM-O-B-8658 RC (KPB536) {ECO:0000313|Proteomes:UP000317393}; RA Myakinina V., Fursova N., Volozhantsev N., Sizova A., Kislichkina A., RA Bogun A., Mukhina T., Mayskaya N.; RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|EMBL:QET11489.1, ECO:0000313|Proteomes:UP000324621} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_630 {ECO:0000313|EMBL:QET11489.1, RC ECO:0000313|Proteomes:UP000324621}; RA Bachman M., Young C., Tallon L., Sadzewicz L., Vavikolanu K., Mehta A., RA Aluvathingal J., Nadendla S., Nandy P., Geyer C., Yan Y., Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx tests."; RL Submitted (SEP-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=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 -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000256|SAAS:SAAS00709641}. 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; PYBH01000003; PWF60258.1; -; Genomic_DNA. DR EMBL; CP044039; QET11489.1; -; Genomic_DNA. DR EMBL; CP035210; QFU72834.1; -; Genomic_DNA. DR EMBL; CP026017; QFY26942.1; -; Genomic_DNA. DR EMBL; CP026023; QFY32358.1; -; Genomic_DNA. DR EMBL; PTFF02000106; ROG81646.1; -; Genomic_DNA. DR EMBL; SGOL01000007; RZG38558.1; -; Genomic_DNA. DR EMBL; UFEU01000002; SSK22687.1; -; Genomic_DNA. DR EMBL; MWQX01000021; TEB00300.1; -; Genomic_DNA. DR EMBL; VKCR01000020; TRW04050.1; -; Genomic_DNA. DR EMBL; UWXT01000001; VCZ45015.1; -; Genomic_DNA. DR RefSeq; WP_015875135.1; NZ_WFJJ01000027.1. DR eggNOG; ENOG4107QKA; Bacteria. DR eggNOG; COG1074; LUCA. DR Proteomes; UP000245017; Unassembled WGS sequence. DR Proteomes; UP000252603; Unassembled WGS sequence. DR Proteomes; UP000269373; Unassembled WGS sequence. DR Proteomes; UP000286610; Unassembled WGS sequence. DR Proteomes; UP000293472; Unassembled WGS sequence. DR Proteomes; UP000297943; Unassembled WGS sequence. DR Proteomes; UP000317393; Unassembled WGS sequence. DR Proteomes; UP000324621; Chromosome. DR Proteomes; UP000325416; Chromosome. DR Proteomes; UP000326098; Chromosome. DR Proteomes; UP000326148; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC. 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 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; IPR038726; PDDEXK_AddAB-type. 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:SF23; PTHR11070:SF23; 1. DR Pfam; PF12705; PDDEXK_1; 1. DR Pfam; PF00580; UvrD-helicase; 1. DR Pfam; PF13361; UvrD_C; 1. DR SUPFAM; SSF52540; SSF52540; 1. 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:SAAS00146071}; Coiled coil {ECO:0000256|SAM:Coils}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS01099294}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS01099287}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00745286}; KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS01033115, ECO:0000313|EMBL:SSK22687.1}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000256|SAAS:SAAS00553650}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000256|SAAS:SAAS00146062, KW ECO:0000313|EMBL:SSK22687.1}; Magnesium {ECO:0000256|HAMAP-Rule:MF_01485}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01485}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000256|SAAS:SAAS01033141}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00145996}. 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 215..235 FT /evidence="ECO:0000256|SAM:Coils" 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 METAL 953 FT /note="Magnesium; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT METAL 1064 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT METAL 1077 FT /note="Magnesium" 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 //