ID A0A0B7J5D1_9GAMM Unreviewed; 1205 AA. AC A0A0B7J5D1; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 29-SEP-2021, entry version 35. 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:CEO38256.1}; GN ORFNames=PPBDW_I20269 {ECO:0000313|EMBL:CEO38256.1}; OS Photobacterium kishitanii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Photobacterium. OX NCBI_TaxID=318456 {ECO:0000313|EMBL:CEO38256.1, ECO:0000313|Proteomes:UP000019762}; RN [1] {ECO:0000313|EMBL:CEO38256.1, ECO:0000313|Proteomes:UP000019762} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ANT220 {ECO:0000313|Proteomes:UP000019762}; RA Genoscope - CEA; RL Submitted (DEC-2014) 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 + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; CC Evidence={ECO:0000256|ARBA:ARBA00001665}; 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}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:CEO38256.1}. 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; CCAR020000004; CEO38256.1; -; Genomic_DNA. DR RefSeq; WP_054262090.1; NZ_LN794352.1. DR STRING; 1454202.PPBDW_120137___1; -. DR EnsemblBacteria; CEO38256; CEO38256; PPBDW_I20269. DR GeneID; 29942242; -. DR eggNOG; COG1074; Bacteria. DR Proteomes; UP000019762; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0140603; F:ATP hydrolysis activity; IEA:RHEA. 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; 3.40.50.300; -; 2. 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 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|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01485}; 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}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_01485}; KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP- KW Rule:MF_01485}; Helicase {ECO:0000256|HAMAP-Rule:MF_01485}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000313|EMBL:CEO38256.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01485}; KW Metal-binding {ECO:0000256|HAMAP-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 9..456 FT /note="UvrD-like helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51198" FT DOMAIN 487..756 FT /note="UvrD-like helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51217" FT REGION 1..866 FT /note="DNA-binding and helicase activity, interacts with FT RecC" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT REGION 914..1205 FT /note="Nuclease activity, interacts with RecD and RecA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT ACT_SITE 1107 FT /note="For nuclease activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT METAL 980 FT /note="Magnesium; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT METAL 1094 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT METAL 1107 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" SQ SEQUENCE 1205 AA; 135182 MW; 645E2B41FB7141EB CRC64; MATEVLTTEV LTNILQPMTF PLHGTRLIEA SAGTGKTFTI ASLYLRLLLG HGNDNNRHQQ QLTVDQILVV TFTEAATAEL RDRIRARIHD ARLAFSRGVS HDPVIAPLLN EHQDHKLAAT ILLQAERQMD EAAIYTIHGF CQRMLTQNAF ESGSRFNNEF VTDESQLKKL VVADYWRSNF YHLPPALAHE VREIWSSPTA LLKEIGNSLT GAPVRLSVAA MTESLAQLHQ QNIVRIDEVK ALWRAHQADL EALIASSGIN KRSYTKKSLP NWLEQVSGWA AQPTVGYELP DNLIRFHQQT LIEKTAKGDA PEHAVFSAIA ELLDNPANLR EPLLAHAIEH CRQLLADAKA RKGWLSFDDL LTQLGAAIDN DVDELLAGKI RAQYPVAMID EFQDTDPLQY GIFSDVYRHH PECGLFMIGD PKQAIYAFRG ADIFTYIQAR RQVSDHYTLA TNWRSTANMI AAVNGVFQQP DSPFIYDQDI EFLAVDHSPK AAQRSWWLEG EAQHALTFWL QESADGKPIT KGNYQATMAA ATAAQIQHIL TQSQQQQAYF LDGEQQHAIA AGDIAVLVRT GTEGRLVREV LSKQGIASVY LSNRDSVFST SEAADIQRLL QAVLTPEDDR ILRAALASGL FARTAIELDQ LNNDENEWEI AVNSFKQYRQ QWLKRGVMPM LRSVMAKNQI AERLLAEDGG ERKLTDLLHI GELLQQASQT LDSDYALLRW LAEHVAEPDG NADDQVMRLE SERNLVQIVT IHKSKGLEYD LVFMPFVCSY REVDSKGEVK YHDEVDNITV LDIAKQAAAI EKADQERLAE DLRLIYVALT RAVYGCYVGM APIRNGRSTK EPTGLHRSAM GHLVQNGQAG GVAALELALA KLSEAQIAIT VTAPPQLLDS QWQPQDEVTE ALVKRPFAAS LERNWWMTSY SNLVKQGHQT AHDSSLDLPG FDIDSVQNAT EEVDDSELEL EPQYSIYTFP RGARPGTFLH TVFEEIDFTA AVDCDETVAK LTELLQLENY ELAWLPVLQQ LIRDVLTCPL DGDMLRLADK TASQRLTEME FLLPIEILQA VTLNKVIAKH DPLSAKAGEL GFATVSGMLK GFIDLVFEHQ GKYYVLDWKS NYLGDDPQVY RGEQLQTAMR EHRYDLQYQI YALALQRFLR SRIPNYSYET HFGGVYYLFL RGVQAGSDSG IFYARPSEIL LDELDLVMNG ALPHA //