ID A0A4D6XS20_9GAMM Unreviewed; 1162 AA. AC A0A4D6XS20; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 24-JAN-2024, entry version 18. 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:QCI17260.1}; GN ORFNames=D9V62_02300 {ECO:0000313|EMBL:QCI17260.1}; OS Buchnera aphidicola (Aphis helianthi). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=2315802 {ECO:0000313|EMBL:QCI17260.1, ECO:0000313|Proteomes:UP000298759}; RN [1] {ECO:0000313|EMBL:QCI17260.1, ECO:0000313|Proteomes:UP000298759} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ahe {ECO:0000313|EMBL:QCI17260.1, RC ECO:0000313|Proteomes:UP000298759}; RA Chong R.A.; RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QCI17260.1, ECO:0000313|Proteomes:UP000298759} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ahe {ECO:0000313|EMBL:QCI17260.1, RC ECO:0000313|Proteomes:UP000298759}; RA Moran N.A.; RT "Genome evolution of the obligate endosymbiont Buchnera aphidicola."; RL Submitted (MAY-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 + H(+) + phosphate; 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}; 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 --------------------------------------------------------------------------- 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; CP034894; QCI17260.1; -; Genomic_DNA. DR AlphaFoldDB; A0A4D6XS20; -. DR OrthoDB; 9810135at2; -. DR Proteomes; UP000298759; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; 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 CDD; cd22352; RecB_C-like; 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; 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; 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}; DNA damage {ECO:0000256|HAMAP-Rule:MF_01485}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01485}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_01485}; Exonuclease {ECO:0000256|HAMAP-Rule:MF_01485}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000256|PROSITE- KW ProRule:PRU00560}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000256|PROSITE- KW ProRule:PRU00560}; 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}; Nuclease {ECO:0000256|HAMAP-Rule:MF_01485}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01485}. FT DOMAIN 1..440 FT /note="UvrD-like helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51198" FT DOMAIN 483..735 FT /note="UvrD-like helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51217" FT REGION 1..874 FT /note="DNA-binding and helicase activity, interacts with FT RecC" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT REGION 887..1162 FT /note="Nuclease activity, interacts with RecD and RecA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT ACT_SITE 1066 FT /note="For nuclease activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT BINDING 20..27 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560" FT BINDING 942 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT BINDING 1053 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT BINDING 1066 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" SQ SEQUENCE 1162 AA; 139028 MW; 5F1FA975D3D63731 CRC64; MKKKLNIFNI PCNGIKLIEA SAGTGKTTSI VLMYLRLLLG IGSKKNNKPL LIQEILVVTF TNFAKEEIYK RIKKNIEQLY LYCITKNTNN SILKPFFKKI KNLEETIHLL EQAKKNINHM SIYTIHGFCK NILKLNFLNF HQKIIEDEKL LYLQATEDFW RSYFYEVPKK IINIILQDYK NPESLLSELK PIFNFRKVYF KKKFNKNQNL ITCHEENINI INIFKKKWLD YNPIILNIVK ELKPNKKIYN DFNISRWQKN ITKWAESETE DYQIPITLKY FLKDTIIKNI KSNQIPCHIF FQDIEKILKI KFSLKDIILF QAIKKITKFL NKEKQKKFLL GFNDLLDTLL KYIKKEKTLR KLIIEKYPIV FIDEFQDTDI QQYQIFNILY NKNNKQTGLF LIGDPKQSIY SFRGADIFSY LYAKSKIKKY YYLNNNWRSS KNICKAINYL FLRNKNPFLF KDIPFIKISS SFNNQNIQFK IKGRIQTAIS FFFKKKEKIY IKDYQEWISK QCANEICYWL ICAKKGEAIL INKDKERILK TNDIVILVRN KNEANIIQNS LEKVNIQSIY SSSNQNIFKT TDAFELLIIL QTILQPTNIK LLKQSIFTHI FYNILLQGKK QNKIKQSYFI IKKLYEYREI WKNVGIFYTI KTIVLDYQKY SNDLNKTQYY QKNINFLHIA ELLEKQSEYL YQDSSLIRWF ENKILEKQNI LEDEHIRYFK QSNAIKIITI HKSKGLEYPI VWIPFAATYK KSNVYLYHDK KTFKMFLDLN QNKETEKIAD EERLAEDLRF LYVAITRSIF HCSIGMGDII NKKHQKTNNN HKSALGYIIQ RGCYMNYNNL LNELSLLNAK SYIKVKYDTM NIKLPYTKQD VYLLSPPQYI IKKIQNCFQI TSFTKLKKEH VSLNKSQDNY NINNILDYKS IYKKQIIFEN FPRGEKTGIL MHYILNKINF IEKLNINFFY KVLKQYEFSE KWAPILMSWV NNIINVKLKN INVNLSMLKQ NQYIKEMKFF LPIQKTLNSI DFNHIIQSLD PISSLTSKIS FNPITGILTG SIDLVFIWNE RYYIIDYKSN YLGDNQNLYS LKNIKKEIIK NRYDLQYQIY TVALHQYLTK KLKKYKYKNN FGGVFYMFLR GINKINENNS IFYTIPDYLL IKKLINLFLI KN //