ID F9ZQ70_ACICS Unreviewed; 1185 AA. AC F9ZQ70; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 12-AUG-2020, entry version 63. 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 OrderedLocusNames=Atc_0256 {ECO:0000313|EMBL:AEK56907.1}; OS Acidithiobacillus caldus (strain SM-1). OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales; OC Acidithiobacillaceae; Acidithiobacillus. OX NCBI_TaxID=990288 {ECO:0000313|EMBL:AEK56907.1, ECO:0000313|Proteomes:UP000006135}; RN [1] {ECO:0000313|EMBL:AEK56907.1, ECO:0000313|Proteomes:UP000006135} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SM-1 {ECO:0000313|EMBL:AEK56907.1, RC ECO:0000313|Proteomes:UP000006135}; RX PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006; RA You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B., RA Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.; RT "Unraveling the Acidithiobacillus caldus complete genome and its central RT metabolisms for carbon assimilation."; RL J. Genet. Genomics 38:243-252(2011). 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 --------------------------------------------------------------------------- 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; CP002573; AEK56907.1; -; Genomic_DNA. DR RefSeq; WP_014002203.1; NC_015850.1. DR EnsemblBacteria; AEK56907; AEK56907; Atc_0256. DR KEGG; acu:Atc_0256; -. DR HOGENOM; CLU_001114_6_0_6; -. DR KO; K03582; -. DR OMA; KQSIYRW; -. DR OrthoDB; 137860at2; -. DR BioCyc; ACAL990288:G1GZF-263-MONOMER; -. DR Proteomes; UP000006135; 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; 2. 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}; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000006135}. FT DOMAIN 1..468 FT /note="UvrD-like helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51198" FT DOMAIN 469..769 FT /note="UvrD-like helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51217" FT REGION 1..891 FT /note="DNA-binding and helicase activity, interacts with FT RecC" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT REGION 887..907 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 917..1185 FT /note="Nuclease activity, interacts with RecD and RecA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT COILED 717..737 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 1091 FT /note="For nuclease activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT METAL 968 FT /note="Magnesium; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT METAL 1078 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT METAL 1091 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" SQ SEQUENCE 1185 AA; 132829 MW; 33D61DFEBADF39E5 CRC64; MSRVLDPLSL PLQGSALIEA SAGTGKTYTI ATLYLRLLLG HGEPATLPRQ PREILVMTFT RAATEELRER IALRLYAAMT ALREGAPPAS GDALLQRLLR DYPDPATRAA AIIRLENAFN SVDEASIHTI DAWCHRVLRE HALATGHDPD AEILTDSAPL RIRAVQDFWR REIYPLQRAA PWWLQRTPDP ETLLEQVAGL PWLDPPLPAP RAAFHDWLEN AAAPLLKAGT ELKAQWSSTL RDTYGRWLRE LADRDPYPLN RKSLPPEKLQ GALQSLDQWC VEKEAAVPTA MATVAKLGSA LAECVKKGMH CPAPPSQAQF DTFLAALQQW QVDDEVLHGQ ALAQAAASMA ALYGEEKQRL RQLEFNDLSR ALWNGLRGPG GEALAEALRQ RFPVILIDEF QDSSARQYAI FERIYRPSEP WPDSLMLLIG DPKQSIYRFR GADLDSYLRA RADTAPRHYV LGTNYRSAEP LVGALNALYA RADERCPGGA FDYRGEGDDP LPYQAVAAAG RSQRWQLGGQ EGPAITFAQH PLALTKEEFL THFAEWTAAT IAQLLGDSTS GFVGADGKLR RVGAGDIAIL LRDRKEAAIM LSALHRRGLP AAFLSEKQSV YHSPEAEELR LWLFALLHPE DEAALRCALA LPLLGLTQHD LWRLDTDEGL WAQEVERLRE YARIWAHSGI LTTLHRRLHQ QATAARILAR PDGERRLGNL LHLGELLQRA SQHLEGREAL LEHLQREQDS EDNPADSHVL RLESDAHCIR IRTIHSAKGL QYPLVFLPFI AATRKDGNIP PWQVVTGDDQ STLSWQSPSA ELMDRERLRE DLRLLYVALT RAEYALWLGL AAGKTASTPL WWRSAVGRLL GADEGKTPDQ CLETWKRHPA CRVLAADTIP SAPAPRSAEP SEPRRTPPVY TARFERDWSI HSFSRLSQSL QTSVGPYPSP DRVDPGAQAA GQGWHTFPQG PGAGRFLHEL LQWLWRDGRW PEDWREDFLH RCDERGYAPW GPVLVHWFAV LRASPLGSLG TTFAELRGAR TEMPFWFPSQ HLPTNQLDTL CRRYLLPGRE RPILGEQNLH GLFHGFMDLV FAVDGRYYVL DYKSTRLGEN DAAYGDTAIG EDVLEHRYEL QAALYLLALH RHLRQRLGRQ YRTEQHLGGA WLWYLRACAT AGGGLLYLAA DPQLLDALDS AVGRS //