ID A0A095TUG9_9GAMM Unreviewed; 1201 AA. AC A0A095TUG9; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 03-MAY-2023, entry version 45. 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 ORFNames=Y5S_00510 {ECO:0000313|EMBL:KGD66038.1}; OS Alcanivorax nanhaiticus. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=1177154 {ECO:0000313|EMBL:KGD66038.1, ECO:0000313|Proteomes:UP000029444}; RN [1] {ECO:0000313|EMBL:KGD66038.1, ECO:0000313|Proteomes:UP000029444} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=19-m-6 {ECO:0000313|EMBL:KGD66038.1, RC ECO:0000313|Proteomes:UP000029444}; RA Lai Q., Shao Z.; RT "Genome Sequence of alkane-degrading Bacterium Alcanivorax sp. 19-m-6."; RL Submitted (SEP-2012) 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 -!- 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:KGD66038.1}. 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; ARXV01000002; KGD66038.1; -; Genomic_DNA. DR RefSeq; WP_035230205.1; NZ_ARXV01000002.1. DR AlphaFoldDB; A0A095TUG9; -. DR STRING; 1177154.Y5S_00510; -. DR EnsemblBacteria; KGD66038; KGD66038; Y5S_00510. DR PATRIC; fig|1177154.3.peg.519; -. DR eggNOG; COG1074; Bacteria. DR OrthoDB; 9810135at2; -. DR Proteomes; UP000029444; Unassembled WGS sequence. 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; 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: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; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF52980; Restriction endonuclease-like; 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}; 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|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|HAMAP-Rule:MF_01485}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01485}. FT DOMAIN 4..466 FT /note="UvrD-like helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51198" FT DOMAIN 467..766 FT /note="UvrD-like helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51217" FT REGION 1..869 FT /note="DNA-binding and helicase activity, interacts with FT RecC" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT REGION 918..1201 FT /note="Nuclease activity, interacts with RecD and RecA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT REGION 939..961 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 942..958 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1107 FT /note="For nuclease activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT BINDING 25..32 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560" FT BINDING 977 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT BINDING 1094 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" FT BINDING 1107 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485" SQ SEQUENCE 1201 AA; 134525 MW; EE504A67F6621486 CRC64; MSQTVAEQRP LPITFPLHGT RLIEASAGTG KTFTLAALYL RLVLGHGDDN GFSRPLLPPE ILVVTFTEAA TEELRERIRD RLAEAARIFS SPHAMASDPV LAELLTDYAD PEQRAHCGQR LDAAAQWMDE AAIYTIHGFC NRMLKQHAFD SGSLFSLELQ EDASDEQQLA ARDYWRNIIA KFPASAAQAL QAEGLNSPDT LLNEARPLFG LREADPNAIP ESVTAWLAAT GPLQENDQQA RATLANELPN FLDWINTAST EKWLNGNSYR TASLPAMKQT LKRYANGEQL KGKDYDTLAR FAHSGMKLTK KGQEHRPGFA CCDALDLMLE SRAQTQLPRT DLLAHTAAWI DQRVDRMRRQ SATMGFDDML SRLHDALQGS NGERLAQVIR EQFPVALIDE FQDTDPTQYG IFSALYQGQT QTGWFMIGDP KQAIYAFRGA DVFTYLKARR ATEGNHYTLD TNFRSTAAMV DAVNHLFGYS QKQFGDVFMM QDAIPFEAVK ANGRSDILLI DDQETAGVTL WVDERDAPIS AGHYRDEQAA RCASEIAHLL NGAEQGVTGF RKNDSFRPLH PNDIAILVRD RTEAKAIRDA LMERGVRSVY LSDQDSVFAQ PEASDLLLIL HACAQPESDR KVRSALACVA LEQPYTELDA LNQDEVRWEA MVEQFHGYRQ QWQQQGVLPM LRSLLLDFQV PARLSQSLDG ERSLTNLLHL AELLQQAATQ LDGEQALIRY LEDTVAEPGS SGKESILRLE SDDDRVKVIT IHKSKGLEYP LVYLPFICSF RPAEKSNPPL RYHDNDHLQV SLEPDDNVEF MADQERLAED LRLLYVALTR ACHTCTLGIA PYIKGRGKQN QLERSAIGRL LFGGPVANNE LMSKLQPAAN TAVTIMAAPD SSDEHYQPNS DVISLCEPRI PKVRQREPWW IASYSALKQV KETLAPADPR GDQLAEHQDE EADNEQEPRP GTIHAFPRGA APGTLLHDFL EAAANPGFSA TQEDPAEFEK MLEEKLQARG WQEHEGVIKQ WWKQTLSTAL PLANSSVALC DMESCIPELE FMLPAQQVNV ADMDTLIREH VHPKQHRPHL EADTLNGMLK GFIDLVFEHH GKYYVLDYKS NWLGVDNNAY TSEAMTNAVL EKRYEVQYVL YLLALHRLLK SRLPDYDPEQ HLGGAVYVFL RGLQGPATGT VFDRPATALI ETLDEMFGGE K //