ID A0A095TUG9_9GAMM Unreviewed; 1201 AA. AC A0A095TUG9; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 15-FEB-2017, entry version 15. 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; Proteobacteria; 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- RT 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 CC highly rapid and processive ATP-dependent bidirectional helicase CC activity. Unwinds dsDNA until it encounters a Chi (crossover CC hotspot instigator) sequence from the 3' direction. Cuts ssDNA a CC few nucleotides 3' to the Chi site. The properties and activities CC of the enzyme are changed at Chi. The Chi-altered holoenzyme CC produces a long 3'-ssDNA overhang and facilitates RecA-binding to CC the ssDNA for homologous DNA recombination and repair. Holoenzyme CC degrades any linearized DNA that is unable to undergo homologous CC recombination. In the holoenzyme this subunit contributes ATPase, CC 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA. CC {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage (in the presence of CC ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'- CC phosphooligonucleotides. {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01485}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01485}; CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits CC contribute to DNA-binding. Interacts with RecA. CC {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- DOMAIN: The C-terminal domain has nuclease activity and interacts CC with RecD. It interacts with RecA, facilitating its loading onto CC ssDNA. {ECO:0000256|HAMAP-Rule:MF_01485}. CC -!- DOMAIN: The N-terminal DNA-binding domain is a ssDNA-dependent CC ATPase and has ATP-dependent 3'-5' helicase function. This domain CC interacts 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:SAAS00597767}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblBacteria; KGD66038; KGD66038; Y5S_00510. DR Proteomes; UP000029444; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 5. 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; IPR004586; RecB. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR014016; UvrD-like_ATP-bd. DR PANTHER; PTHR11070; PTHR11070; 1. DR Pfam; PF00580; UvrD-helicase; 1. DR Pfam; PF13361; UvrD_C; 2. DR SUPFAM; SSF52540; SSF52540; 4. 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, ECO:0000256|PROSITE- KW ProRule:PRU00560, ECO:0000256|SAAS:SAAS00553698}; KW Complete proteome {ECO:0000313|Proteomes:UP000029444}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00440913}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00440586}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00621705}; KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|SAAS:SAAS00440824}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000256|PROSITE- KW ProRule:PRU00560, ECO:0000256|SAAS:SAAS00493105}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000256|PROSITE- KW ProRule:PRU00560, ECO:0000256|SAAS:SAAS00553587}; 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 ECO:0000256|SAAS:SAAS00440810}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01485, KW ECO:0000256|PROSITE-ProRule:PRU00560, ECO:0000256|SAAS:SAAS00553576}. FT DOMAIN 4 466 UvrD-like helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51198}. FT DOMAIN 467 766 UvrD-like helicase C-terminal. FT {ECO:0000259|PROSITE:PS51217}. FT NP_BIND 25 32 ATP. {ECO:0000256|PROSITE-ProRule: FT PRU00560}. FT REGION 1 870 DNA-binding and helicase activity, FT interacts with RecC. {ECO:0000256|HAMAP- FT Rule:MF_01485}. FT REGION 918 1201 Nuclease activity, interacts with RecD FT and RecA. {ECO:0000256|HAMAP-Rule: FT MF_01485}. FT ACT_SITE 1107 1107 For nuclease activity. FT {ECO:0000256|HAMAP-Rule:MF_01485}. FT METAL 977 977 Magnesium; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01485}. FT METAL 1094 1094 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01485}. FT METAL 1107 1107 Magnesium. {ECO:0000256|HAMAP-Rule: FT 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 //