ID K9DC80_9BURK Unreviewed; 1220 AA.
AC K9DC80;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 60.
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=HMPREF9710_02782 {ECO:0000313|EMBL:EKU81828.1};
OS Massilia timonae CCUG 45783.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=883126 {ECO:0000313|EMBL:EKU81828.1, ECO:0000313|Proteomes:UP000009874};
RN [1] {ECO:0000313|EMBL:EKU81828.1, ECO:0000313|Proteomes:UP000009874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 45783 {ECO:0000313|EMBL:EKU81828.1,
RC ECO:0000313|Proteomes:UP000009874};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Massilia timonae CCUG 45783.";
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:EKU81828.1}.
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DR EMBL; AGZI01000035; EKU81828.1; -; Genomic_DNA.
DR RefSeq; WP_005667325.1; NZ_JH992923.1.
DR AlphaFoldDB; K9DC80; -.
DR STRING; 47229.LO55_3471; -.
DR PATRIC; fig|883126.3.peg.2804; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_6_0_4; -.
DR OrthoDB; 5905204at2; -.
DR Proteomes; UP000009874; 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 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; PF12705; PDDEXK_1; 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}; Reference proteome {ECO:0000313|Proteomes:UP000009874}.
FT DOMAIN 1..467
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 498..776
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..906
FT /note="DNA-binding and helicase activity, interacts with
FT RecC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT REGION 934..1220
FT /note="Nuclease activity, interacts with RecD and RecA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT ACT_SITE 1120
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 994
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"
FT BINDING 1120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
SQ SEQUENCE 1220 AA; 136352 MW; FAA533D272F66F9E CRC64;
MSSKLEAIRF PLHGSRLIEA SAGTGKTWTI AALYVRLVLG HGGDDAFVRP LLPSEILVMT
FTRAATRELS NRVRERLVQA AAYFRGEAHE QDAYLDELAE AYAPGSERSI AAHRLMLAAE
TMDEAAIFTI DAWCQRMLRE HAFDSGSLFD EELVSDERML FEDAAHDYWR QHVYPLGAQN
LAIVLDTWSD VEALKGSVRE LVQRGPLLGE VAREPLGKQV ARLAQAQREE LARLKHGWVE
RADAMERWIA GHRERAPKCF NGNKMRADSL VKWFEALRAW ATDPARHMPD LSDTAWKRLT
PDGIVDAFSK DFSAEVPDCF DGTAALQEAL GAIDPIAHAL LRHAAGHIGA RMQELKRRNR
QFGFADMLER LKLALEGENG AALRERIVQQ YPVAMVDEFQ DTSPDQYRIF DLLYRVGAND
PQQGLFLIGD PKQSIYGFRG ADIHSYLSAR RATTGRHYQL DTNYRSTAAL VGAVNALFLH
AEGGDGRTGH AQAAFRFRRG DDNPLPFEAV KARGHRERLV GVESDGEIEA MSVCTTCDDL
KAEDYRSFFA HHCAEHIVRL LNDERVGFRD EQDGGFRRLM PADIAILVRD RREAAAVRQA
LVRRKVASVY LSDKDSVVES EEAADMLRWL YAVANPLDGA LARAAFATRT AGLPMGELAR
LSSDELAWER RVEQLKALHG AWQRRGVLAM LRTFIHELGL PARLLGEPGG ERRLTNLLHL
AELLQEASAQ LEGEQALIRW FAEQIEGLGA GGDERVLRLE SDAELVKVVT VHKSKGLEYP
LVYLPFAVTA RATNRRNRAF FEYVDDAGSR RLDLALSDEA LEAVDRARIE EDLRLLYVAL
TRARHFLWLG AAAVAGTRKG ENRLHESALG YLLAGGAPIP ADGLRARFEA VAGAGGGIAL
RELEREDGVT MLARQDARPA LLDAPVYRAD FEKDWSIGSF TSLTRHAVAP PPTPMRAQEQ
TLLEEAPQAP LPPRIDDVAW HRFPRGSVPG NFMHEQLEWL AREGFDCLDQ PHCETRLVQR
IERAGWSNRL EDALTWLRAI VDTPLPPLGA ALRALQGVLP EMEFWFPSER LALPALDALC
RAHLLNGIER PVLPERDLHG MLKGFADLVF EHEGRYWVLD YKTNALGPND AAYSQAAMEA
GMAEHRYEIQ GSIYLLALHR LLRARLGEAY EPEVQLGGAI FMFLRGIANP DTRGCCVLAP
DLELLDKLER LLDKEKHGQD
//