RECB_BORBU
ID RECB_BORBU Reviewed; 1169 AA.
AC O51578;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=RecBCD enzyme subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
DE EC=3.1.11.5 {ECO:0000255|HAMAP-Rule:MF_01485};
DE AltName: Full=Exonuclease V subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
DE Short=ExoV subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
DE AltName: Full=Helicase/nuclease RecBCD subunit RecB {ECO:0000255|HAMAP-Rule:MF_01485};
GN Name=recB {ECO:0000255|HAMAP-Rule:MF_01485}; OrderedLocusNames=BB_0633;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
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:0000255|HAMAP-Rule:MF_01485}.
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:0000255|HAMAP-
CC Rule:MF_01485};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01485};
CC -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC to DNA-binding. Interacts with RecA. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01485}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000255|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; AE000783; AAC66981.1; -; Genomic_DNA.
DR PIR; H70178; H70178.
DR RefSeq; NP_212767.1; NC_001318.1.
DR RefSeq; WP_010889786.1; NC_001318.1.
DR AlphaFoldDB; O51578; -.
DR SMR; O51578; -.
DR STRING; 224326.BB_0633; -.
DR PRIDE; O51578; -.
DR EnsemblBacteria; AAC66981; AAC66981; BB_0633.
DR KEGG; bbu:BB_0633; -.
DR PATRIC; fig|224326.49.peg.1023; -.
DR HOGENOM; CLU_008504_0_0_12; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 3.
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; 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; PTHR11070; 2.
DR PANTHER; PTHR11070:SF23; PTHR11070:SF23; 2.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
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; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1169
FT /note="RecBCD enzyme subunit RecB"
FT /id="PRO_0000102039"
FT DOMAIN 1..436
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT DOMAIN 459..746
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT REGION 1..843
FT /note="DNA-binding and helicase activity, interacts with
FT RecC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT REGION 883..1169
FT /note="Nuclease activity, interacts with RecD and RecA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT ACT_SITE 1065
FT /note="For nuclease activity"
FT /evidence="ECO:0000250|UniProtKB:P08394"
FT BINDING 18..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 939
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 1052
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 1065
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
SQ SEQUENCE 1169 AA; 137829 MW; B61D63C1C959B91F CRC64;
MNKILEKIQN NTTILIEASA GTGKTHILEN VVINLIKTKL YSINEILVLT FTKKATEEMH
TRILKVIENA YSNSKTNEIL KEAYEQSKKL FISTINKFAL HALNNFQIET ENYSKYKPKE
KFSKEIDEIV YDFLRKSDSL IQALDIKDYE LKVFKSDAKK TEEIVLKIKK AYERDTTQEL
GDWLKTQTAF ENILLKKEEL IKDYNKIIED LDKMTKDEIL SFYNKHIQTG KLEIEYSKEN
DIFKIAETLL KNKFFSTLIE KETKKNSKLS PKELKIKNDL ICLGINIKHE KYKSEDNRNK
NRNNLKQYVI LKVEYKILKY IEKELKKTIK STNTIDQNYI ISNLKNYLKS EDKKLLNAIK
NRYKIILIDE AQDLSLIQIE IFKILKTAGI KLIFIADPKQ IIYSFRKADI SFYNKEIKNK
INTDARIVLK INHRSSKKLI GPLNKIFNNI YNNAIADEIE KIDFTNSLPN QKNDNNKIVI
NGQEIEGINI ITTNTESEED IYQKTALTIK YLLAYGKIAE NNKIRNIKMQ DIKVLCRGKN
EINLIDKALK KEQIQTNKTQ EKFLKTKEFS EIFYIIKCLD RKQSFKTLNY ILSSKILNVP
WNLQRILIKQ DKICLIEEFI ENIIVLLEKN EITLINAINK ITFEKNLWIK IANITKDQKI
IEWAKNKINY KGLLIKEGKL ENLKTYETTL EIISKIYHKE QNIQSLISTL ESLIINEEPE
EIEEKINNIN NDNESIELMT IHKSKGLGMN IVFLLNTTPI ENSNFFSKKN QFYKFYQDGK
IEYDFFKLEE NKKYARLKIL SEEKNIFYVG ATRAKFALFI IKINSITSKL LEIAKIFTID
DIKHDFNIHE FIGQKRFNKK KYNTNVNTKL IPPKPIIKNM FKKEYTSSFS SLTAQAHHKE
FYENYDFKNI NYEKETELDY EPGLEETLPK GKDIGNILHA AMEEIIFSTA KDTFDNFKKN
NIEIIEKQIQ KINSNLNTIE IQNSLAKMIY NILTYNIRAI NTRLCDIEEL QKEMEFLIKI
NPEFQKQKYL FDKHFEDLHI KLSDGYLKGI VDLIFKANNK IYILDYKTNY LGKNKEDYNI
TNLENTIKKE YYDLQYKIYA LGIKKILFKN KKEYNQKFGG IIYLFTRAFE DNIECLKSKF
ENGIYFNLPK FNDVDLDKII LELGIKRHL
