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Database: UniProt
Entry: O51578
LinkDB: O51578
Original site: O51578 
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   05-DEC-2018, entry version 117.
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};
GN   OrderedLocusNames=BB_0633;
OS   Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM
OS   4680).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680;
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.,
RA   Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D.,
RA   Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A.,
RA   Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K.,
RA   Roberts K.M., Hatch B., Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia
RT   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
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:0000255|HAMAP-Rule:MF_01485}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage (in the presence of ATP) in
CC         either 5'- to 3'- or 3'- to 5'-direction to yield 5'-
CC         phosphooligonucleotides.; EC=3.1.11.5;
CC         Evidence={ECO:0000255|HAMAP-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
CC       contribute to DNA-binding. Interacts with RecA.
CC       {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01485}.
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01485}.
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   ProteinModelPortal; O51578; -.
DR   STRING; 224326.BB_0633; -.
DR   PRIDE; O51578; -.
DR   EnsemblBacteria; AAC66981; AAC66981; BB_0633.
DR   GeneID; 1195485; -.
DR   KEGG; bbu:BB_0633; -.
DR   PATRIC; fig|224326.49.peg.1023; -.
DR   eggNOG; ENOG4107X59; Bacteria.
DR   eggNOG; COG1074; LUCA.
DR   KO; K03582; -.
DR   OMA; KQSIYRW; -.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; 3.90.320.10; -; 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; 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; Complete proteome; DNA damage; DNA repair; DNA-binding;
KW   Exonuclease; Helicase; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN         1   1169       RecBCD enzyme subunit RecB.
FT                                /FTId=PRO_0000102039.
FT   DOMAIN        1    436       UvrD-like helicase ATP-binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   DOMAIN      459    746       UvrD-like helicase C-terminal.
FT                                {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   NP_BIND      18     25       ATP. {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   REGION        1    843       DNA-binding and helicase activity,
FT                                interacts with RecC. {ECO:0000255|HAMAP-
FT                                Rule:MF_01485}.
FT   REGION      883   1169       Nuclease activity, interacts with RecD
FT                                and RecA. {ECO:0000255|HAMAP-
FT                                Rule:MF_01485}.
FT   ACT_SITE   1065   1065       For nuclease activity.
FT                                {ECO:0000250|UniProtKB:P08394}.
FT   METAL       939    939       Magnesium; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   METAL      1052   1052       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01485}.
FT   METAL      1065   1065       Magnesium. {ECO:0000255|HAMAP-
FT                                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
//
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