RECB_BUCBP
ID RECB_BUCBP Reviewed; 1180 AA.
AC Q89AB3;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=bbp_404;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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}.
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DR EMBL; AE016826; AAO27116.1; -; Genomic_DNA.
DR RefSeq; WP_011091517.1; NC_004545.1.
DR AlphaFoldDB; Q89AB3; -.
DR SMR; Q89AB3; -.
DR STRING; 224915.bbp_404; -.
DR PRIDE; Q89AB3; -.
DR EnsemblBacteria; AAO27116; AAO27116; bbp_404.
DR GeneID; 56470941; -.
DR KEGG; bab:bbp_404; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_6_0_6; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
DR Proteomes; UP000000601; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 Gene3D; 3.40.50.300; -; 2.
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; 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; 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..1180
FT /note="RecBCD enzyme subunit RecB"
FT /id="PRO_0000102042"
FT DOMAIN 3..448
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT DOMAIN 478..745
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT REGION 1..896
FT /note="DNA-binding and helicase activity, interacts with
FT RecC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT REGION 905..1180
FT /note="Nuclease activity, interacts with RecD and RecA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT ACT_SITE 1088
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 24..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 964
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 1075
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 1088
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
SQ SEQUENCE 1180 AA; 139436 MW; 55E1C0F9F389FAE9 CRC64;
MITTIPKSIN VTTIPLSGKI LIEASAGTGK TFSLTILYIR LLLGITNHVK YKKGLLIKEI
LVVTFTEHTR AELEIRIKTY IKIFKTACIK KYSNNYVLSK LLSKITDFPK TIDILSKAEN
SIHELSIYTI HGFCYKILKL NKFNSELMLQ NKILKHTYPL YLKISIKFWK YYFAFLSLDI
TSILLEYFNN PKTLLKEILP LLNKTQLISK LTKTKRKNIV QEYYILIKKI KLFKQKWANY
SHLIHSEIIK TNVNKRIYTK SNLKRWINNI TAWATQKQTK NFFIPSELKY FRYSFIIKKT
TSEKILDDKF FKFIDTFLDS KFSLKEIFII DASLEIKAMF MQEKIKNRYF EYDDLITFCW
NMVNKNNFNI SQTILKKYPV ALIDEFQDTN NKQYNIFKKI YKKENLLILI SDPKQAIYSF
SGADITSYLQ AKSNIKNQYF LDTNWRSSPK IINSINLLFS RLKNPFLTKN ITFYPVKSSR
INKTTKFEVN GKNQPALRFL LNKNKNISIN EYKEWISITT AKYISYWISS GIKGNATITI
SNKVRTVNFS DIAIIVRNNL EAKTIQLELT KLNIQSLYLT SKNNIFQSKE ILEILWILQA
ILNPNIERLL KRAMSTNIMS KNTKEIISIP NNHSYWIKLS QEFNQYLIFW NNYGILYVIQ
QLIINYNISN NNNLLHNFSP NIKNILYIGE LLEEKSITIK NKFLLINWLK KNITQDFYLT
KPKYIKPNYE KNNYIKIVSI HKSKGLEYPI TIIPFATITF NKTVSTVEKI CFNLNNTKIK
KQKTLKIEKH KFSEDIRLLY VALTRSIIHC SIGISLAQTI TQKKKIQKEK SKFKINVLRY
IIQSGKNHIS TKKLYTELSI LKKNKNIEII SEIPNIIKKN FQIPTLNTNS QSLMHYQVSR
KFNYNYNFTS YSQLKKNIKP STMYSTLNTK KLFELNVKKK HCFENKILTP HTFPSGKIYG
TLLHKILKNI SFHKSINSNW LLKKLSEYNL DKRWCLILKN WMYSILYKNL DKNYNLRLSK
LDSKNYIKEL KFLLPIKKKL TALKLNNIFQ THQCSSLENK LCFHPIQGIL SGSIDLVFLW
KTKYFLVDYK SNWIGNSNQS YSQQNIKKII KKHHYNFQLQ LYSLVLHRYL KQHIKNYSFY
NHFGGTYILF IRSINEIPSQ NGIFYSIPNI EIIKKLEQIF
