RECB_BUCAI
ID RECB_BUCAI Reviewed; 1174 AA.
AC P57529;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, 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=BU454;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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; BA000003; BAB13152.1; -; Genomic_DNA.
DR RefSeq; NP_240266.1; NC_002528.1.
DR RefSeq; WP_010896126.1; NC_002528.1.
DR AlphaFoldDB; P57529; -.
DR SMR; P57529; -.
DR STRING; 107806.10039118; -.
DR EnsemblBacteria; BAB13152; BAB13152; BAB13152.
DR KEGG; buc:BU454; -.
DR PATRIC; fig|107806.10.peg.464; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_6_0_6; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000001806; 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..1174
FT /note="RecBCD enzyme subunit RecB"
FT /id="PRO_0000102040"
FT DOMAIN 4..449
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT DOMAIN 479..745
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT REGION 1..891
FT /note="DNA-binding and helicase activity, interacts with
FT RecC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT REGION 900..1174
FT /note="Nuclease activity, interacts with RecD and RecA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT ACT_SITE 1081
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 957
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 1068
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 1081
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
SQ SEQUENCE 1174 AA; 139038 MW; 668FE1336F1F190A CRC64;
MKIDSLKEKL NIFKIPLNGI KLIEASAGTG KTFTIVLLYL RLLLGIGEKK IYKKKLLVHE
ILVVTFTNKA KEELYIRIKD GIQNMYLTCI NKTTSDSSFQ FFFKEIHDIK EAIYVLKRAQ
NDMNSSSIYT IHSFCQHILQ LHTFHFNDIF EEKIIENEDN LYLQATQDFW RRFFYTLPED
IIKIIYQDYK SPDHLLKTIK PFFYIKSINF PTKILNNKKL IMYHEENIKK IIFFKEMWLI
YHKIIQKTIN DLEINKKIYS KFNLIKWINK ITEWAKSETK DYTIPSILKY FTKKNIEKNT
INNTCSKYII FEESEKILKK KFSLKNVIII YAVKKIHQFL LKEKKKKSLI GFNDLLSILL
KTIKKEKFLK DLIIKKYPAA FIDEFQDTDI QQYKIFNLLY KKNKTTVLFL IGDPKQAIYS
FRGADIFSYL YAKSKIKKYY YLDTNWRSSI NICKSINFLF SQNINPFIFK NIPYIPVVPS
SKNLKMNFTI NDVAQTPISF FLQEEKEVSI DDYQVWISKQ CANEISFWLT CAKTGKAKIT
TKNGEKILTA NDIAILVRNR KEADLIQDEL EKLNIISIYS SNKNSVFQTL DAQELLWILE
SILEPENEIL LQQSMASHIL KKLSLVVENK TISNKNSYFI IEKLYEYHDI WEKIGVFQMI
KIMILEYQKN SFCTEINENH IKNLNFLHIG ELLQEQFQFF HKKISLIRWF QKKISTKTQP
EYNESIKCFD ESPSIKIITI HKSKGLEYPI VWIPFSIDFK KSTLAIYHDQ KSLKTFFDEN
YSNKFLKIAD EERLAEDIRF LYVALTRSIL HCSIGLACLI KKIIKNRNNS DIHQSGLGFT
IQGGKTMNYE GLLEKLKKLS INNFIEVKNN TDNFSFSRKP QTISLICKNK FLNKKNIRNT
WSITSFSQLN KINKLSKHHQ KEVALKELCI KNQEKKNQSL LTIHNFPKGK KTGLMIHYIL
KNLHVLKNKN SNWFSCILEK YNIHIKWTSV LIYWIKNIIN TPLNDEKIIL SRIDEKSSIR
ELEFFFPIKN MLYSTELNKI IQSINPTSIT SPQLSFNPVK GMLTGFVDLV FIWKKKYYIL
DYKSNWLGKN NNFYSSIHIN KEIVKKRYHL QYQIYTIAIH KYLQKKLKNY NYKDDFGGVF
YFFLRAIDCP KKNNGIFYTM PNYSLIKKTM TLIS
