RECB_BUCAP
ID RECB_BUCAP Reviewed; 1179 AA.
AC Q8K9A9;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=BUsg_439;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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; AE013218; AAM67982.1; -; Genomic_DNA.
DR RefSeq; WP_011053949.1; NC_004061.1.
DR AlphaFoldDB; Q8K9A9; -.
DR SMR; Q8K9A9; -.
DR STRING; 198804.BUsg_439; -.
DR EnsemblBacteria; AAM67982; AAM67982; BUsg_439.
DR KEGG; bas:BUsg_439; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_6_0_6; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
DR Proteomes; UP000000416; 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.
FT CHAIN 1..1179
FT /note="RecBCD enzyme subunit RecB"
FT /id="PRO_0000102041"
FT DOMAIN 18..459
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT DOMAIN 485..755
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT REGION 1..899
FT /note="DNA-binding and helicase activity, interacts with
FT RecC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT REGION 910..1179
FT /note="Nuclease activity, interacts with RecD and RecA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT ACT_SITE 1086
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 962
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 1073
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
FT BINDING 1086
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01485"
SQ SEQUENCE 1179 AA; 141041 MW; FECEC60F11420937 CRC64;
MVYSDTKTSK KIKKYKINIM KKKLNIFQIP LKGIHLIEAS AGTGKTSTIA FLYLRLLLGL
EKNKENIRKL SVKEILVVTF TNAAKEELYI RIKKSIKELH LSCIKKKSKD PIFQSFLTKI
KNFDEAIHIL EDAKININNA AIYTIHGFCQ DVLENNTLIS NREIIENESF LYLQATQDFW
RYFFYNLPKK IIKIIYEEYR SPEDLLREIK PILKVNSSIN FKKKFDKKET LITFHEKIIN
KINIFKQKWL NYNLIILKII NQLKVNKKIY SNFNILKWKK KITEWAESET KNYKMPICLK
YFSETSIEKN IKNYNFKKHI FFEEIDKILK KNFSLKNIIL FYAIKNIPKF VKREKEKKLL
LGFNDLLKIL LKNIKKEESL REIIIKQYPV ALIDEFQDTN IQQYQIFNTL YKNKKTALFL
VGDPKQSIYS FRGADIFSYL HAKFKIKNYY YLDTNWRSSK NICKAINYLF SKNKNPFYFK
NIPFEPILSS SKNLNMKFKI KEKNQTAISF FFQKKEEVNI EEYRDWIAKQ CANEISYWLT
CSKKGEAIIS DGSQERILTE KDIVILVRNR TEAQIIKESL KKVNILSKYS SPYESVFKTF
DALELLSILK SILDPTDINL LKKSILTHIL NKIAFQKIKE NSKTKISHFL IQKLYEYNDK
WKTIGIFYTI KTMILEYQKY ANNFEMYKNQ QRNINFLHIA ELLQEKSQNC YKENSLMRWF
EKKILEKNNI SENEYIKNFA ESKIIRIITI HKSKGLEYPI VWIPFIVDFN VSKSYFYHEK
KTLKIFFDNN KSSETLKKSD EERLAEDLRF LYVALTRSIY HCSIGISYLV KKRKKNKKSS
DIHKSSLGYI IQNGKCMNYK ELLYELKILN KKLYIEVKYQ AMNCKSLTIK KDDLYILSQP
QFLLKEIKLY SQITSFTKIK QENKHFNNIQ YNNIESYFFK EKDKKKTIHN FPHGNKAGIF
IHYILKTIKF NNTFNIDWFY TILKKYEFSE KWAKTLMFWI NNILNFKINN LNITLSSLKK
TQYIKELEFF LPIKNTLYCE DLNQIIQSID LISSISQKIF FNPVIGILKG FIDLVFIFNK
KYYILDYKCN YLGNNDNCYS SKNIKKEIIK NRYDIQYQLY TLALHQYLKK KVKQYHYKTH
FGGVFYLFLR GINVKDSIFY ILPDYLLIKK LTKLILQKK
