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Database: UniProt
Entry: Q89AB3
LinkDB: Q89AB3
Original site: Q89AB3 
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   05-DEC-2018, entry version 105.
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=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
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; AE016826; AAO27116.1; -; Genomic_DNA.
DR   RefSeq; WP_011091517.1; NC_004545.1.
DR   ProteinModelPortal; Q89AB3; -.
DR   STRING; 224915.bbp404; -.
DR   PRIDE; Q89AB3; -.
DR   EnsemblBacteria; AAO27116; AAO27116; bbp_404.
DR   KEGG; bab:bbp_404; -.
DR   eggNOG; ENOG4107QKA; Bacteria.
DR   eggNOG; COG1074; LUCA.
DR   KO; K03582; -.
DR   OMA; KQSIYRW; -.
DR   OrthoDB; POG091H02P3; -.
DR   BioCyc; BAPH224915:G1G09-407-MONOMER; -.
DR   Proteomes; UP000000601; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; 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; 3.90.320.10; -; 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; 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; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 2.
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   1180       RecBCD enzyme subunit RecB.
FT                                /FTId=PRO_0000102042.
FT   DOMAIN        3    448       UvrD-like helicase ATP-binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   DOMAIN      478    745       UvrD-like helicase C-terminal.
FT                                {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   NP_BIND      24     31       ATP. {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   REGION        1    896       DNA-binding and helicase activity,
FT                                interacts with RecC. {ECO:0000255|HAMAP-
FT                                Rule:MF_01485}.
FT   REGION      905   1180       Nuclease activity, interacts with RecD
FT                                and RecA. {ECO:0000255|HAMAP-
FT                                Rule:MF_01485}.
FT   ACT_SITE   1088   1088       For nuclease activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   METAL       964    964       Magnesium; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01485}.
FT   METAL      1075   1075       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01485}.
FT   METAL      1088   1088       Magnesium. {ECO:0000255|HAMAP-
FT                                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
//
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