ID   RECD_BUCAI              Reviewed;         602 AA.
AC   P57530;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=RecBCD enzyme subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487};
DE            EC=3.1.11.5 {ECO:0000255|HAMAP-Rule:MF_01487};
DE   AltName: Full=Exonuclease V subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487};
DE            Short=ExoV subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487};
DE   AltName: Full=Helicase/nuclease RecBCD subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487};
GN   Name=recD {ECO:0000255|HAMAP-Rule:MF_01487}; OrderedLocusNames=BU455;
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 has
CC       ssDNA-dependent ATPase and 5'-3' helicase activity. When added to pre-
CC       assembled RecBC greatly stimulates nuclease activity and augments
CC       holoenzyme processivity. Negatively regulates the RecA-loading ability
CC       of RecBCD. {ECO:0000255|HAMAP-Rule:MF_01487}.
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_01487};
CC   -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC       to DNA-binding. {ECO:0000255|HAMAP-Rule:MF_01487}.
CC   -!- SIMILARITY: Belongs to the RecD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01487}.
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DR   EMBL; BA000003; BAB13153.1; -; Genomic_DNA.
DR   RefSeq; NP_240267.1; NC_002528.1.
DR   RefSeq; WP_010896127.1; NC_002528.1.
DR   AlphaFoldDB; P57530; -.
DR   SMR; P57530; -.
DR   STRING; 107806.10039119; -.
DR   EnsemblBacteria; BAB13153; BAB13153; BAB13153.
DR   KEGG; buc:BU455; -.
DR   PATRIC; fig|107806.10.peg.465; -.
DR   eggNOG; COG0507; Bacteria.
DR   HOGENOM; CLU_007524_1_2_6; -.
DR   OMA; MIDLEMM; -.
DR   Proteomes; UP000001806; Chromosome.
DR   GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro.
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:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.1020; -; 1.
DR   Gene3D; 3.40.50.300; -; 3.
DR   HAMAP; MF_01487; RecD; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006344; RecD.
DR   InterPro; IPR041851; RecD_N.
DR   InterPro; IPR027785; UvrD-like_helicase_C.
DR   Pfam; PF13538; UvrD_C_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR01447; recD; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW   Hydrolase; Nuclease; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..602
FT                   /note="RecBCD enzyme subunit RecD"
FT                   /id="PRO_0000087112"
FT   BINDING         171..178
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01487"
SQ   SEQUENCE   602 AA;  69495 MW;  340FFAE9BB436059 CRC64;
     MLILLKKAVK LKIIRPIDFY FSQFIAQKNN IVMLVAACVS YESSRGYISL PIKYFEKHYF
     FSSSNEVFIK KILTLLEKKI NWPVELLKHA SIGNGGTSTP LVLHKKKIYL YKMWKSESNI
     FNYLYTKNKK NKINQKKCSK ILENLFPQKN MSFQKIAVAL TLINNITFII GGPGTGKTTT
     ILKIIIALIK SSKKSIKIQL SAPTGKATTH LNEILKNNIF DLYFSEKEKC SLPSTATTIH
     QLLGIQKISQ KSFFNKSNCL DLDVLIIDEI SMVDILMMEK ILSSISKNTK LIFIGDHNQL
     GPIESGSILR KICYYANDGY SFKSMISIEK LTQYKLCKKI NKKTTNFISD NICVLNKNYR
     FNKNSGIYTL SNAIFKKKTR IIESLFDNSI KNIFFYETNS SEQYKKMIKN ICLNYEDFWE
     KIYKKATMKE IIESFQNYQV LCILHDGLFG VNIINKKLEE NMYKKNIIKY FYIDGEEWYI
     GKPIMIINNN RALNVSNGNI GITNINKNGI LQVSFLKENN TINNIPVKIL RNYKTAWAIT
     VHKSQGSEFM NTALILPNFN SHILNKDTLY TGITRSRKIL SIFSDKKIFL NTIFKNTNKI
     LF