ID   RECD_BUCBP              Reviewed;         618 AA.
AC   Q89AB2;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=bbp_405;
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 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; AE016826; AAO27117.1; -; Genomic_DNA.
DR   RefSeq; WP_011091518.1; NC_004545.1.
DR   AlphaFoldDB; Q89AB2; -.
DR   SMR; Q89AB2; -.
DR   STRING; 224915.bbp_405; -.
DR   EnsemblBacteria; AAO27117; AAO27117; bbp_405.
DR   GeneID; 56470942; -.
DR   KEGG; bab:bbp_405; -.
DR   eggNOG; COG0507; Bacteria.
DR   HOGENOM; CLU_007524_1_2_6; -.
DR   OMA; MIDLEMM; -.
DR   OrthoDB; 961809at2; -.
DR   Proteomes; UP000000601; 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; 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   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..618
FT                   /note="RecBCD enzyme subunit RecD"
FT                   /id="PRO_0000087114"
FT   BINDING         174..181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01487"
SQ   SEQUENCE   618 AA;  71577 MW;  2DB3EA48C36C968F CRC64;
     MTITSILQKM VKLKIITSSN FYLSTMLFNK NTLATFLSIC VNHFTNHGHV CLPHVLIQHQ
     KIFFTNHIAL ITKLWEIAKI NTCGWIEQLL NSNTISNGSK NTPFIFYKNN FYINKFWLAE
     QKILKFISQK QNFKLINKNK IQKILKNIFN TNIDDTQKLA IILSIINNIT FIIGGPGTGK
     TTIILKILLV LIRLHKKKIN IKLTALTGKA ANRLSESIHE NIKKLNLTEH EKNIFNQKTT
     TLHNLLDLKP NKSFNYSCCK NKLYNLNLLI IDEASMIDIT IMDKLISSIP KTTKIIFLGD
     YNQLPSISGG NILKNICSYY QEGFSTTTNK FLKQLFPNRI TIKTIKKHQF SNINDKIIML
     KKSYRFKKKS DIFKISEMLT KNKINNIKTL YQNINNDVNF KQISSKTNYN NIIFEITNSY
     SKYWSALKQS LPFLKIINIF NNYKILCILK NGLFGITELN LAIEKEMKKI GWIKKVTIIN
     GQTWYFGKPI LILKNNEEMN LFNGECGLTL LDANKKLKVF FLPKNQEQIY SIPIHLVPEH
     QTNWTMTVHK SQGSEFSEVV LILPTIMTSI LTKELIYTAV TRSKKKLTIY SDENIFIKSL
     KKNIIRYSGL SIHQKIKF