ID   RECD_MYCTO              Reviewed;         575 AA.
AC   P9WHJ0; L0T4A3; P96919; Q7D9I4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 45.
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=MT0657;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(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 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK44881.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK44881.1; ALT_INIT; Genomic_DNA.
DR   PIR; B70612; B70612.
DR   RefSeq; WP_003900979.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHJ0; -.
DR   SMR; P9WHJ0; -.
DR   EnsemblBacteria; AAK44881; AAK44881; MT0657.
DR   KEGG; mtc:MT0657; -.
DR   PATRIC; fig|83331.31.peg.697; -.
DR   HOGENOM; CLU_007524_1_3_11; -.
DR   Proteomes; UP000001020; 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.
FT   CHAIN           1..575
FT                   /note="RecBCD enzyme subunit RecD"
FT                   /id="PRO_0000428178"
FT   BINDING         170..177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01487"
SQ   SEQUENCE   575 AA;  61747 MW;  A250708D407DE561 CRC64;
     MKLTDVDFAV EASGMVRAFN QAGVLDVSDV HVAQRLCALA GESDERVALA VAVAVRALRA
     GSVCVDLLSI ARVAGHDDLP WPDPADWLAA VRASPLLADP PVLHLYDDRL LYLDRYWREE
     EQVCADLLAL LTSRRPAGVP DLRRLFPTGF DEQRRAAEIA LSQGVTVLTG GPGTGKTTTV
     ARLLALVAEQ AELAGEPRPR IALAAPTGKA AARLAEAVRR EMAKLDATDR ARLGDLHAVT
     LHRLLGAKPG ARFRQDRQNR LPHNVIVVDE TSMVSLTLMA RLAEAVRPGA RLILVGDADQ
     LASVEAGAVL ADLVDGFSVR DDALVAQLRT SHRFGKVIGT LAEAIRAGDG DAVLGLLRSG
     EERIEFVDDE DPAPRLRAVL VPHALRLREA ALLGASDVAL ATLDEHRLLC AHRDGPTGVL
     HWNRRVQAWL AEETGQPPWT PWYAGRPLLV TANDYGLRVY NGDTGVVLAG PTGLRAVISG
     ASGPLDVATG RLGDVETMHA MTIHKSQGSQ VDEVTVLMPQ EDSRLLTREL LYTAVTRAKR
     KVRVVGSEAS VRAAIARRAV RASGLRMRLQ STGCG