ID RECD_MYCTU Reviewed; 575 AA.
AC P9WHJ1; L0T4A3; P96919; Q7D9I4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=RecBCD enzyme subunit RecD {ECO:0000255|HAMAP-Rule:MF_01487};
DE EC=5.6.2.3 {ECO:0000255|HAMAP-Rule:MF_01487};
DE AltName: Full=DNA 5'-3' helicase subunit RecB {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=Rv0629c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12657046; DOI=10.1046/j.1365-2958.2003.03425.x;
RA Sassetti C.M., Boyd D.H., Rubin E.J.;
RT "Genes required for mycobacterial growth defined by high density
RT mutagenesis.";
RL Mol. Microbiol. 48:77-84(2003).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011445;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 Holoenzyme degrades any linearized DNA that is unable to undergo
CC homologous recombination. In the holoenzyme this subunit has ssDNA-
CC dependent ATPase and 5'-3' helicase activity. When added to pre-
CC assembled RecBC greatly stimulates nuclease activity and augments
CC holoenzyme processivity. Unlike the case in E.coli, suppresses RecA-
CC dependent homologous recombination, is instead required for single-
CC strand annealing pathway repair of DSB. {ECO:0000250|UniProtKB:A0QS28}.
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=Couples ATP hydrolysis with the unwinding of duplex DNA at the
CC replication fork by translocating in the 5'-3' direction. This
CC creates two antiparallel DNA single strands (ssDNA). The leading
CC ssDNA polymer is the template for DNA polymerase III holoenzyme which
CC synthesizes a continuous strand.; EC=5.6.2.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01487};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.3;
CC Evidence={ECO:0000255|HAMAP-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 -!- DISRUPTION PHENOTYPE: Not essential for growth.
CC {ECO:0000269|PubMed:12657046}.
CC -!- MISCELLANEOUS: In the RecBCD complex, RecB has a slow 3'-5' helicase,
CC an exonuclease activity and loads RecA onto ssDNA, RecD has a fast 5'-
CC 3' helicase activity, while RecC stimulates the ATPase and processivity
CC of the RecB helicase and contributes to recognition of the Chi site.
CC {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; AL123456; CCP43370.1; -; Genomic_DNA.
DR PIR; B70612; B70612.
DR RefSeq; NP_215143.1; NC_000962.3.
DR RefSeq; WP_003900979.1; NZ_NVQJ01000033.1.
DR AlphaFoldDB; P9WHJ1; -.
DR SMR; P9WHJ1; -.
DR STRING; 83332.Rv0629c; -.
DR PaxDb; 83332-Rv0629c; -.
DR DNASU; 887999; -.
DR GeneID; 887999; -.
DR KEGG; mtu:Rv0629c; -.
DR TubercuList; Rv0629c; -.
DR eggNOG; COG0507; Bacteria.
DR InParanoid; P9WHJ1; -.
DR OrthoDB; 9763659at2; -.
DR PhylomeDB; P9WHJ1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0009338; C:exodeoxyribonuclease V complex; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; 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:0017116; F:single-stranded DNA helicase activity; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR CDD; cd17933; DEXSc_RecD-like; 1.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR Gene3D; 1.10.10.1020; RecBCD complex, subunit RecD, N-terminal domain; 1.
DR HAMAP; MF_01487; RecD; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006344; RecD.
DR InterPro; IPR041851; RecD_N_sf.
DR InterPro; IPR027785; UvrD-like_helicase_C.
DR NCBIfam; TIGR01447; recD; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43788:SF6; RECBCD ENZYME SUBUNIT RECD; 1.
DR Pfam; PF13245; AAA_19; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Isomerase; Nuclease; Nucleotide-binding; Reference proteome.
FT CHAIN 1..575
FT /note="RecBCD enzyme subunit RecD"
FT /id="PRO_0000390680"
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
//
