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Entry: A8AP32_CITK8
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ID   A8AP32_CITK8            Unreviewed;       608 AA.
AC   A8AP32;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   24-JAN-2024, entry version 92.
DE   RecName: Full=RecBCD enzyme subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
DE            EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01487};
DE   AltName: Full=Exonuclease V subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
DE            Short=ExoV subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
DE   AltName: Full=Helicase/nuclease RecBCD subunit RecD {ECO:0000256|HAMAP-Rule:MF_01487};
GN   Name=recD {ECO:0000256|HAMAP-Rule:MF_01487};
GN   OrderedLocusNames=CKO_04184 {ECO:0000313|EMBL:ABV15245.1};
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338 {ECO:0000313|EMBL:ABV15245.1, ECO:0000313|Proteomes:UP000008148};
RN   [1] {ECO:0000313|EMBL:ABV15245.1, ECO:0000313|Proteomes:UP000008148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696
RC   {ECO:0000313|Proteomes:UP000008148};
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC         Rule:MF_01487};
CC   -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC       to DNA-binding. {ECO:0000256|HAMAP-Rule:MF_01487}.
CC   -!- SIMILARITY: Belongs to the RecD family. {ECO:0000256|HAMAP-
CC       Rule:MF_01487}.
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DR   EMBL; CP000822; ABV15245.1; -; Genomic_DNA.
DR   RefSeq; WP_012134934.1; NC_009792.1.
DR   AlphaFoldDB; A8AP32; -.
DR   STRING; 290338.CKO_04184; -.
DR   GeneID; 45137806; -.
DR   KEGG; cko:CKO_04184; -.
DR   HOGENOM; CLU_007524_1_2_6; -.
DR   OMA; MIDLEMM; -.
DR   OrthoDB; 9803432at2; -.
DR   Proteomes; UP000008148; Chromosome.
DR   GO; GO:0009338; C:exodeoxyribonuclease V complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   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; 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   NCBIfam; TIGR01447; recD; 1.
DR   PANTHER; PTHR43788:SF6; DNA HELICASE B; 1.
DR   PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF13245; AAA_19; 1.
DR   Pfam; PF21185; RecD_N; 1.
DR   Pfam; PF13538; UvrD_C_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01487}; DNA damage {ECO:0000256|HAMAP-Rule:MF_01487};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01487};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01487}; Exonuclease {ECO:0000256|HAMAP-Rule:MF_01487};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01487};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01487};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01487};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01487}; Reference proteome {ECO:0000313|Proteomes:UP000008148}.
FT   DOMAIN          163..320
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         171..178
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01487"
SQ   SEQUENCE   608 AA;  66314 MW;  2D762CBC2BD21970 CRC64;
     MTIQKRLLEA VEQKLLRPLD AQFALAVAGQ DDPCVTLAVA LLSRDAGEGH VCMPLSRLAI
     TEESHPLLVS WFSERDVPED WASCLLASGA VSRGERPTPL ILHEDRLYLN RMWSNERTVA
     RFFSEVNQAI AVDEQQLART LDALFPPTDD VNWQKVAAAV ALTRRISVIS GGPGTGKTTT
     VAKLLAALIQ MADGERCRIR LAAPTGKAAA RLTESLGAAL RQLPLTDEQK KRIPDDASTL
     HRLLGAQPGS QRLRHHAGNP LHLDVLVVDE ASMIDLPMMS RLIEALPPHG RVIFLGDRDQ
     LASVEAGAVL GDICAWVNAG FTAGRAQQLS RLTGSPIPAG AGTEAASLRD SLCLLQKSYR
     FGHDSGIGQL AAAINCGDKA AMKTVFQQGF SDIEKRTLQS SEDYAAMLDE ALAGYGRYLA
     LVREGAEPGA IIQAFNEYQL LCALREGPFG VGGLNERIEQ VMLQKRKIQR HPHSRWYEGR
     PVMIARNDSA LGLFNGDIGI ALDRGQGLRV WFAMPDGSIK SVQPSRLPEH ETTWAMTVHK
     SQGSEFDHAA LILPSQRSPV VTRELVYTAV TRARRRLSLY ADERVLSGAI ATRTERRSGL
     SAFFNNGL
//
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