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Database: UniProt
Entry: N9NBG0_9GAMM
LinkDB: N9NBG0_9GAMM
Original site: N9NBG0_9GAMM 
ID   N9NBG0_9GAMM            Unreviewed;       590 AA.
AC   N9NBG0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
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   ORFNames=F899_00594 {ECO:0000313|EMBL:ENX02956.1};
OS   Acinetobacter sp. CIP 101934.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1144661 {ECO:0000313|EMBL:ENX02956.1, ECO:0000313|Proteomes:UP000018437};
RN   [1] {ECO:0000313|EMBL:ENX02956.1, ECO:0000313|Proteomes:UP000018437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 101934 {ECO:0000313|EMBL:ENX02956.1,
RC   ECO:0000313|Proteomes:UP000018437};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter sp. CIP 101934.";
RL   Submitted (FEB-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ENX02956.1}.
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DR   EMBL; APRQ01000023; ENX02956.1; -; Genomic_DNA.
DR   RefSeq; WP_005220753.1; NZ_KB850094.1.
DR   AlphaFoldDB; N9NBG0; -.
DR   PATRIC; fig|1144661.3.peg.567; -.
DR   HOGENOM; CLU_007524_1_1_6; -.
DR   Proteomes; UP000018437; Unassembled WGS sequence.
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   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   HAMAP; MF_01487; RecD; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006344; RecD.
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; 1.
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|HAMAP-Rule:MF_01487};
KW   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}.
FT   DOMAIN          505..551
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13538"
FT   BINDING         147..154
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01487"
SQ   SEQUENCE   590 AA;  66043 MW;  1C1DB360E56AFA67 CRC64;
     MENEQNHISQ LASPSMLWIE HICQPPFSSA NFGDEAKLLM HAVLEAMQNG NSCIDAAEDQ
     VALLHNLVRR GESDQHAIAP FIFQDQQLYL YRYWKLEHAI AAHVVRIKSQ QLKAVQLNEH
     HRSLLADPQQ QKALEMVASQ GLSIITGGPG TGKTYTLAHI IAVLNESLPD IRIAMAAPTG
     KAAQRMKEAL QNALSSPALA QFNLETLKQL QPVTLHRLLG LGITAQPRFH ARQPLPYEVI
     VVDEASMLDL SLAQMLLAAV PDGARLILLG DANQLASVDV GTVLADLQQV PALANNRINL
     MKTRRFSEGA RIGALAHFIQ KAHPDHDLLT EFEQQVVTAS ELQAIDLEQI EIDHLQLQYL
     PENLLLNDAQ PYYDQLMYGY QGYVQALKTG GGSQDFNRFV EQIIRHFDDY RILTAIRHGV
     LGLTRLNQQI EQRLLTATGQ IKQGDWYIGR PVMMTYNDYQ LGLSNGDIGI CFLREHLGQR
     QFEVYFPSLE KWVLATRLPK SIETAFALTI HKSQGSEFRH TAVVLDHKAS NLLSKELIYT
     AITRAKKAVT LLVDREAFIQ SLSLKTTRRS GLSKKIIEQC HNFSGNSETD
//
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