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Database: UniProt
Entry: K9DC80_9BURK
LinkDB: K9DC80_9BURK
Original site: K9DC80_9BURK 
ID   K9DC80_9BURK            Unreviewed;      1220 AA.
AC   K9DC80;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=RecBCD enzyme subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
DE            EC=3.1.11.5 {ECO:0000256|HAMAP-Rule:MF_01485};
DE   AltName: Full=Exonuclease V subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
DE            Short=ExoV subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
DE   AltName: Full=Helicase/nuclease RecBCD subunit RecB {ECO:0000256|HAMAP-Rule:MF_01485};
GN   Name=recB {ECO:0000256|HAMAP-Rule:MF_01485};
GN   ORFNames=HMPREF9710_02782 {ECO:0000313|EMBL:EKU81828.1};
OS   Massilia timonae CCUG 45783.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=883126 {ECO:0000313|EMBL:EKU81828.1, ECO:0000313|Proteomes:UP000009874};
RN   [1] {ECO:0000313|EMBL:EKU81828.1, ECO:0000313|Proteomes:UP000009874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 45783 {ECO:0000313|EMBL:EKU81828.1,
RC   ECO:0000313|Proteomes:UP000009874};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Massilia timonae CCUG 45783.";
RL   Submitted (SEP-2012) 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
CC       contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA
CC       onto ssDNA. {ECO:0000256|HAMAP-Rule:MF_01485}.
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=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618};
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_01485};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01485};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01485};
CC   -!- SUBUNIT: Heterotrimer of RecB, RecC and RecD. All subunits contribute
CC       to DNA-binding. Interacts with RecA. {ECO:0000256|HAMAP-Rule:MF_01485}.
CC   -!- DOMAIN: The C-terminal domain has nuclease activity and interacts with
CC       RecD. It interacts with RecA, facilitating its loading onto ssDNA.
CC       {ECO:0000256|HAMAP-Rule:MF_01485}.
CC   -!- DOMAIN: The N-terminal DNA-binding domain is a ssDNA-dependent ATPase
CC       and has ATP-dependent 3'-5' helicase function. This domain interacts
CC       with RecC. {ECO:0000256|HAMAP-Rule:MF_01485}.
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01485}.
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:EKU81828.1}.
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DR   EMBL; AGZI01000035; EKU81828.1; -; Genomic_DNA.
DR   RefSeq; WP_005667325.1; NZ_JH992923.1.
DR   AlphaFoldDB; K9DC80; -.
DR   STRING; 47229.LO55_3471; -.
DR   PATRIC; fig|883126.3.peg.2804; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_6_0_4; -.
DR   OrthoDB; 5905204at2; -.
DR   Proteomes; UP000009874; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR   CDD; cd22352; RecB_C-like; 1.
DR   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.3170.10; Recbcd, chain B, domain 2; 1.
DR   HAMAP; MF_01485; RecB; 1.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   InterPro; IPR004586; RecB.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   NCBIfam; TIGR00609; recB; 1.
DR   PANTHER; PTHR11070:SF23; RECBCD ENZYME SUBUNIT RECB; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01485}; DNA damage {ECO:0000256|HAMAP-Rule:MF_01485};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01485};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01485}; Exonuclease {ECO:0000256|HAMAP-Rule:MF_01485};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01485, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01485};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01485}; Nuclease {ECO:0000256|HAMAP-Rule:MF_01485};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01485}; Reference proteome {ECO:0000313|Proteomes:UP000009874}.
FT   DOMAIN          1..467
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          498..776
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          1..906
FT                   /note="DNA-binding and helicase activity, interacts with
FT                   RecC"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   REGION          934..1220
FT                   /note="Nuclease activity, interacts with RecD and RecA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   ACT_SITE        1120
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   BINDING         20..27
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT   BINDING         994
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   BINDING         1107
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT   BINDING         1120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
SQ   SEQUENCE   1220 AA;  136352 MW;  FAA533D272F66F9E CRC64;
     MSSKLEAIRF PLHGSRLIEA SAGTGKTWTI AALYVRLVLG HGGDDAFVRP LLPSEILVMT
     FTRAATRELS NRVRERLVQA AAYFRGEAHE QDAYLDELAE AYAPGSERSI AAHRLMLAAE
     TMDEAAIFTI DAWCQRMLRE HAFDSGSLFD EELVSDERML FEDAAHDYWR QHVYPLGAQN
     LAIVLDTWSD VEALKGSVRE LVQRGPLLGE VAREPLGKQV ARLAQAQREE LARLKHGWVE
     RADAMERWIA GHRERAPKCF NGNKMRADSL VKWFEALRAW ATDPARHMPD LSDTAWKRLT
     PDGIVDAFSK DFSAEVPDCF DGTAALQEAL GAIDPIAHAL LRHAAGHIGA RMQELKRRNR
     QFGFADMLER LKLALEGENG AALRERIVQQ YPVAMVDEFQ DTSPDQYRIF DLLYRVGAND
     PQQGLFLIGD PKQSIYGFRG ADIHSYLSAR RATTGRHYQL DTNYRSTAAL VGAVNALFLH
     AEGGDGRTGH AQAAFRFRRG DDNPLPFEAV KARGHRERLV GVESDGEIEA MSVCTTCDDL
     KAEDYRSFFA HHCAEHIVRL LNDERVGFRD EQDGGFRRLM PADIAILVRD RREAAAVRQA
     LVRRKVASVY LSDKDSVVES EEAADMLRWL YAVANPLDGA LARAAFATRT AGLPMGELAR
     LSSDELAWER RVEQLKALHG AWQRRGVLAM LRTFIHELGL PARLLGEPGG ERRLTNLLHL
     AELLQEASAQ LEGEQALIRW FAEQIEGLGA GGDERVLRLE SDAELVKVVT VHKSKGLEYP
     LVYLPFAVTA RATNRRNRAF FEYVDDAGSR RLDLALSDEA LEAVDRARIE EDLRLLYVAL
     TRARHFLWLG AAAVAGTRKG ENRLHESALG YLLAGGAPIP ADGLRARFEA VAGAGGGIAL
     RELEREDGVT MLARQDARPA LLDAPVYRAD FEKDWSIGSF TSLTRHAVAP PPTPMRAQEQ
     TLLEEAPQAP LPPRIDDVAW HRFPRGSVPG NFMHEQLEWL AREGFDCLDQ PHCETRLVQR
     IERAGWSNRL EDALTWLRAI VDTPLPPLGA ALRALQGVLP EMEFWFPSER LALPALDALC
     RAHLLNGIER PVLPERDLHG MLKGFADLVF EHEGRYWVLD YKTNALGPND AAYSQAAMEA
     GMAEHRYEIQ GSIYLLALHR LLRARLGEAY EPEVQLGGAI FMFLRGIANP DTRGCCVLAP
     DLELLDKLER LLDKEKHGQD
//
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