ID A0A233HFW4_9VIBR Unreviewed; 1205 AA.
AC A0A233HFW4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=B9J89_24680 {ECO:0000313|EMBL:OXX60151.1};
OS Vibrio sp. V15_P4S5T153.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1938669 {ECO:0000313|EMBL:OXX60151.1, ECO:0000313|Proteomes:UP000215241};
RN [1] {ECO:0000313|EMBL:OXX60151.1, ECO:0000313|Proteomes:UP000215241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V15_P4S5T153 {ECO:0000313|EMBL:OXX60151.1,
RC ECO:0000313|Proteomes:UP000215241};
RA Vazquez-Rosas-Landa M.;
RT "High clonality and local adaptation shapes Vibrionaceae linages within an
RT endangered oasis.";
RL Submitted (FEB-2017) 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:OXX60151.1}.
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DR EMBL; NDIJ01000024; OXX60151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A233HFW4; -.
DR Proteomes; UP000215241; 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};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01485};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01485};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01485};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01485};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01485};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01485};
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};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01485};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01485}.
FT DOMAIN 6..451
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 482..753
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..856
FT /note="DNA-binding and helicase activity, interacts with
FT RecC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT REGION 906..1205
FT /note="Nuclease activity, interacts with RecD and RecA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT ACT_SITE 1095
FT /note="For nuclease activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT BINDING 968
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 1082
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 1095
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
SQ SEQUENCE 1205 AA; 135130 MW; 294168D2CB5D62E6 CRC64;
MSMTPATVTT PLNTLTFPLH GARLIEASAG TGKTFTIAGL YLRLLLGHGD AKSRHQVPLT
VDQILVVTFT EAATAELRDR IRRRIHEARI AFSRGFSDDP VIKPLLEQTS HHKQAAQILL
QAERQMDEAA VYTIHGFCQR MLTQNAFESG SRFNNEFVTD ESHLKAQVVA DYWRRQFYPL
SIQLAAEVRR LWSSPAALLE KISGYLTGSA LTLSVEAMSG DLSALYQSCL SRIESLKKQW
LDSCDDLPPC IEASDLHAAT KKALLKRLEG LALWASNPQH ELNLPCELQE FAQSALEAKS
KKGQPPQHAL FTTIELFLQQ PISLEAPLLA HAITYCRAML AKAKAQKQWL SFDDLLTQLS
AAIDNDELGI LTERIRSLYP VAMIDEFQDT DPLQYSIFSR IYLPKAECGL FMIGDPKQAI
YAFRGADIFT YIKARKQVSA HYTLGTNWRS SANMVNAVNQ IFSTPDSAFI YDQDIPFLPV
EASPNAQQRQ WWLNGTVQPA LTYWLQEAQD SPLPKGEYLQ CMAKACASQI QTILSAAQHQ
QAYFDTAKGQ KSVQAGDIAV LVRTGNEGRM VKEALATQGI ASVYLSNRDS VFSSEVAQDV
QRLLQAVLTP EHDRALRACL ASPLFSLDAA SLDDLNNDES VWESAVNEFK QYRQLWLERG
VLPMLRSVMS KRHVAERWLE EPQGERSLTD FMHIGELLQQ ARQEIDSDHG LLRWLAQAIS
DAEHGLGSRD DQIQRLESER NLVQIVTIHK SKGLEYDLVF LPFVASYREA SEGKYHDAVN
EETVLDITAS EASLKQADKE RLAEDLRLIY VALTRAVYGC FIGIAPLRNG RSTKEPTGVH
LSAIGYLLQN GQAAGIADLN AALHAQSNQY IRVSEPPAEQ PEPFKALSVE TPVLSAKTLQ
AQIDRFWRMT SYSGLVKQGV KHASHDASLE VSGFDIDSAD EQAEALLVEP ERSIFTFPRG
ATPGTFLHSL FEEVEFTEPA SSDANQKVIL DLLVREQIDI EWLPVLQTLV DTVLQTPLDG
KTLRLNQKTS TQRLVEMEFL LPIEVLSAPA LNRVIQRHDP LSAKAGDLGF YTVQGMLKGF
IDLLFEHQGK YYVLDWKSNH LGDDVSAYHG DRLKAAMAEH RYDLQYQLYA LALHRFLRSR
LENYDYHHHF GGVYYLFLRG MDGESEHGIF STKPSFELLD EMDRLIDGET VDTRTTDAGQ
MELDL
//
