ID J3VSX2_9ENTR Unreviewed; 1190 AA.
AC J3VSX2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=A359_06700 {ECO:0000313|EMBL:AFP85056.1};
OS secondary endosymbiont of Ctenarytaina eucalypti.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts.
OX NCBI_TaxID=1199245 {ECO:0000313|EMBL:AFP85056.1, ECO:0000313|Proteomes:UP000003936};
RN [1] {ECO:0000313|EMBL:AFP85056.1, ECO:0000313|Proteomes:UP000003936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ceuc_S {ECO:0000313|EMBL:AFP85056.1};
RX PubMed=22821013; DOI=10.1093/molbev/mss180;
RA Sloan D.B., Moran N.A.;
RT "Genome reduction and co-evolution between the primary and secondary
RT bacterial symbionts of psyllids.";
RL Mol. Biol. Evol. 29:3781-3792(2012).
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}.
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DR EMBL; CP003546; AFP85056.1; -; Genomic_DNA.
DR RefSeq; WP_014888353.1; NC_018419.1.
DR AlphaFoldDB; J3VSX2; -.
DR STRING; 1199245.A359_06700; -.
DR KEGG; sect:A359_06700; -.
DR PATRIC; fig|1199245.3.peg.798; -.
DR HOGENOM; CLU_001114_6_0_6; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000003936; Chromosome.
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; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000003936}.
FT DOMAIN 1..446
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 476..742
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..850
FT /note="DNA-binding and helicase activity, interacts with
FT RecC"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT REGION 899..1190
FT /note="Nuclease activity, interacts with RecD and RecA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT ACT_SITE 1081
FT /note="For nuclease activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 21..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
FT BINDING 957
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 1068
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
FT BINDING 1081
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01485"
SQ SEQUENCE 1190 AA; 136096 MW; 60B65AF64599116B CRC64;
MNAESLNPLT LPLQGVRLIE ASAGTGKTYT LAVLYLRLLL GLGGEAAYSR PLSVKEILVV
TFTEVATEEL RCRIRKNIHN LRLACLQGTS EDPLLSSLLA QINDFRLAAC YLLAAERQID
EAAIHTIHGF CQRILHHYAM ESGMFFQQTL IEDESFLRQQ VSDDFWRRHC YLLPLDIARI
VQKYWEGPEQ LLAELLPYLQ GEMPVFPNPP DITEPIIARH ARIIAAIDAL KQKWRESSVA
LREIFDNYTL NHLISNKKNL STWLEKIDFW ASNSTIDYQV PDELANFKIS ALGKIITDGE
PPKHELFFAI EAFFQQKLSL RELIFVMALV EIRRSLEEEK KQRAEIGFDD LLSLLDRTLS
AGDSALCKSL RTRYPVAIID EFQDTDPQQY RIFRQIYSSH ITCALLLIGD PKQAIYAFRG
ADIFTYMRAR SEVDAYYTLD TNWRSSAGMI NAVNQLFQNL YMPFIFSAIP FFSVRSVDRN
TGLRLVVQQQ SQPALRIWLQ SGGAVSIREY QECMAHQCAV TIREWLDAAR LGKAWLEGRQ
GNQALRASDI TVLVRNRNEG TLVRTALAAL KIPAVYLSNR DSVFETLEAR ELQFILQAVL
APENNTWMRL ALSTRLLGLN AAALDVLNND EDRWEKWFEE FSRYRERWKK HGVLPMLRQI
LINYRLAERL LASERGERRL TDVLHIGELL QEASMKLENE FSLVRWLILQ VESPQPQVKN
QQLRLESDAH LVQIITVHKS KGLEFPIVFL PFPADFRLNK QPLFHNRASY TACLDLSKDA
ESLRLAEEER LAEDVRLLYV ALTRSIYHCS LGIAPLFRSR RKKTGVSDLH LSALGYLIQQ
GKACDANVLH KRLAALVRRA GGDIALRKTL KVTGTPLTAA PAPLPVLGAR SFPGLQRDPW
RVTSYTGLQR YFSPAVMALK QSSRLDVGVR SSGRQQKRLS LTPHTFPRGV LPGLFLHDLF
KTLDFNRPVD PKWLNQKLAE QGIEALWLPA ITHWLECVIA MPLDGNSLTL AHLGPNRRYS
ELPFYMSIDA TVQARDLDRL CKRHDALSAR CLQLAFPPVK GILKGFIDLV FHWQDRYYLL
DYKANWLGKD SSAYTQSAIE EAMILHRYDL QYQLYTVALH RFLRHRLVNY EYHRNFGGVY
YLFLRGFDAP TLGNSIFYCR PDIALVDGLD NLFIGNKIAT DGESLSKSME
//
