ID A0A1I3T061_HALDA Unreviewed; 1168 AA.
AC A0A1I3T061;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B {ECO:0000256|HAMAP-Rule:MF_01452};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01452};
DE EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_01452};
DE AltName: Full=ATP-dependent helicase/nuclease AddB {ECO:0000256|HAMAP-Rule:MF_01452};
DE AltName: Full=DNA 3'-5' helicase AddB {ECO:0000256|HAMAP-Rule:MF_01452};
GN Name=addB {ECO:0000256|HAMAP-Rule:MF_01452};
GN ORFNames=SAMN04487936_103173 {ECO:0000313|EMBL:SFJ64498.1};
OS Halobacillus dabanensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=240302 {ECO:0000313|EMBL:SFJ64498.1, ECO:0000313|Proteomes:UP000183557};
RN [1] {ECO:0000313|EMBL:SFJ64498.1, ECO:0000313|Proteomes:UP000183557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3704 {ECO:0000313|EMBL:SFJ64498.1,
RC ECO:0000313|Proteomes:UP000183557};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The heterodimer acts as both an ATP-dependent DNA helicase
CC and an ATP-dependent, dual-direction single-stranded exonuclease.
CC Recognizes the chi site generating a DNA molecule suitable for the
CC initiation of homologous recombination. The AddB nuclease domain is not
CC required for chi fragment generation; this subunit has 5' -> 3'
CC nuclease activity. {ECO:0000256|HAMAP-Rule:MF_01452}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01452};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01452};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01452};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01452};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_01452};
CC -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000256|HAMAP-
CC Rule:MF_01452}.
CC -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01452}.
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DR EMBL; FOSB01000003; SFJ64498.1; -; Genomic_DNA.
DR RefSeq; WP_075035787.1; NZ_FOSB01000003.1.
DR AlphaFoldDB; A0A1I3T061; -.
DR STRING; 240302.BN982_03440; -.
DR OrthoDB; 9758506at2; -.
DR Proteomes; UP000183557; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 6.10.140.1030; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR HAMAP; MF_01452; AddB_type1; 1.
DR InterPro; IPR049035; ADDB_N.
DR InterPro; IPR014140; DNA_helicase_suAddB.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR NCBIfam; TIGR02773; addB_Gpos; 1.
DR PANTHER; PTHR30591; RECBCD ENZYME SUBUNIT RECC; 1.
DR PANTHER; PTHR30591:SF1; RECBCD ENZYME SUBUNIT RECC; 1.
DR Pfam; PF21445; ADDB_N; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01452};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01452};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01452};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01452};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01452}; Helicase {ECO:0000313|EMBL:SFJ64498.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01452};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01452};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01452};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01452};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01452};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01452};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01452}.
FT DOMAIN 283..588
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 802
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1127
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1133
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1168 AA; 134777 MW; 6BBB1FAAA044CDF1 CRC64;
MGMRFLLGRS GAGKSTRCLD EIEKKLKDDP RGATVIYIVP DQMTFQQEYG LLKRDGVEGS
IRAQVFSFSR LAWRVLQETG GGTRKFITST GVQMMLRKIV EERTSDWRVF QKAIEKQGFI
EQLEGMITEF KRYRITPNDL HSQIDALDQF VHSTNQEQGL RDKLDDLVYI YDRLVDSLKD
QYIDSEDQLQ LLASKIPEAA FLEGAEVYID GFHSFTPQEY GVIEALLKKV KTVNVTLTAE
QPEHDENPEL DLFHETKQTY LDLKNVVEEA GVKVDDVEIL DHKEGRMKHQ PAFQHLEQCY
DVRPAEAFEG EAPIQIAEAV HPRAEVEGVA QEILRLVRDE GYRYKDIAIL MREPEVYHSL
VETLFDDYDI PVFIDEKRTM LNHPMIELVR SGLDVIEGNF RYDAVFRLLK TGFIPATDRN
DPLTEDAIDE LENYVLEYGI RARSQWFSDE PWVYQRFRGF ENSSQTDEEK AKQQRINAYR
EQVRDALQSF DEELRAAETI EEQARAIYLW LEGLKVPGQL ETWRDYYDEK GEIERGREQA
QVWDEFLQLL DEMVEMAGDE KMSLQVFRHT LDSGIESLTF AHVPPSMDHV IVGSVDRSRM
TGIKAAFLLG VTDGMWPMKP PSDGMISEQE RSLLAEHGLQ LADGSNRQLL DDRFYVYLAL
TMASDKLWIS YPLSNEEGKS KVPANLIPRI EELFPVCKEH VMLHDPDDLH DATRFITNPQ
KTRSALTSQF ARYLKGYVMQ PVWWEVLNWY IEHEQPNGLT NRILQSLFYK NKPVSLSKET
TGQLFDPTVK TSVSRLETYH RCSYQYFAQH SLGLEERRTY KLDAPDIGQL FHEALKQITE
WIQVEGRDFS QLDRRETNLY AEKATNELAP VLQNQILKSS NRYQYIQKKL QQVIARATFV
LSEQARNSNF SPVGLELGFG TGGDAKLPPL SLDLPNGYEL MLRGRIDRVD KALSEEDLYL
RIIDYKSSSK GLSLVDVFYG LSLQMLAYLD VVLTNAEHWL GQSASPAGVL YFHVHNPMIT
GKQLLKDEQI EEEIFKKFKM QGLLLENERV VQMMDTGLDK GYSQIVPAAL KAKGGFYKSS
KTADAERFEQ LKQYIRSLMT EAGTKITDGQ VDLDPFQKKQ QVACEFCSYR PVCQFDPTLE
DHNYRKLQEM KDEDVLERLI KREGDGKW
//
