ID A0A1M4M7Q9_9FIRM Unreviewed; 1130 AA.
AC A0A1M4M7Q9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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 ECO:0000313|EMBL:SCG83697.1};
GN ORFNames=DW1_2131 {ECO:0000313|EMBL:SCG83697.1};
OS Proteiniborus sp. DW1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Proteiniborus.
OX NCBI_TaxID=1889883 {ECO:0000313|EMBL:SCG83697.1, ECO:0000313|Proteomes:UP000185208};
RN [1] {ECO:0000313|EMBL:SCG83697.1, ECO:0000313|Proteomes:UP000185208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW1 {ECO:0000313|EMBL:SCG83697.1};
RA Seilhamer J.J.;
RL Submitted (AUG-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|HAMAP-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; FMDO01000042; SCG83697.1; -; Genomic_DNA.
DR RefSeq; WP_074350598.1; NZ_FMDO01000042.1.
DR AlphaFoldDB; A0A1M4M7Q9; -.
DR STRING; 1889883.DW1_2131; -.
DR OrthoDB; 9758506at2; -.
DR Proteomes; UP000185208; 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; 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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01452};
KW Iron {ECO:0000256|HAMAP-Rule:MF_01452};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01452};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01452};
KW Metal-binding {ECO:0000256|HAMAP-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}; Reference proteome {ECO:0000313|Proteomes:UP000185208}.
FT DOMAIN 5..283
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21445"
FT DOMAIN 754..1097
FT /note="PD-(D/E)XK endonuclease-like"
FT /evidence="ECO:0000259|Pfam:PF12705"
FT BINDING 765
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1087
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1090
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1096
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1130 AA; 131719 MW; 803AF60F824519E7 CRC64;
MKIRYILGRA GSGKTSRILD EIEYRLKEKS NHKLILLVPE QFTLQAEADL IFKKNLQGIM
RVEVLSFQRL GYKVLNEVGG IKKTAINELG KIMVLRKLFE ENAKDLTVFN KASKKDGFLS
SFCQLITELK KDDIQTEVIE EKLESITQDC MLKRKLKDIS LIYSKFNEYM EGKYADDEDK
MKLVIEKLDN SIYFDDAEIW VDGFNSFSAL EYKIIEKLML KSRKLNVSLT LDLNSSNDAN
IFRTTLNTYG RLRKIAQQNS VEERKTVLNI NPIYKNQEIW HLEQQLFAYP YRKYEKKTER
IKVFYSLNQY TEIENVASQI VSLVRDKNYR WRDISVVCNI IDVYSPTIKR VFSEYGIPYF
IDEKRSIMNN PIVKFIISGL EIVSRNFRYD DIFKFIKTGF SDLDKNEYEE LENYVLRYGI
MGDKWLDDFA YGEQSSELER INSIRKKFTE HILEFKKKVK SKTRVDEITK YLFEFLTVMN
IEEKLNNLIE DQKDKGYLDL VNENTQIWNI LMEVLDQLVE ILGDKKVTIS EYVKILESGL
LEYQVGVIPP TMDQVLVGNL DRSRSHDIKA LFVVGVNDGI LPSTIEEGGL LLDEEKADMK
SLGIEISTDS ETKACEEEFS VYASFTKPSD YLFISYALGD SEGKTIRPSM YIDRIKKVYS
NLTIYSDIVK DEESELNLVS TPMSTFKYLV ENLRNALDGD NINSIWWDIY NWYFNKDEWR
EKLKIVIEGL YHKNQQERID EHYTRQIYQV PFRTSISRLE KFVNCPYSHF VKYGLAPEER
KIHEIKSPDI GMLFHDSIEE FSKELTLENL SWSDIDRNKS DEIVEKVLDK MIDDFQHGLL
LSTNRYKYMV NRLKRISKRA LWTITEHIRK GDFVPKQHEV IFGDGPNSKI PPIIISLPNG
DEVRLEGRID RVDVLEGEKE SFVKIIDYKS GTKAFSLSDV YYGLQIQLLV YADAIISNGD
KLVKSDIYPA GVFYFRIDDP MVQSDEEDLE IIEKEIAKKL KLDGIILKDI NIVRAIDRDI
EETNHSTVIP VSINKDGSFS KNSSVLDKEE LNMLIKHVKG LISEIAEEIL KGKIKIEPCK
TDKYVSCTYC EFSTICQFET SFEDNKFKNI KKLKDEDVLQ KIKEKTGGEE
//
