ID A0A1G5APK7_9BACL Unreviewed; 1167 AA.
AC A0A1G5APK7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN05720606_10144 {ECO:0000313|EMBL:SCX79843.1};
OS Paenibacillus polysaccharolyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=582692 {ECO:0000313|EMBL:SCX79843.1, ECO:0000313|Proteomes:UP000198538};
RN [1] {ECO:0000313|EMBL:SCX79843.1, ECO:0000313|Proteomes:UP000198538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL9 {ECO:0000313|EMBL:SCX79843.1,
RC ECO:0000313|Proteomes:UP000198538};
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|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; FMVM01000001; SCX79843.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5APK7; -.
DR STRING; 582692.SAMN05720606_10144; -.
DR Proteomes; UP000198538; 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; 4.
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}; Helicase {ECO:0000313|EMBL:SCX79843.1};
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}.
FT DOMAIN 5..295
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21445"
FT DOMAIN 792..1133
FT /note="PD-(D/E)XK endonuclease-like"
FT /evidence="ECO:0000259|Pfam:PF12705"
FT BINDING 803
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1123
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1126
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1132
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1167 AA; 132357 MW; 60F3E3B65584A295 CRC64;
MSVRFVIGRA GSGKSTLITR EITSLLRQEP RGKPLILLVP EQSSFRTEQA LVSSGDIKGT
MRAEVLGFRR LAYRVMQEAG GSARVPIGAE GKKMLLYKVI QRRKEELRLF AASGSQLGFI
GELTNLYSEF KRYEVHASAL EEGLATWSIA SASPILEDKL HDLNLIYHDY EKELADLYID
DEDTLNELTG RLPESTWLQG AEVWIDGFHG FTPQEMSVIG QLMLQASSVT ISLTLDRRYE
QGVLPGELEL FYPTASAYVR LKGMAEHLDV SAETTVLHDE VLPRFKERPG LAHLEAGFDR
RIRWRSQGED SGIRLMAAEN RRAELEGALR EMRRLTQEEG ARYRDMAVLV RGLETYADIA
EPLFRDYDVP VFLDRRRSEL HHPLSEFIRA ALDIVRRNWR YEDVFRCVKT DLLLPLDGSI
TREDMDQLEN YVLACGIHGY RWNDGKPWKY VPSLSLEDNA QEERSRGRDA VLSLMESCRT
LITSALGTFE KRMKKAKTAA AQCEALFRLL EDADIAHKLD QMSAEAKTQG DPERSREHRQ
MWGAVLDLLD QMVDMMGNER LDITLFAGMM ETGLTELKLG LVPPALDQVL FGSMDRTRLR
DMKYVFILGA VDGELPAIPQ DNGVLTEQER LLLTERGMGL GPGATRLMLD ERFLIYTALT
AASKQLWLSY PVADDEGKSI LPSEIVRHVR KMFGLQEQPL LAQPPVSDLE SVHLSYAIHP
EQSLSMLIGQ LRRWRRGEDI PEIWWAVYNW HVNREASRPQ LERLLGSVFY RNRARRLDTS
TSRRLYGTEV RTSVSRMERF VACPFSHFAS HGLKLKDRQL YRLQAPDIGQ LFHAALSQLA
MRLREENRSW GSLTPEQCRQ EAEQTVEQIA PQLQGEILLS TKRYGYIFRK LKDIVSRASV
ILGEQSRRGS FEPIGLELDF GPGKPLPPLR FELENGCVLE IVGRIDRVDV AEGENGLLLR
VIDYKSSQTD LKLHEVYYGL SLQMLTYLEV LLSAAEEWLG ETAMPGGTLY FHVHNPLLQS
ANGMTSEQAE QELLKRFKMK GLLLADRDAV AQMDNTLDKG HSAIIPVALK ADGSFYSSAA
VATPEQWDTL LTAVRGNIRE IGTRITDGDT AIEPYRIQQE IACTFCSYKS LCQFDENIEG
NDYKLLSKPG KQQVWDMLSH SKEGETL
//
