ID A0A437KH26_9BACI Unreviewed; 1165 AA.
AC A0A437KH26;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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:RVT67621.1};
GN ORFNames=EM808_03850 {ECO:0000313|EMBL:RVT67621.1};
OS Niallia taxi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=2499688 {ECO:0000313|EMBL:RVT67621.1, ECO:0000313|Proteomes:UP000288024};
RN [1] {ECO:0000313|EMBL:RVT67621.1, ECO:0000313|Proteomes:UP000288024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M5HDSG1-1 {ECO:0000313|EMBL:RVT67621.1,
RC ECO:0000313|Proteomes:UP000288024};
RA Tuo L.;
RT "Bacillus sp. M5HDSG1-1, whole genome shotgun sequence.";
RL Submitted (JAN-2019) 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}.
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:RVT67621.1}.
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DR EMBL; RZTZ01000001; RVT67621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437KH26; -.
DR Proteomes; UP000288024; 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; 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 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:RVT67621.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000288024}.
FT DOMAIN 278..584
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 800
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1120
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 1129
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1165 AA; 133680 MW; 17E64D6EF4FDAFE1 CRC64;
MSVRLLAGRS GSGKTAFCID SIREKLFADP EGNPIIYLVP DQMTFMSDQN LAGSEGLGGM
FRAQVYSFTR LAWRVLQETG GISRQHINSV GISMLIRSII EEKKEELSLF KKVADKNGFI
GQVEQLVTEF RRYCVTPEEL GGRQQGIAEA GNTDRALLDK LHDLEIIYQS FEENMLGKYI
DGEDYFRLLA EKISSSEYLK KAEVFIDGFY SFTPQEYLIL QQLIQTCKNV TITFTVDEPD
RNSFANELDL FRMSKETYAT IYSFAKQLGV EVEEEFFGEI HRDLHESLKH IEAHFDSRPA
VPYSGDSAVR FAESVNPRAE IEGVAREIKK LIRQQGYRYR DISLLSRNTG EYQNIIETIF
ADYEIPFFID QKRTMHFHPL VELIRSTLEI IETNWRYEPV FRAVKTELLF PLHMRKSNIR
EKVDKLENYC LAYGIKGDKW TRKERWKYRR FQGLEWDQGV QTDSEKQMEQ ELNELRLSLA
APIMRLANRL KRAKTGRAKC EALYLYLEEL EVPEKMDLWK AELEEKGELV KAGEHDQAWN
SIVDLLDQFV EILGEEEMAR KQFATILDAG LDTLKFSLVP PAIDQVLIAD LENSRLGRIK
AAFVIGLNEG VFPAKFTDDG IFADSDRESL VEAGMKLAPT SKTRLLDEEF LAYKAFTSAS
ERLYLTYPLA NDEGKSLLPS LYVKRMRDLV PEAKTLYFMA DPKELSELGQ LGYAVDLKTS
LSYLNGQLQL KKRHYPIYDF WWDVYNAYIE NDQWRAAAKK VFSSLTYQNR TSSLADETST
MLYGESITAS VSRMELFQSC PFSHFATHGL KLKERQVYRL EAPAIGDLFH AALKYIAETV
LHENMMWSDL TKEQCEMLAK DAVEMLAPKL QNEILLSTNR HHYIKRKLEQ IISRASFILS
EHAKYSGFAP IDLELEFGPK GKLPPMGFSL RNGTKMELVG RIDRVDKAEL DNEVYLRVID
YKSSAHELNM NEVYYGLSLQ MLTYLDLIIS NSSILVEKEA NPAGVLYFHV HNPVLSTKKV
LTLDEIEEEL FKKFKMNGLM LGKEDVIKLM DGSLEKGDSP IVPAGVKTDG TLTKRSKVAS
REDFSSLQKF VRHKYVETGN KIIGGNVEIA PYQLKEKSPC TFCSFKSVCQ FDEGLESNQY
RKLQTFSKEE ALELIRKEAN ANENY
//
