ID A0A1I5ZBX3_9BACI Unreviewed; 1164 AA.
AC A0A1I5ZBX3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=SAMN05421670_2613 {ECO:0000313|EMBL:SFQ53974.1};
OS Psychrobacillus psychrotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX NCBI_TaxID=126156 {ECO:0000313|EMBL:SFQ53974.1, ECO:0000313|Proteomes:UP000198734};
RN [1] {ECO:0000313|Proteomes:UP000198734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11706 {ECO:0000313|Proteomes:UP000198734};
RA Varghese N., Submissions S.;
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; FOXU01000004; SFQ53974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5ZBX3; -.
DR STRING; 126156.SAMN05421670_2613; -.
DR OrthoDB; 9758506at2; -.
DR Proteomes; UP000198734; 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 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:SFQ53974.1};
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:UP000198734}.
FT DOMAIN 276..582
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 799
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1119
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1122
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1128
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1164 AA; 133791 MW; EB745840C4B0E3EA CRC64;
MSLRIVSGRS GSGKTTFIHE EIITALQKAP IGDPIFYIVP DQMSFSSEYD LAAESGLPGL
IRAQVTTFKR LAWRVLQETG GIAKEEISGF GYRMLIRSLL ENHKDEFTLF KRAATKRGFT
DQIEVLLKEF SRYCMDYSTM ANALNNLENV NAPKTLIDKS SDIMLMLEKV EQKLGVSYID
GEGYLTLLAN KIKDSSLLAN TDLYIDGFTS FTPRELEIIE QLMKQVKRIT VALPMESLQD
AVDEQSLFYQ PANTCARLLE IAQMEKVEIE ETVHQSEQKR FRSPEIAHIE ANLDKLPPLQ
AKSEGNIHIT EAANRRAEMH AIARHIRELM QQKSIRFNEM AILHRDADTY EGLIETIFPQ
YDIPFFISKK KPMLHHPLIE LSRTILEIIR TDWKYEPVFR AVKTDLFFPL DASKKTWRER
ADRLENFVLA FGIYGDRWLD ERRWVYKKYR GLEFYSKVQT DEEKSIQADI HTMRDLIVEP
IKLLSDQLKQ SRTGKDFAIA IYTFIEALNV YEKLQSLKQA EEENGQLLLA SEHEQVWNEW
VNVIDQFVLM FGEKEMSLEE VAKILDEGYD QLTFSGIPPT IDQVIVGNVD IIRLTNIKTA
FVVGVNDGAY PKRMDHEGLL TDTEREWFTQ IGFELAPTSK MRLMDENYLI YKALVTASHF
LYVSYPMADN EGKALLPSLY IKKLHQMVSD LPVEIAVVDP SDMLSDELDL TSISHPRPTL
PYVVMQLRGA LATGKLTEVW QSVYQYYLED PYWSKLLKRI TKPLIHGNKT ERLNEEMTAA
LYGDTMISSV SRVEKYYSCP FAHYASYGLK LEERAEYRLE APQMGDLFHA ALKWIADETK
RIDIQWSDLT RPQCHQLARQ AVDYIVPVFV HQLLLSTNRY RYIQRKLEQI VANTLIALSR
HSKGSGFVPI AIEAGFGPGE VLPALEIPLK RNRKMQLRGR IDRVDAANIN GNMFVRIVDY
KSSKKGIDLN EVYHGISLQM LTYLDVAVEN ADVWLHEDAD PAGVLYVHMH NPFIQSQKEM
EEEELEDAIY KSYKMNGLLL DDTEVIMEMD DQISGFSKVI PVRMNKDGNL SKSSSKVVEP
EQMRLLQSFV RKKHEQAGNG MNAGDTRVLP YRIKDKMPCN YCSFRSVCQF DPADPAQQVR
ALKVEQPEII AEKIREEMSP HEHS
//
