ADDB_BACP2
ID ADDB_BACP2 Reviewed; 1169 AA.
AC A8FBR0;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B {ECO:0000255|HAMAP-Rule:MF_01452};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01452};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01452};
DE AltName: Full=ATP-dependent helicase/nuclease AddB {ECO:0000255|HAMAP-Rule:MF_01452};
GN Name=addB {ECO:0000255|HAMAP-Rule:MF_01452}; OrderedLocusNames=BPUM_0993;
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032;
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA Weinstock G.M.;
RT "Paradoxical DNA repair and peroxide resistance gene conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(2007).
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:0000255|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=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01452};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000255|HAMAP-
CC Rule:MF_01452}.
CC -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01452}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABV61677.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000813; ABV61677.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041815374.1; NC_009848.4.
DR AlphaFoldDB; A8FBR0; -.
DR SMR; A8FBR0; -.
DR STRING; 315750.BPUM_0993; -.
DR EnsemblBacteria; ABV61677; ABV61677; BPUM_0993.
DR KEGG; bpu:BPUM_0993; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OrthoDB; 1283891at2; -.
DR Proteomes; UP000001355; Chromosome.
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-EC.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
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; 3.40.50.300; -; 4.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_01452; AddB_type1; 1.
DR InterPro; IPR014140; DNA_helicase_suAddB.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR02773; addB_Gpos; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; DNA damage; DNA repair; Exonuclease; Hydrolase; Iron;
KW Iron-sulfur; Metal-binding; Nuclease; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1169
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379163"
FT DOMAIN 1..285
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 280..586
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 801
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1130
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1169 AA; 134856 MW; 1F43DF6882C00EE8 CRC64;
MEIQFLAGRS GSGKTTAILE EIKEQLRLDP LGPPIIFLVP DQMTFLMEYE LAKTSEAGGM
IRAKVFSFTR LAWSILQQTG GANRQFVTST GIQMLLRKVI EEQKDKFKVF KKASDKPGFV
EQIEKTMAEF KRYCMLPEEI EKISVESMLS EYTEERRAAE KLHDLHVLYQ QMEEHLQDEY
VHSEDYLNLL AQQIPSAEEI KGAHIYIDGF YQFTPQQLLV IEQLLLHAAK VTAAFTVDQS
YHDRQPNELD LFRMTGKTYF QLYQLAKECG ADISETIFER NHRHLYTPDL AYLEHQYEQR
PVQPYQENTP HLTVSKSASK RAEIEGVARD ILDLVREKGL RLRDISVVAR HVDDYKDTLK
EVFRDYDIPF FIDGNESMQY HPLIELIRSS LDVIKGNWRY EAVFRCVKTE FLFPLEITKN
KAREQADQLE NYCIAYGVKG ERWTNGSRFH YRRFQSLDED FRQTDQEIEM EQMLNDVKEW
ITPPLYQLQK RLKNAQKVRD MVEAVYVFLE EIQVPDKLEK ARLEAEEAGR LAEAMQHGQV
WDAVIQLMDE FVDMLGDEEL SFPLFQQMID TGLASLKFAL IPPSLDQVFI GSMDLSRMYQ
VKCMFIIGVN DGVIPARPSD ESVLSEDDRE WLKRAGAELA ETGKERLLDE QFLIYQALSS
PSHHLYLSYA ASDAEGRSLL PSPLIKYCQE LMPNHQQALY VLDPELLEDD EQLKFVANEH
VSLSYTISQL QQWLNQYPIS GVWWSVYNYL MTSPNRDVSK NIMSSLFFTN RAKPLKPNVT
KELYGDHIQG SVSRMEKFNA CAFSHFASHG LKLKDRQFYK LEAPDIGQLF HSALKHISDT
LVEQKKDWKN LTKEDCVTYS RHAIEQLAPR LQKEILLSSN RHAYIKEKLQ KILIRVSSIL
SEHAKVSGFS PVGLELGFGG QGPLPPFTFQ LKNGCTMELV GRIDRVDKAE GSKGLFLRIV
DYKSSEKGLD LAEVYYGLAL QMLTYLDLTI TYSKEWLGIE ATPAGILYFH IHDPFIQAPI
PLAEDEIEQE IFKKFKMKGL LLEDVEAVKL MDQTLESGRS QVIQAGLKKD GSFRSDSAVL
SEDHFHILTQ HVRRTFEEAG ERITNGEVAI NPYKLKDQTP CRFCSFKSIC QFDESIEDND
FRVLTSEKDD VVIERIKKEG DQYANTKTE
