ADDB_ANOFW
ID ADDB_ANOFW Reviewed; 1154 AA.
AC B7GM52;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 77.
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=Aflv_2231;
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1;
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
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=ACJ34590.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000922; ACJ34590.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041638832.1; NC_011567.1.
DR AlphaFoldDB; B7GM52; -.
DR SMR; B7GM52; -.
DR STRING; 491915.Aflv_2231; -.
DR PRIDE; B7GM52; -.
DR EnsemblBacteria; ACJ34590; ACJ34590; Aflv_2231.
DR KEGG; afl:Aflv_2231; -.
DR PATRIC; fig|491915.6.peg.2291; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR OrthoDB; 1283891at2; -.
DR Proteomes; UP000000742; 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; -; 3.
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 Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
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..1154
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379150"
FT DOMAIN 1..284
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 279..583
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 799
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1120
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1123
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1129
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1154 AA; 135151 MW; EBB638682549C591 CRC64;
MSVRFIIGRS GSGKTTMCLK EMIDQLAQKP DGDPIIYLVP EQMTFQSEYA LMNGSLKGMI
RAQVFSFTRL AWRILQETGG MSRHHLTQTG VHMLLRKIVE QQKEQLTLFR KAADKRGFIE
QLEQMLTEYK RYCVTPATLK QTEEQLRRHA TANETVLADK LKDTAMIFEQ FEQQMAHHYV
DSEDYLRLLA EKIRHSSYMK RARIYMDGFY EFTPQEYMVI EQLFIHCPHV TVALTLDAPY
EQLPDDLHVF RNTWRTYAQL RDIALQNGVP IEKVEQLRHN VRHKHEELRH LEAHYDDRPV
CKWEKQTEAI IIGEATTRRA EIEGIAREII RLVRDEGYRY RDIALLIRNV GDYRNVLKTV
FADYRIPYFI DEKEPMLDHP FIEWLRASME AVRTNFRYEA VFRAVKTDFF FHLDQPVHDM
RMAMDQLENY VLAFGIQGDK WTEHWTYRKY KGLEGVHAPQ TDEEKRYEQQ LNEWRKLVIS
PLLVLQKRLK QAKTGREQCE ALYAYAEHLQ IPQKLERLRD EAEERGDLSV ARHHEQVWQA
FIDLLDQYVE ILGDETLSLE TFLTIIETGF ESLQFSLVPP ATDQVLIAHF DRSRLSNIRC
TFLVGVNEGV IPMRKNDDGM LSETDRELLY HYSLHVAPAS RERMLDEPFL LYLALVSSSE
RLYVTYALSN EQEKTLLPSM FIKRLTDMFP NVTKMQWGTD PFLLPLQQQL AYVTNDVATL
GPLVQQLEAW KRQYAIEPMW WDVYNAYVQH EQWKERIAVV VRALFYENRA KRLNKQLAKE
LYGKKVKASI SRMETFNRCP FAHFAAHGLK LKERTVFQLK APDMGQLFHQ ALKVIADRLR
QEQLPWSQLS KQQCEQLSYE AVEQIAPYIQ QEVLLSTHRY RYMKKKLQTI MTKATTVLSE
HAKRSGFVPI GVELGFGDGE PLPPLTFTLS DGTVLQFVGR IDRVDQAMSE QGVLLRVIDY
KSKQKTLDLT EVYYGLALQM LAYLDIVLEY AEKLVGTSAF PAGVLYFPIH NPMMKVNEWL
DEHELEKKFL EQFKMGGYVL ADEKTVRLMD EHVEPGTSSL IIPVRLNKNG TFAQHSKVLT
EQQFTMLRQH VRRFIVDVGE QMIEGVTHIA PYKQKNKTAC QYCEFRDVCQ FDEGVDAEQY
RVLTPKNIDE WLKG
