ADDB_DESHY
ID ADDB_DESHY Reviewed; 1220 AA.
AC Q24WW7;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=DSY1686;
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51;
RX PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(2006).
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}.
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DR EMBL; AP008230; BAE83475.1; -; Genomic_DNA.
DR AlphaFoldDB; Q24WW7; -.
DR SMR; Q24WW7; -.
DR STRING; 138119.DSY1686; -.
DR EnsemblBacteria; BAE83475; BAE83475; DSY1686.
DR KEGG; dsy:DSY1686; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000001946; 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 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; 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..1220
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379187"
FT DOMAIN 1..281
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 283..590
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT REGION 989..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 788
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1128
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1131
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1137
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1220 AA; 137379 MW; DB7917CE372FD21D CRC64;
MSMRFIVGRA GTGKSTLCRQ EIHKESQEHP EGLPLILLVP EQATHQMEMS LAHDPQSGGI
LRAQVLSFRR LGWRVFSEVG GGGKAVIGEV GKRMLLRRLL LNHRSDLRVF ARSATRPGMA
DLLAQAIAEF KIYRITPDQL RGIEDADELL LQKTHELAFL YEELNKSLGT AARDPDDELN
LVAGKISQAP FLQGAKIWVD GFKGFTPQEL YVIQAMLGTA AEITVSLPLD PELLKAGTPR
FKPGEELFYE PRQTYQGLVD LAREAKASIS HVFLTETHRF EKAGLKHLER FYNAYPTQTF
PGGDDSTAPD PLGIALFPAA NKRAEVEGVA RELRRLAREE GRTWRDCSVV TRDLPGYQGI
IEQVFNAHEI PYFLDHKRPV IHHPLLELLL SAIETVQKDW AYEPLFRCLK TDFFPCSKDR
IDRLENYCLA YGIHGSAWKG NRSWSYYPDP NHKEETAGLN ETRQIIYDLF SPFDQAIRPH
PEAGGPSVTV AQITEAIYEL LIRLKVPEHL QEWAEAAHSR GDLAEAQLQN QIWDAVIQVL
DELVAGLGEE VMDLSDFAMI LTSGLENLQL GLIPPGYDQV LVGSLDRSRN PETAVLFLLG
ANDGILPGKP SDEGVFDELE RLRLESKGIM LAPKGKVQVY EEQYFIYTAL TRAREQLYIS
YPLTDEEGRG LTVSPVIHRL KMIFPGLPEK YLSLDEEEPG ALPHPYALLP AYALHLQKLR
QGSSLSPLWQ AIRLWFLSQT AAFPQVQLLE KGLRDQNEEG KLPQPLARQL YGKRLVTSVS
RLELFARCPF AHFAQYGLKL KERSNYRLSP PDMGQFFHAV LHDYAIALRE RGLDWGELSK
EQSWQLVNET AEPIALQLQN KILLSNARYR YLTHKLKRTV HHAVRVLGEH ARQGVFLPME
LEVKFGPQEA LPPLEVPLSG GNSLLLRGQI DRIDGAVLGH EIYLRIFDYK SREAHVSLNQ
IYHGLDLQLL AYLDAALQGA QILVSSSGLA EGSKGSEGSE GSEDSEDSTI HPAGFLYFPV
LEPQLKSKTL LYPEQLEKDR IKAVKVKGYL LADRQVLLAM DRDLENSSLL GIKLTKSGEF
KKGSPILTEE QFALLRKHLQ HFLRCSGEAL LEGDISITPY RQGKHTACQF CSYKPLCHFD
PYLPENNYRN LPVIQDEEFW QRVQSQDSEQ YPEQHPPTSV PGETSRRALQ KDGGNSPRGQ
ELIWLGEDEA GAGKEDDGHE
