ADDB_DESHD
ID ADDB_DESHD Reviewed; 1218 AA.
AC B8FXD8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=Dhaf_2833;
OS Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=272564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10664 / DCB-2;
RX PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA Tiedje J.M.;
RT "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT anaerobe capable of dehalogenation and metal reduction.";
RL BMC Microbiol. 12:21-21(2012).
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; CP001336; ACL20857.1; -; Genomic_DNA.
DR RefSeq; WP_005816091.1; NC_011830.1.
DR AlphaFoldDB; B8FXD8; -.
DR SMR; B8FXD8; -.
DR EnsemblBacteria; ACL20857; ACL20857; Dhaf_2833.
DR KEGG; dhd:Dhaf_2833; -.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000007726; 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.
FT CHAIN 1..1218
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379186"
FT DOMAIN 1..279
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 281..588
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT REGION 987..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 6..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 786
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1126
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"
FT BINDING 1135
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1218 AA; 137160 MW; 98538C90CD2CF436 CRC64;
MRFIVGRAGT GKSTLCRQEI HKESQEHPEG LPLILLVPEQ ATHQMEMSLA HDPQSGGILR
AQVLSFRRLG WRVFSEVGGG GKAVIGEVGK RMLLRRLLLN HRSDLRVFAR SATRPGMADL
LAQAIAEFKI YRITPDQLRG IEDADELLLQ KTHELAFLYE ELNKSLGTAA RDPDDELNLV
AGKISQAPFL QGAKIWVDGF KGFTPQELYV IQAMLGTAAE ITVSLPLDPE LLKAGTPRFK
PGEELFYEPR QTYQGLVDLA REAKASISHV FLTETHRFEK AGLKHLERFY NAYPTQTFPG
GDDSTAPDPL GIALFPAANK RAEVEGVARE LRRLAREEGR TWRDCSVVTR DLPGYQGIIE
QVFNAHEIPY FLDHKRPVIH HPLLELLLSA IETVQKDWAY EPLFRCLKTD FFPCSKDRID
RLENYCLAYG IHGSAWKGNR SWSYYPDPNH KEETAGLNET RQIIYDLFSP FDQAIRPHPE
AGGPSVTVAQ ITEAIYELLI RLKVPEHLQE WAEAAHSRGD LAEAQLQNQI WDAVIQVLDE
LVAGLGEEVM DLSDFAMILT SGLENLQLGL IPPGYDQVLV GSLDRSRNPE TAVLFLLGAN
DGILPGKPSD EGVFDELERL RLESKGIMLA PKGKVQVYEE QYFIYTALTR AREQLYISYP
LTDEEGRGLT VSPVIHRLKM IFPGLPEKYL SLDEEEPGAL PHPYALLPAY ALHLQKLRQG
SSLSPLWQAI RLWFLSQTAA FPQVQLLEKG LRDQNEEGKL PQPLARQLYG KRLVTSVSRL
ELFARCPFAH FAQYGLKLKE RSNYRLSPPD MGQFFHAVLH DYAIALRERG LDWGELSKEQ
SWQLVNETAE PIALQLQNKI LLSNARYRYL THKLKRTVHH AVRVLGEHAR QGVFLPMELE
VKFGPQEALP PLEVPLSGGN SLLLRGQIDR IDGAVLGHEI YLRIFDYKSR EAHVSLNQIY
HGLDLQLLAY LDAALQGAQI LVSSSGLAEG SKGSEGSEGS EDSEDSTIHP AGFLYFPVLE
PQLKSKTLLY PEQLEKDRIK AVKVKGYLLA DRQVLLAMDR DLENSSLLGI KLTKSGEFKK
GSPILTEEQF ALLRKHLQHF LRCSGEALLE GDISITPYRQ GKHTACQFCS YKPLCHFDPY
LPENNYRNLP VIQDEEFWQR VQSQDSEQYP EQHPPTSVPG ETSRRALQKD GGNSPRGQEL
IWLGEDEAGA GKEDDGHE
