ADDB_DESRM
ID ADDB_DESRM Reviewed; 1155 AA.
AC A4J4E2;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Dred_1415;
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) 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: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; CP000612; ABO49945.1; -; Genomic_DNA.
DR RefSeq; WP_011877764.1; NC_009253.1.
DR AlphaFoldDB; A4J4E2; -.
DR SMR; A4J4E2; -.
DR STRING; 349161.Dred_1415; -.
DR PRIDE; A4J4E2; -.
DR EnsemblBacteria; ABO49945; ABO49945; Dred_1415.
DR KEGG; drm:Dred_1415; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR OrthoDB; 1283891at2; -.
DR Proteomes; UP000001556; 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; 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..1155
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379189"
FT DOMAIN 1..300
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 280..590
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 792
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1111
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1114
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"
SQ SEQUENCE 1155 AA; 131126 MW; A6F9CC93B3F3EB59 CRC64;
MSLRFIVGRA GSGKSHSCLE EVRQRLRQNQ GESSIILLVP EQATFQYEYM LATTPELKGM
IWAQVLSFRR LAFRVLQEMG GAARAHIDDL GKKMVLRRIL EQRKSELKVF HRAAKQPGFA
DSLASALSEL KLYRIEPQEL QKGIQHMQEA PGSAIRDKLA DLSLLYNDLE EFLSGRFTDP
DDYLNLLAQR LPGSRTVQGA EIFIDGFTGF TPQEYGVIEQ MLGTADRVHV ALCFDPMYLQ
EPCDELEFFY PTVETYHTLL DMAGALRISL EPPIICGKET PVRFQKDSAI AHLEKYYFRH
PLQASDAAQG VSLVACANRR AEVEAAAREI IRLCREEELS WRDIVVVLRD LTNYSDLINT
IFNDHGIPVF IDEKRNVLHH PLVELIRSAL EVITQHWAYD PVFRYLKTDL IPVQRDDVDR
LENYVLAHGI RGNRWNDNRD WTYRRQYTLG EDCDIDDNEA EQLAQLNVVR YAAIEHINNF
SKKVANCGNV RQITTALFEL LESLSVAERM EAWAKEAEVA GRLIEAKEHA QIWDNVILLL
DEIVEAMGEQ ELNLEEYLQV LEAGLESLKL GLIPPGLDQV VVGTLERSRN PNVKAALVLG
ISDGVLPARP VEEGLFSDYE REALREIGLN LAPGARRKLF DEQYLIYTAL TRASSRLWLS
YPQADDEGKA LMPSPVIQRV KELLPLIQEE ILPVEPPCLG GDLAFIANPS RSLSYLAAML
RETVAGRLVD PVWQDVYSWF VQQPQYQESC RRVLAGLYHV NQETSLPPSM GRRLYGSRLR
ASVSRLERFT TCPFSHFLSH GLKLKERSQF KLAAPDLGQF FHAALKLFAE RIKALSLDWG
QLSRGQIITI TGEIVEELAP QLQNEILLST ARHRYLIKKL RRTLERAVVT LAEHARRGSF
RPVAVEIGFG DNAELPAVQL DLADHCQMEM AGRIDRIDSA CEGGQHYYSL IDYKSGQPDI
KLADIVHGLK LQLLTYLDVA LRYSKQLTQQ EALPAAMLYF SVRDPFVAST GPMTEEEAEK
NLLKQLKMKG LLLADPLVIS KMDKELSGQS DLLPVGLKKN GDFYSNSRVI TEEQFKLLRN
YLEFKLKSIG QQMVSGDIAI SPYQRGKEKA CRYCIFKSVC QFDPLLEDNL FRLLADQEEQ
VLWSLIKESL GDKHE
