ADDB_LACP7
ID ADDB_LACP7 Reviewed; 1147 AA.
AC A9KTE7;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 83.
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=Cphy_3424;
OS Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS (Clostridium phytofermentans).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=357809;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL Submitted (NOV-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABX43777.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000885; ABX43777.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_049762422.1; NC_010001.1.
DR AlphaFoldDB; A9KTE7; -.
DR SMR; A9KTE7; -.
DR STRING; 357809.Cphy_3424; -.
DR PRIDE; A9KTE7; -.
DR EnsemblBacteria; ABX43777; ABX43777; Cphy_3424.
DR KEGG; cpy:Cphy_3424; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR Proteomes; UP000000370; 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; 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.
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..1147
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379183"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 780
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1092
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1095
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1101
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1147 AA; 132134 MW; CD6C1F2A422CDBA4 CRC64;
MSLQFVIGGS GAGKSYQLYQ RVIESSLKEP KGKFLILVPE QFTLQTQKDL VTMHPKKGIH
NIDILSFLRL AFRIFEETGG NDRLVLEDTG KSMIVKKVMM EKRNDLILFG ANVKKQGFVE
EMKSIISELA QYSIHTDELQ KMKEVAKGKP LLNHKLTDIM TIYQAYEEFL QDKYINSEEI
LDLLCDVIDD SSFVNDSEIC LDGFTGFTPS QYKLLSHLMK KAKSVTVTIT MDESQINRKQ
EEHQLFYLSG KMAEKLTDLA ITQKIEIKPP ILVASENGGY SYRFHNSMAL SALEKNIFRY
PYKSFTEEQD DISITAAKDP MAEARHAVIE ITRLLREEEY RYKDIAIVSG AMEVYGDIVK
RELELAGIPC FVDHKKNILT NPVVEFLRSA LDVVTHNFDY EAIFRFLKCG LTDFTMDEID
LFENYVIAFG IRGKYRYEHE WERKYKTNYE VDLEKINYVR ECILKEFTPL YETLTSKKSS
VRECVNALYN LLCTYHIEEK IHIFVEKFKA QGEKEDKLRA KEYEQIYRMV LEIFDRMVEL
LGEDVLPLKE FRDILDTGFR EAKVGLIPPS IDQILVGDIE RTRLKDIKAL FFLGVNDGIV
PKANPGGGIL SDAERQLFAD HEIELSPTKR QTAYLTEFYL YLNLTKPQNK LYLYYSKLDV
SGKSIRASYL LGKISKIFPK LKIYDADRKS REDELLGTDQ GLSYLISVLR DYEGEQPKLW
REVYHLYVSG QIKGRISLDK VLQGVFYQNY EQGLTKEVAR KLYGETLLGS VTRMEKYAAC
AFAHFLQYGL SLEERQEYKI SMPDIGSLFH EALERFSKAL KELDISWHEL PEDVRISLGE
RCVREAVENF GNGILESSKR SAYLATRVER ILQRTTKTLT HQLQQGVFEP GSYEQYFSHA
DRYLNLRGRI DRVDLYEQDG KLYVKVIDYK SGSTSFDLMN LYYGLQLQLG VYLSAAMELM
KEQYPNHEIH PAGVFYYNLD DPIVTKSSSV EEDIEKKLAM NGLVNASKVV VPLLDTSFCG
DEGELAPSTK STVIPVETGK DGTFTKRSSV AKEEELITLT DYIKDLMHRF SEQIMEGKVR
HNPYRAKNRN ACTYCSFQSV CGFDCKVSGF SYRNLKTLNK EEVWNLIKKE DEFFGKDELD
TGATEGN
