ADDB_CLOPE
ID ADDB_CLOPE Reviewed; 1158 AA.
AC Q8XPE3;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=CPE0020;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB79726.1; -; Genomic_DNA.
DR RefSeq; WP_011009571.1; NC_003366.1.
DR AlphaFoldDB; Q8XPE3; -.
DR SMR; Q8XPE3; -.
DR STRING; 195102.gene:10489248; -.
DR EnsemblBacteria; BAB79726; BAB79726; BAB79726.
DR KEGG; cpe:CPE0020; -.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000000818; 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; 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 InterPro; IPR011335; Restrct_endonuc-II-like.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF52980; SSF52980; 1.
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..1158
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379180"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 791
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1112
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1158 AA; 134286 MW; 2B2ECFFCC43EAE38 CRC64;
MGLKIIYGRA GTGKSTFCIN QIKKKINNSP NNKLILLVPE QFTFQTENKV LSAIGERYVL
NAEVLSFKRL AHNVFNECGG ATRTIMGDAG KSMLIFKVLE DLGDNMTVFK NASRQKGFID
IASKTITEFK KYNVNNEVLD LTINEIEDEN LKMKMEELKD VFNEFNSRLH EGYVDEEDQL
LLLNEKLDGC SLYDGAEIWI DEFSSFTPNQ LSVIGKLLKR AKSVNITLSI DEVNSLKGES
DLFVATKNTE KRLMNLIQEE GIAFSGYINL NEDIPYRFKE NKELAHIERQ LYAYPFKQYR
GKNNSLRLYR ANNNYDEIEF VAKDILRLVR EKQYRFKDIS VICRDVDNYE KVVSAIFSEY
EIPYYIDKKI DIASNPLIVF INSAVDIISK NWTYESMFKY LKTGLIKEFR GIEGAELIDE
LENYVLAYGI KGKKWMEEWV NYSSSILKEE EISEENKQRL ERLNDIRETI VTPLDEFNKQ
CKGKKTLKEF ATILYEFLDS KLDIMDTLDK YVDYFKENDM AIEAKEYSEV RDIFIDVLEQ
AVDVLGNEVM DLNEFMKVLN IGLSQYEMGL IPVALDQVNI GDITRIKSRG TKALYIIGVN
DGVLPSASKE EGILSDNDRE ILLEKGISLA SDTRTKIFEE QFLVYTAFTI AEEYLVVTYP
LADFEGKSQR PSIIVHRLKK ILPNVKEESE GFKLVDDKYE KISAKIPTLN ELMIAIRKNY
DGAEIEDYWK YVYDWYLREP KWKERIEYVR KGLEYTNLEN NISKEKAKKL YEDNKNKISL
SVSRLERYAQ CPFAYYIQYG LKAKDRKIYE FTAPDLGSFM HEILDEFTNE IKEKDLKWSD
LSKENCRNII NSLVDNQVKN NKSSILNSSK RYSYFTDRFK RILTKSVMVI SEQMKRSDFE
IYKNELAFGF SKDVNSIKLD LPSGESFYLN GRIDRVDKLN LDGETYLRII DYKTGSKKFD
LNKFYNGLQM QLLVYLDALI NNSENIVENQ AMPGAILYFR IDDPILKSKG DLTEEEIKSE
VLKELKLEGL LLDDVKVVKA MDNTLEPGTH SLIIPANMKK AGDLGKNKAL ITMEQFELLR
KYVNEKMVEI CQNMIEGKID IEPCKENKNI VCDYCNYSHI CQFDSSLEDN RYKVIPKKKD
EDIWKSINEK VGGEVNGD
