ADDB_CLOPS
ID ADDB_CLOPS Reviewed; 1158 AA.
AC Q0SWW7;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=CPR_0024;
OS Clostridium perfringens (strain SM101 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=289380;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM101 / Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(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; CP000312; ABG86087.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0SWW7; -.
DR SMR; Q0SWW7; -.
DR EnsemblBacteria; ABG86087; ABG86087; CPR_0024.
DR KEGG; cpr:CPR_0024; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000001824; 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.
FT CHAIN 1..1158
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379182"
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; 134336 MW; 6BDE0D798B11A74B CRC64;
MGLKIIYGRA GTGKSTFCIN QIKKKINNSP TNKLILLVPE QFTFQTENKV LNAIGERYVL
NAEVLSFKRL AHNVFNECGG ATRTIMGDAG KSMLIFKVLE DLGDNMTVFK NASRQKGFID
IASKTITEFK KYNVNNEVLD LTINEIEDEN LKMKMEELKD VFNEFNSRLH EGYVDEEDQL
LLLNEKLDGC SLYDGAEIWI DEFSSFTPNQ LSVIGKLLKK AKSVNITLSI DEVNSPKVES
DLFVATKNTE KRLMNLIQEE GIAFNGYINL NEDIPYRFKE NKELAHIERQ LYAYPFKQYR
GENNSLRLYR ANNNYDEIEF VAKDILRLVR EKQYRFKDIS VICREVDNYE KVISAIFAEY
EIPYYIDKKI DIASNPLIVF INSAVDIISK NWTYESMFKY LKTGLIKEFR GIEGAELIDE
LENYVLAYGI KGKKWMEEWV NYSSSILKEE EISEENKQRL ERLNDIRETI VTPLDEFNKE
CKGKKTLKEF AIILYEFLDS KLNIMDTIDK YVEYFKENDM AIEAKEYSEV RDIFIDVLEQ
AVDVLGNEVM DLDEFMKVLN IGLSQYEMGL IPVALDQVNI GDITRIKSRG TKALYIIGVN
DGVLPSASKE EGILSDNDRE ILLEKGISLA SDTRTKIFEE QFLVYTAFTI AEEYLVVTYP
LADFEGKSQR PSIIVHRLKK ILPNVKEESE GFKLVNDKYD KISAKIPTLN ELMIAIRKNY
DGAEIDDYWK YVYDWYLREP KWKERIEYVR KGLEYTNLEN NISKEKAKKL YEDNKNKISL
SVSRLERYAQ CPFAYYIQYG LKAKDRKIYE FTAPDLGSFM HEILDEFTNE IKEKDLKWSD
LSKENCKNII NSLVDNQVKN NKSSILNSSK RYSYFTDRFK RILTKSVMVI SEQMKRSDFE
IYKNELAFGF SKDVNSIKLD LPSGESFYLN GRIDRIDKLN LDGETYLRII DYKTGSKKFD
LNKFYNGLQM QLLVYLDALI NNSENIVENQ AMPGAILYFR IDDPILKSKG DLTEEEIKSE
ILKELKLEGL LLDDVKVVKA MDNTLEPGTH SLIIPANMKK AGDLGKNKAL ITMEQFELLR
KYVNEKMVEI CQNMIEGKID IEPCKENKNI VCDYCNYSHI CQFDSSLEDN RYKVIPKKKD
EDIWKSINEK VGGEVNGD
