ADDB_CLOP1
ID ADDB_CLOP1 Reviewed; 1158 AA.
AC Q0TV47;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=CPF_0024;
OS Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS 6125 / NCTC 8237 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC 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; CP000246; ABG82499.1; -; Genomic_DNA.
DR RefSeq; WP_011590030.1; NC_008261.1.
DR AlphaFoldDB; Q0TV47; -.
DR SMR; Q0TV47; -.
DR STRING; 195103.CPF_0024; -.
DR EnsemblBacteria; ABG82499; ABG82499; CPF_0024.
DR GeneID; 29569849; -.
DR KEGG; cpf:CPF_0024; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR OrthoDB; 1283891at2; -.
DR Proteomes; UP000001823; 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_0000379181"
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; 134361 MW; 8D3D1555579ED9A8 CRC64;
MGLKIIYGRA GTGKSTFCIN QIKKKINNSP TNKLILIVPE QFTFQTENKV LNAIGERYVL
NAEVLSFKRL AHNVFNECGG ATRTIMGDAG KSMLIFKVLE DLGDNMTVFK NASRQKGFID
IASKTITEFK KYNVNNEVLD LTINEIEDEN LKMKMEELKD VFNEFNSRLH EGYVDEEDQL
LLLNEKLDGC SLYDGAEIWI DEFSSFTPNQ LSVIGKLLKR AKSVNITLSI DEVNSPKGES
DLFVATKNTE KRLMNLIQEE GIAFNGYINL NEDISYRFKE NKELAHIERQ LYAYPFKQYR
GKNNSLRLYR ANNNYDEIEF VAKDILRLVR EKQYRFKDIS VICRDVDNYE KVVSAIFAEY
EIPYYIDKKI DIASNPLIVF INSAVDIISK NWTYESMFKY LKTGLIKEFR GIEGAELIDE
LENYVLAYGI KGKKWMEEWV NYSSSILKEE EISEEDKQRL ERLNDIRENI VTPLDEFNKQ
CKGKKTLKEF ATILYEFLDS KLDVMDTIDK YVDYFKENDM AIEAKEYYEV RDIFIDVLEQ
AVDVLGNEVM DLNEFMKVLN IGLSQYEMGL IPVALDQVNI GDITRIKSRG TKALYIIGVN
DGVLPSASKE EGILSDNDRE ILLEKGISLA SDTRTKIFEE QFLVYTAFTI AEEYLVVTYP
LADFEGKSQR PSIIVHRLKK ILPNVKEESE GFKLVDDKYE KISAKLPTLN 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
