ADDB_CLOD6
ID ADDB_CLOD6 Reviewed; 1155 AA.
AC Q18AP0;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=CD630_10400;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(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; AM180355; CAJ67881.1; -; Genomic_DNA.
DR RefSeq; WP_011861078.1; NZ_CP010905.2.
DR RefSeq; YP_001087521.1; NC_009089.1.
DR AlphaFoldDB; Q18AP0; -.
DR SMR; Q18AP0; -.
DR STRING; 272563.CD630_10400; -.
DR PRIDE; Q18AP0; -.
DR EnsemblBacteria; CAJ67881; CAJ67881; CD630_10400.
DR KEGG; cdf:CD630_10400; -.
DR KEGG; pdc:CDIF630_01180; -.
DR PATRIC; fig|272563.120.peg.1080; -.
DR eggNOG; COG3857; Bacteria.
DR OMA; DRLENYV; -.
DR PhylomeDB; Q18AP0; -.
DR BioCyc; PDIF272563:G12WB-1159-MON; -.
DR Proteomes; UP000001978; 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 PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR SUPFAM; SSF52540; SSF52540; 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..1155
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379177"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 793
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 1118
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1155 AA; 133531 MW; 6D80BB03011E8823 CRC64;
MGLRFVLGRS GSGKSTYILD EIKKEAQKNE TTSIILLVPE QYTFEAENRV SKLFLGKEKD
KYLRVRVLSF KTLSNIVFSQ VGGLTDVNIN SSGKAMMVYR AIEDVSEELN VFSKSKSQSG
FVSSITDMIS EMKQYNISPE MLENISGELD NETLSLKLKD ISKIYNSFEG KLHENYVDAQ
DMLTSLTSKI ELSSYLDGAC VYIDEFTGFT PNQYNVIKSI LNKSKSVNIS LTVDDINYIG
YSKSDMFSRT KFTYSKLTQL CNEEGIKILP QVNLNTGVIK RFEKVKELQH LERFYNAYPY
KIYSNPTENI KIKEFNNLYS EVEEIAREIV HLVRDKNVRY RDITIATRDL NRYDFLVHSI
FNEYNIPNFI DKKREAKSNP IVILIISALE MKNRRYGYET MFRYLKSGLI GIDNDDINLL
ENYVLANGIK GKKWFDEKWD YRITQSLSGQ ESEFELELKE KINEIKNRVL EPIVILQEKL
RGKNRVKEIC RYIYEFLLDI NMPETIESLI VNFKDKGELD VANQYSQVWD IVVDILDQMV
ELMGDEIISL EKFIKLITLG FDEYELGLVP PSIDQVLVSS VDRMKNPDTK YLYLVGTTDG
VFPLITKDSG ILSDNDRESL GNKGIEVDID SKTRSFEEQF LVYKALTSTS KNLTITYPIS
DHEGKTLRPS IIISRLKKIF PNIENKSYLV EENKNTDKDI LKKITVKSPT FNELINVIKN
YDSDGYNTEE INSIWLDIYR YYLKDEIYSS ITKKVIKGLS YTNQVHKIEE KKIRSLYKSN
SLSISRLEKY AECPFAYFIQ YGLKAKKRKE YSFTPPDLGT FIHNILDRFS KELLQDNLTW
RDIDEKYIEL KIGIIVDEII LKIPGYILNS SERYKYLAYR LKNMLTTAIT IISQQIKQGS
FEPIDYEVKF GDNGKYPPIK MVLENGQEVS LIGQIDRVDE FEEGENKYIR IIDYKSGNKS
ISLTEIYYGL QLQLLVYLDA ILESAKDEDM NINPAAILYC RINNPIAKFN EDKDDEEIQE
AILKELRMKG LVVKDSHIVK EMDKSLIDGE RKNSLVIPVG LTKDGNVGKS TSAISYEDFK
LLRKYVRHAI KDLCEEMLSG EIRIAPYKHK DGTSCDFCDY SAICQFDSTI KDNKYKNLNN
KSNEEIIKMM KGDVN
