ADDB_CLONN
ID ADDB_CLONN Reviewed; 1134 AA.
AC A0PY66;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=NT01CX_1235;
OS Clostridium novyi (strain NT).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=386415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NT;
RX PubMed=17115055; DOI=10.1038/nbt1256;
RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA Zhou S.;
RT "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT NT.";
RL Nat. Biotechnol. 24:1573-1580(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; CP000382; ABK61063.1; -; Genomic_DNA.
DR RefSeq; WP_011721326.1; NC_008593.1.
DR AlphaFoldDB; A0PY66; -.
DR SMR; A0PY66; -.
DR STRING; 386415.NT01CX_1235; -.
DR PRIDE; A0PY66; -.
DR EnsemblBacteria; ABK61063; ABK61063; NT01CX_1235.
DR KEGG; cno:NT01CX_1235; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR OrthoDB; 1283891at2; -.
DR Proteomes; UP000008220; 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; 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..1134
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379179"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 771
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1089
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 1098
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1134 AA; 131908 MW; BE241D29577FB3D0 CRC64;
MSFRFIYGRA GSGKSKFCID DIEKRLQEDT NKQLILIVPE QFSFQAEKSV VEKVKGTGIT
NVKVTSFERI AYDVFNEVGG STHKIINSSG KLMLIFNIIN NLKDELKVFA TAANQEGFVN
NISDIITELK RYDVTATELR ATLNLIEDEF LKDKINDISY IFEQFQESLH KNYIDSEDEL
TLLYRKIDTS KMFDGAEVWI DEFSSFTPQQ YKILEKLMEK ASRVNITLCM DYYRVIDGTD
VFAPTKRTEE KLREILKEKD VKLDKPIILN NDDVNRFKDS SELKYLEENY FKYPYKPYDK
TTDDIKIIRA LNPYSEVENI AKEIAKISME SNIRYRDIAV ITRDLEGYEK IVKTIFDEYE
IPYFIDKKKE IDDNPLIVLI TSVIEIFNKS WSYEAMFRYL KTGLSNVSKE EVDLLENYVL
AYGIRGKKKW QSPWEYGNEN ILEKINEIRI KVSEPLIKFS SKLKGKSKAD EICSAVYNFL
CSIGVNETIE KWVYKFKNEG NQALAKEYSQ IWNMVIELLD QVVEVFKEEE LQLKDFVKIL
SLGFKDYKMG LIPPSLDQVL VSDVERVRTH EIKLLYIIGV NDGIFPAVSK DEGILSDSDR
GSLKKIGIEI AEDTKSKAFE EQYLIYRTLT TTQKYLRICY SIADYEGKAL RPSIIVSRFK
SLFPKIAEES DNIAMDYEEE NIDLISREIP TFNNLVSVLR REDNKVKVSP FWSDVYKWYS
ENPRWKETLD TVFSAISYTN AVDDISEEKI RKMYGNKLYL TVSRLEKYAQ CPFGYYIKYG
LKAKERKIFA LTPPDLGTFM HNVIDEFSEV VDKSGFKWYE IEDKWCKDTV SEIVDRKAEE
SAGGIFTSSA RYKYFTERLK RVLIKTILVI IEHLKRSGFQ PIGHEVGFGN DEKYPPIEIE
LSSGEKVKLI GRIDRVDKLD MEKKDYYRII DYKSGNKDFS LSDVYYGLQL QLLTYLDAIL
TNEELKDREE ALPGGVLYLK IDDPIIKGKR NLSEEEIQDE IMKALKMKGL LLADEEVVKE
MDRKIEGNSL IIPARINKDG SLGKSSVGTE EQFRLLREHV KKNLIKACED MLKGDIKIRP
IRSKNADACT YCLYSSICEF DTNFEDNEFK VVQEKKDEEV WELLRKEGEE SWEK
