ADDB_CLOAB
ID ADDB_CLOAB Reviewed; 1153 AA.
AC Q97GV2;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=CA_C2263;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK80220.1; -; Genomic_DNA.
DR PIR; A97179; A97179.
DR RefSeq; NP_348880.1; NC_003030.1.
DR RefSeq; WP_010965561.1; NC_003030.1.
DR AlphaFoldDB; Q97GV2; -.
DR SMR; Q97GV2; -.
DR STRING; 272562.CA_C2263; -.
DR PRIDE; Q97GV2; -.
DR EnsemblBacteria; AAK80220; AAK80220; CA_C2263.
DR GeneID; 44998741; -.
DR KEGG; cac:CA_C2263; -.
DR PATRIC; fig|272562.8.peg.2463; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR OrthoDB; 1283891at2; -.
DR Proteomes; UP000000814; 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..1153
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379167"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 786
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1104
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1107
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1113
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1153 AA; 133688 MW; EE7D3A5EE4C1975D CRC64;
MSLRFIYGRA GSGKSQFCIE SINTRIEKGG DKPLILIVPE QFSFQSEKNI LDLIGEKSIN
RVKVISFKRL AYRIFDEVGG IAREHMNSSG KSMLFYHIMN TLKSEFRVFA LSARQKGFVN
TIADTVSEFK KYELTTEVLR DTIDEIEDEE LKNKLHDLSL IYDEFNRLLY KNYIDPDDDL
TILKDKIKQS TVLQGAEIWL DEFSSFIPQQ YGIIEELLKK CSRVNITLTM DYDNASKDND
IFSVTQNTEK RLLKLAENNN ISIEKPINLN GRPFYRFKNS PELSFLEKNL YSFPYEIYKK
GPDKIEIFKT SNLYTEVEKI ARNIIEFVRE DNVRFSDIAV VTGDLGSYEK TVSVIFKEYR
IPFFIDRNKD IEDNTLIILI KSIIDIFVKN WSYETVFRYL KTGFADIEPD EIDILENYVL
AAGIKGKKKW TEEEWTYNVY GDALEGDISE ESKEKLSKVN EIKNRFLRPI LNFRERVLRR
NNVAEICRAL FEFLYDINVP EAVEKMVNEF RESGRQILAN EYSQIWNIII ELMDQLVEVM
GNEKVNLEQF SRILFIGIKE HKMGLIPSSL DQVLVGSIDR LKSHAIKILY IIGVNDGVFP
SAAMEEGILS DRDREILNSK GVELAKDTKT QAMEQRFLVY TAITNSKEYL FLSYPIADYE
GKTLRPSLIV NRVKTLFPKI VEKSDVIKIE NDEESMKLIS ATVPTFNEMI SSFRKEIDGE
GEVSSIWHDV YRWYSKSDEW TGKCNNMFKA ISYTNQVDYI SEEKALKLYG GSLKMSVSRL
EKYIECPFSY YVQYGLNIKD RKIFSLTPPD LGSFMHKVID RFCETIKEEN IDWNEVNDHI
CEEKIYKIVD QEIEGRGGSI LNSSPRYSYI ALRLKRILKR TVRIVAEQFK RGSFKPVGYE
VSFENGGSYP PITVGLNDGS EVVLTGRIDR IDMMEKDGST YIRIVDYKSG NKIFKLSDVY
YGFDIQLLLY LNAILENENL DEEDKVLPGA ILYFTMDDPI IKGKNNLTDE QIREEIMKSL
KMKGLLLSDP DVIKEMDREM EGSSIIIPAS IKKDGTLGRS SAATKEQFDI LIEHVRNLVV
KNCENLLMGD IRIKPYKKGK EKPCDYCMYS SICRFDTMFD GNNYRYVKEK SDEEVWKLIE
REMSEEGDER GED
