ADDB_GEOKA
ID ADDB_GEOKA Reviewed; 1167 AA.
AC Q5L264;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, 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=GK0681;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD74966.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5L264; -.
DR SMR; Q5L264; -.
DR STRING; 235909.GK0681; -.
DR PRIDE; Q5L264; -.
DR EnsemblBacteria; BAD74966; BAD74966; GK0681.
DR KEGG; gka:GK0681; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000001172; 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; -; 4.
DR HAMAP; MF_01452; AddB_type1; 1.
DR InterPro; IPR014140; DNA_helicase_suAddB.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
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.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 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..1167
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379191"
FT DOMAIN 1..359
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 282..588
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 804
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1126
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1129
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1135
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1167 AA; 134138 MW; A24BB84B06849D10 CRC64;
MSLRFLLGRS GSGKTAVCLE EIRRQLQEDP KGRAIVYLVP EQMTFQCEYA LIHTEGVGGM
IRAQVFSFTR LAWRVLQETG GMTRYHIHDV GVQMMIRKII EQRKQELKLF GRAADKHGFI
EQLNEMITEC KRYCLTPGEL RRHAKAFEDG PDQPGRRLLA DKLSDVALVY EELERSLIGH
YLDSEDYLRL LAEHIPRSSY LRDADIYIDG FHHFAPQEYM IIEQLLRHCR RVTVCLTIDR
PYDDGMPDEL HLFYLPAQTY RQLRELALSN DIAIEEPIVL SANRRHEDRA LVHLEAQFHR
RPLLPYGAKT DAVHLYEASN RRAEIEAVAR EIIRLVRDEG ARYRDIALII RQTEAYRDLV
KTVFFDFGIP YFMDEKEPMH HHPLIELVRA ALETVVTRWR YEAVFRAVKT DLLFPTDGDL
HMWREAADKL ENYVLAYGIK GDKWTNNERW AYRRYQALDG LNVPQTDEER QFEDMLNEWR
EALAAPLRRL ERRLRRAEDG RGFCMALYLF LEELQIPKKL EKMSAQAEAD GRLVEARQHE
QAWNAVVDLL DQYVEMLGTE SLPLAEFVKI IEAGLDRLEF SLVPPAMDQV IVAQLDRSRL
IDIKYAFVIG ANDGVIPAKV KEDGLMAEVE REQLRELGVA LAPGGREQLF YDPFFVYLAL
VCPSRRLYVT YPLADGEGKA LMPSPLIKQL TELFPHAPVH LCGNDPFDAP AEKAEAFVTA
PRATQTYLIS QLRAWKRNYG IDPLWWDVYN TFIGHRDWKE QVRHAVSALF YTNGATPLKK
QWSQRLYGKK IQASVSRMEQ FQKCPYAHFA SHGLRLKERN VFRLEAPDVG QLFHAAIKQI
ADRLREQHLD WRELSRPDCE RLSAEAVERI APLIQQQVLS SSHRYEYMKR KLKHVVARTT
HVLSEHARAS GFVPIGLELS FGPNGDLPPL RFRLPDGTVM ELVGRIDRVD KAESSQGVLL
RIIDYKSSAK TLDLTEVYYG LALQMLTYLD IVLTYAEQLV GQPALPAGVL YFHIHNPIVQ
AKQWVDDEVE MAKKLLEPFR MRGLLLADVE AIRLMDGRTE DGQWSLIVPA QLTKSGSIHS
RSSVASPSDF AALRQHVRRL FIDIGGQIAD GVVSIAPYKL KDKTACEFCV FKPVCQFDEA
LSGNEYRKLA PQTKEAVIEK LAEGKEG
