ADDB_CARHZ
ID ADDB_CARHZ Reviewed; 1090 AA.
AC Q3AA34;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B;
DE EC=3.1.-.-;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase/nuclease AddB;
GN Name=addB; Synonyms=rexB; OrderedLocusNames=CHY_2187;
OS Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS Z-2901).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Carboxydothermus.
OX NCBI_TaxID=246194;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT "Life in hot carbon monoxide: the complete genome sequence of
RT Carboxydothermus hydrogenoformans Z-2901.";
RL PLoS Genet. 1:563-574(2005).
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 (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CP000141; ABB14962.1; -; Genomic_DNA.
DR RefSeq; WP_011345073.1; NC_007503.1.
DR AlphaFoldDB; Q3AA34; -.
DR SMR; Q3AA34; -.
DR STRING; 246194.CHY_2187; -.
DR EnsemblBacteria; ABB14962; ABB14962; CHY_2187.
DR KEGG; chy:CHY_2187; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000002706; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 4.
DR Gene3D; 3.90.320.10; -; 1.
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; 2.
DR Pfam; PF12705; PDDEXK_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; DNA damage; DNA repair; Exonuclease; Helicase;
KW Hydrolase; Iron; Iron-sulfur; Metal-binding; Nuclease; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1090
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379363"
FT DOMAIN 1..275
FT /note="UvrD-like helicase ATP-binding"
FT DOMAIN 256..518
FT /note="UvrD-like helicase C-terminal"
FT BINDING 7..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 719
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 1035
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 1038
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 1044
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1090 AA; 124203 MW; 9A7D35F43AB54763 CRC64;
MLTIVRGPVG SGKSRYCREE IIKVLKEAPL GPMVLYIVPE SATFENEYLL NTREDLPGSF
RLQVLSFSRL ALNVVREFKA FFKNSSEFVY QHTLKKILQE NKGKLQILQK AADNPGFIED
LLKLFKEFRR YRVKPENLEK ASSEIENWML QQKLKDVYLL YKLYLEKFGE EYTSEGLLEK
FLEYAPKSKF LAGAKVFIDG FYTFTPLELE VIKTLLKTCA EVTVTLPTEY DPGIFNRLYS
EALNLGIKVK ELKLEKIERY RASELLHLAQ NYYPLLPDPY SGSLENLSLI AAANPLEEME
KAARIIRYLA KFKGYKLSDI LVLIPEDGYY ISNIKTVFNE YGLPVYVDKG LAFDHHGLYF
LLKGVLGEFN REAAINCLKS GLLNLTADEV FALENYLLSR GLDGEKLVLK EAWEDPNSSY
WESWEKGFGE IISFSQILPL INTYREFSQS LKQLLLKIGV PRRISDENGE RFWQAFTNLL
TEIEEVFGAE RLNPTTFAEE LLAYLAKLSL KTIPKGLDQV RAGGSKRYWT GEARAVIILG
AVEGKFPSPP AAGLIFTEEE RAKLKKVGLE LSPLIRQRLK EDNFHVFLAL TRARERVYVS
YPRVSLTGES FTPALLVDWL KKAFPNLKSE EGSYGNETTP QALTRLLSRE MVKVKKNGEL
PFIAQGAFNA LLLSKPELIT KIARAFATNP GKIKLNAGFK EFLPSKTLSV SRLETYYSCP
LKYFLKYLIK AEEREIFTPE ATEIGALLHG AVAEIIKTVR EKGQKLSTLL AEDLKTLVYQ
AFTKAQQEYG EKFLATYRGR YFLNRLYLML FKAIEALAYF EGFTKFTPFG EEIAFGEKER
LKSPVFEVNG EKYTLAGKID RIDVYENNGK TYLRIIDYKT GSISISLDEV VGGINLQLLT
YLLVASENKE LFGENLVPAG AFYFRFQNPM LDEKAEGLSM EELKEEVYKN FRLSGYALKD
EESLKHLDSF YAQNNKFKTV NLRTYKDGRI DNALTPAELE ALFTKIKGLI TEAIFKISAG
EFSAIPYQLK DATGCRYCSY LEVCRLEEQE KQYRVIPRKK DPEVLLALSG GGVGDEKLDS
RTNAGYHLQG
