ID A5N6V7_CLOK5 Unreviewed; 1150 AA.
AC A5N6V7;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B {ECO:0000256|HAMAP-Rule:MF_01452};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01452};
DE EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_01452};
DE AltName: Full=ATP-dependent helicase/nuclease AddB {ECO:0000256|HAMAP-Rule:MF_01452};
DE AltName: Full=DNA 3'-5' helicase AddB {ECO:0000256|HAMAP-Rule:MF_01452};
GN Name=addB {ECO:0000256|HAMAP-Rule:MF_01452,
GN ECO:0000313|EMBL:EDK33038.1};
GN OrderedLocusNames=CKL_0996 {ECO:0000313|EMBL:EDK33038.1};
OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK33038.1, ECO:0000313|Proteomes:UP000002411};
RN [1] {ECO:0000313|EMBL:EDK33038.1, ECO:0000313|Proteomes:UP000002411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680
RC {ECO:0000313|Proteomes:UP000002411};
RX PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA Hagemeier C., Thauer R.K., Gottschalk G.;
RT "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT metabolic features.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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:0000256|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=5.6.2.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01452};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01452};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01452};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01452};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_01452};
CC -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000256|HAMAP-
CC Rule:MF_01452}.
CC -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01452}.
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DR EMBL; CP000673; EDK33038.1; -; Genomic_DNA.
DR RefSeq; WP_012101368.1; NC_009706.1.
DR AlphaFoldDB; A5N6V7; -.
DR SMR; A5N6V7; -.
DR STRING; 431943.CKL_0996; -.
DR KEGG; ckl:CKL_0996; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR Proteomes; UP000002411; 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-UniRule.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; 3.90.320.10; -; 1.
DR Gene3D; 6.10.140.1030; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR HAMAP; MF_01452; AddB_type1; 1.
DR InterPro; IPR049035; ADDB_N.
DR InterPro; IPR014140; DNA_helicase_suAddB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR NCBIfam; TIGR02773; addB_Gpos; 1.
DR PANTHER; PTHR30591; RECBCD ENZYME SUBUNIT RECC; 1.
DR PANTHER; PTHR30591:SF1; RECBCD ENZYME SUBUNIT RECC; 1.
DR Pfam; PF21445; ADDB_N; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01452};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01452};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01452};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01452};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01452};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01452};
KW Iron {ECO:0000256|HAMAP-Rule:MF_01452};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01452};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01452};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01452};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01452};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01452}; Reference proteome {ECO:0000313|Proteomes:UP000002411}.
FT DOMAIN 5..289
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21445"
FT DOMAIN 778..1119
FT /note="PD-(D/E)XK endonuclease-like"
FT /evidence="ECO:0000259|Pfam:PF12705"
FT BINDING 789
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1112
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1118
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1150 AA; 133639 MW; F9EE18D0E9A5A5CC CRC64;
MSIRFIYGRA GSGKSHYCLE DIKRRIQEVN DRNLILLVPE QFSFQAEKNL IKSIGEKGTL
KAQVLSFRRM AEKVFDEVGG GIKKYINDAG KNILLYKIIE ENKNKLKVYK TSAKKQGFVN
LVSDIIGEFK KYNISPEFLK ENLDSIENKS LKNKLEDIGM LFLEFQNRLS KNYIDLEDTL
HILCEKLDKS IIFKNSEVWI DEFSTFTPQE YSIIEKIMCS AYRVNITLCM DALGEYSERE
SIDLFLPIKI TERNILQIAE KNNIIYQKPV NLRCSPCYRF KNSTALQHLQ HSLFSYPYKN
YEKSTEDINI FKALNKYTEI DYIARDIVKA CRDKNLRFKD MAVVTGDLDE YENLIKAVFN
QYDIPYFIDK KREIIHNQIV ILIISAVEIL AKNWSYESVF RYLKTGLLDL EFDDIDILEN
YVLANGIRGR QWLDTKPWSF KINYGNFKED DSEEEQEYLN KINCIRDKVR EPILKLSNDI
KGKKKGRHIC EELYNFLCEL KIPEKVEELI IEFRNTDRLD KANEYSQIWD IVVDVLDQIV
DVLGEQSFGM EIFNEALEIG FSQYEIGVIP PALDQVLVSN ITRIKSYNIS ALYIAGVNDG
IFPVTISPEG IFTDQDRDEL KQNGLEIAPN TRSRAFEEQF LIYATLTIVD KYLTLTYSMS
DEEGKAKRPS VVISMIKKIF PKLQEKSNLL DASGYEGGIE AVNSPKVTFN MLISNIRRNL
GHRENINSLW IDVYRWYREH EIWNKRLDTV LGAFYYNNEI KISDLVKIRR LYGKHLNMSV
SRLEKFAQCP FGYFVQYGLK VKDRKMYSLS APDLGSFMHG ILERFSIGLK QKSLTWENVD
ERCCEENIND LVDNVLYDNP NSILNSSKKY KHVTDKLKKT LTRSVWLIAQ HMKKGRFIPR
AYELVFGEIG DFPPISIELD SGEKVSLTGK VDRVDTAKED IITYIRIVDY KSGTREFKLS
DVYYGFQLQL LIYLDAILTE FDKMTKGKSI PAGLLYFKLE DPIVRTKENI PDHEIEDRIT
KSLKMNGLLL NDVNVIRQMD TSMEKSSDII SVSIKKDGNL SKSKSSLATR KQFEILRKYV
RSTIADLCKK ILTGNIEVTP YKNKTKNGCS YCEYSAICQF DTSIKGNKYR IIEDKSDEEI
WKHIENKVQE
//
