ID A0A433RTT1_9BACL Unreviewed; 1172 AA.
AC A0A433RTT1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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 ORFNames=QI30_11515 {ECO:0000313|EMBL:RUS55546.1};
OS Kurthia sp. 3B1D.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX NCBI_TaxID=1562256 {ECO:0000313|EMBL:RUS55546.1, ECO:0000313|Proteomes:UP000288623};
RN [1] {ECO:0000313|EMBL:RUS55546.1, ECO:0000313|Proteomes:UP000288623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3B1D {ECO:0000313|EMBL:RUS55546.1,
RC ECO:0000313|Proteomes:UP000288623};
RA Lawson J.N., Gonzalez J.E., Rinauldi L., Xuan Z., Firman A., Shaddox L.,
RA Trudeau A., Shah S., Reiman D.;
RT "Genome sequence and analysis of novel Kurthia sp.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00034618, ECO:0000256|HAMAP-
CC 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUS55546.1}.
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DR EMBL; JTFC01000031; RUS55546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433RTT1; -.
DR OrthoDB; 9758506at2; -.
DR Proteomes; UP000288623; Unassembled WGS sequence.
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; 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; IPR014017; DNA_helicase_UvrD-like_C.
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.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, 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}; Helicase {ECO:0000313|EMBL:RUS55546.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01452};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01452};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01452};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01452};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW 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:UP000288623}.
FT DOMAIN 277..594
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 800
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1125
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1128
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
FT BINDING 1134
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1172 AA; 135430 MW; D79F41856C4B817D CRC64;
MALRVISGRA GVGKTHFMER EIMDAVNKEP LGAPIFMVVP DQMSFSSERN LTWMAGESRG
TIRVQVTSFK RLAWRILQEA GGISRQELNG FGYRMLLKSI LEENKDKLRL FGKAADKRGF
TEEMEQLLKE LSRYSVNGDK MALIQREFDQ LDAPRTLQDK VHDIQLIQAA VEERLGTTYV
DSEGYLPLLQ QKLVHSTMIR EASIYIDGFM SFTTQEFELV QELLATAKNV TIALPFEQEF
DADDEQALFY EPANTARRLK DVAFSNGIEV KPDVHLTQTM RYSNDTLQTI ESQFEHYHPK
QAKTTAHLDI AAAVNPHAEI HEVARKIRTL SHEGIAYNEM AIIYRQAEQY DPLLSTIFPQ
YDIPFFISQK KPMLHHPLIE FSRSILESIQ TDWKYEPIFR AIKTDLFFPL HADKKIWRER
ADRLENFVMA QGIYGERWFD DIRWVYKKYR GLEFFTTKQT DEERAFQQEI EAVRVLVREP
LQQLQQQLEQ AHTGRAYAEI LYTFIDELAI FAKLQELKDY ENAHGKLLAA TEHEQAWNEW
VNVLDQFVEM FGDVELTLDE FIEILDEGLD SLEFSRIPPS IDEVTVVTAD LARLMNMKAV
FVIGMNEGVY PQRIDREGLL ADTEREWFER TGNEIAPTSR ERLLEENFIA YRAFTVASHE
LFISYTMADS EGKSVLPSTY LKKIHDLVPG LEERYIYMSP EESLDTEDDW HYIAHPRTAL
AYLMIQLRKQ YYDQDALTPA WAALKEYYQN DPYWEDVLKR LMRPLITHNR AENLTPEYTR
ELYGKDIISS VSRIEKYYSC PFSHFTTYGL HLEERKEYRL ETPTIGDLFH AALKYISEKT
EALGLTWGQL SVEECRKLSQ EAVAEIVPML YHKILLSTAR YRYIMRKLTQ IVERTMLSLA
NHAKTTGFKP IAIEAAFGPG QGDMLPPLVI QLDNEHKLQM RGRIDRIDAT EVNNKPYIRV
IDYKSSAQKL DLNDVYHGLS LQMLTYLDVA MTNSSEWLPL HAEAGGVLYI HVHNPMLKAD
AVLSNDAQEQ EVLKDFKMKG LLLDNRDVLV EMDENLADNG GRSHIIPAYL KKDGSTSASW
SSVINEKDMG DLQKFVRQKH KIAGQGILKG DTSISPYRMK QKTACEYCSY KSVCQFDVND
AHQQYRALPI DKPEVVIEKI RKEAVADDNI TD
//
