ID ADDB_BACVZ Reviewed; 1166 AA.
AC A7Z367;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 110.
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 AltName: Full=ATP-dependent helicase/nuclease subunit AddB {ECO:0000255|HAMAP-Rule:MF_01452};
GN Name=addB {ECO:0000255|HAMAP-Rule:MF_01452}; OrderedLocusNames=RBAM_010790;
OS Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS (Bacillus amyloliquefaciens subsp. plantarum).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=326423;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX PubMed=17704766; DOI=10.1038/nbt1325;
RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA Strittmatter A., Gottschalk G., Borriss R.;
RT "Comparative analysis of the complete genome sequence of the plant growth-
RT promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL Nat. Biotechnol. 25:1007-1014(2007).
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 subunit has 5' -> 3'
CC nuclease activity but not helicase activity. {ECO:0000255|HAMAP-
CC Rule:MF_01452}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
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 -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000255|HAMAP-
CC Rule:MF_01452}.
CC -!- MISCELLANEOUS: Despite having conserved helicase domains, this subunit
CC does not have helicase activity. {ECO:0000255|HAMAP-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; CP000560; ABS73443.1; -; Genomic_DNA.
DR RefSeq; WP_012117250.1; NC_009725.2.
DR AlphaFoldDB; A7Z367; -.
DR SMR; A7Z367; -.
DR KEGG; bay:RBAM_010790; -.
DR HOGENOM; CLU_007838_0_0_9; -.
DR Proteomes; UP000001120; 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; 3.
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; 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; DNA-binding; Exonuclease;
KW Helicase; Hydrolase; Iron; Iron-sulfur; Metal-binding; Nuclease;
KW Nucleotide-binding.
FT CHAIN 1..1166
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379151"
FT DOMAIN 1..390
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 281..586
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 801
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1130
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1166 AA; 133295 MW; F24722658F895BA9 CRC64;
MGVEFLVGRS GSGKTRLIID SIQDELRREP FGKPIIFLVP DQMTFLMEYE LAKTPDIGGM
IRAQVFSFSR LAWRVLQHTG GMNRPFVTTT GVQMLLRKLI EEHKHEFKVY QKASDKTGFT
EQVERMLTEF KRYCIEPEDV RRMAESGTAS EYRGERMLSE KLHDLGILYQ QMERSLAGHY
LHSEDYLTLL AQQIPLADVV KGAHVYVDGF YQFTPQELRV LEQLIMHAEH VTFSLTADSP
SAEQAPDELD LFRMTGSTYY KLYQTAKELN ADISCKELHG TKRHQHAPEL ACIESQYDVR
PAAAYTGGQE AFTVMQAQNR RAELEGIARE IQSLVRDGGY RYKDMAILIR QPEDYKDLLK
EVFADYGLPY FIDGKASMQH HPLIEFIRSS LDVVKGNWRY EAVFRCAKTE LLFPLDQPEQ
KIREQVDQLE NYCIAYGIKG ERWTSGERFV YRRFVSLDED FAQTDQEIEM EHMLNETKEW
MAAPLVKLQN RMKKAKTVQS MAEALYLFLE DTDVPLKLDR KRQRAEEAGN MIEAQQHGQA
WDAVIQLLEE FAGMMGEDEI SLALFQQMLE TGTESLHFSL IPPALDQVFV GNMDLSRMYG
TSCTFVIGAN DGVLPARPDE NGVLSDDDRE WLKAVGVELS SAGRERLLDE HFLIYMALSS
PSDRLYVSYP IADAEGKTLL PSIVVNRLGE LFPDHQEKLS AADPEQVSEE EQLQYLVNKQ
VAQTYTASQL RLWTREYEIS DVWWSAYNVL MKEPDHRRAK KLFSSLFFRN EAKRLERPVS
RQLYGEHIKG SVSRMEAFNA CQFSHFASHG LQLKERQFFK LDAPDIGQLF HSSLKLISDR
LREQKLEWRD LTKDQCRNFS YEAVERLAPK LQKEILLSSN RHFYVKEKLQ KIVTRVSGIL
SEHAKASGFV PVGLELGFGG SGPLPPLTFT LKNGCTMELV GRIDRVDKAE SSKGLLLRIV
DYKSSDRGLD LAEVYYGLAL QMLTYLDLSI THSEDWLGMK ATPAGVLYFH IHDPMIQASL
PMGLDEIEQE IFKKFKMKGL LLGDREAISL MDTTLEEGRS NIVNAGLKKD GSLRSDSAAV
SEQDFHLLTD HVRRTFEQAG EAITDGLVSI TPYKLKDKTP CTYCAFQSVC QFDESLKENE
YRSLKAEKDG TILDWLKKEA DDDANS
//
