ADDB_BACLD
ID ADDB_BACLD Reviewed; 1166 AA.
AC Q65LK0; Q62WZ1;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
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};
GN OrderedLocusNames=BLi01156, BL01351;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(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; CP000002; AAU22717.1; -; Genomic_DNA.
DR EMBL; AE017333; AAU40064.1; -; Genomic_DNA.
DR RefSeq; WP_009328899.1; NC_006322.1.
DR AlphaFoldDB; Q65LK0; -.
DR SMR; Q65LK0; -.
DR STRING; 279010.BL01351; -.
DR EnsemblBacteria; AAU22717; AAU22717; BL01351.
DR GeneID; 66216710; -.
DR KEGG; bld:BLi01156; -.
DR KEGG; bli:BL01351; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR OrthoDB; 1283891at2; -.
DR BioCyc; BLIC279010:BLI_RS05740-MON; -.
DR Proteomes; UP000000606; 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 Gene3D; 3.90.320.10; -; 1.
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; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
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..1166
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379162"
FT DOMAIN 1..285
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 279..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; 134408 MW; D234A27685429F28 CRC64;
MGAVFLSGRS GSGKTTFILN EIREKLRDEP LGKPIIFLVP DQMTFLMEYE LSKTPDLGGT
IRAQVYSFSR LAWRVLQHTG GMNRPFLTGT GIQMLLRRLI EEHKGEFKVY QNASDKSGFT
EQVERMLTEF KRHCLPPQSI RDMMEGTGKS EYEDERILSD KLHDLYILYS KLEENLENQY
VQSEDYLTLL AEQIPYAEEI RNAAVYVDGF HQFTPQEMSV LEQLMVHAEE ITFSLTADKP
FTANSPNDLH LFRMTGKAYY DLYQKAKELG LDPSEVRLEE TKRHRHHPEL QHLERYFDER
PAKPYPGQTE SLRIMQASNR RTEIEGIARE IHSLIRQGRF RLRDIAVIAR NVEDYKDTIK
EVFKDCELPF FIDGKESMQN HPLIELIRST LDIIKGNWRY EAVFRCVKTE LLFPEGQPKE
RLREQIDQLE NYCIAYGIKG DRWTSKDPFV YRRYASLDED FAKTDKEIET ENMLNELKGW
IVPPIHRLQK RLKKAETVRE MAEAVYLYLE EADVPMKLEQ ERRLAEEGGR IAESRQHEQV
WDAVIQLLDE FVEMMGTERI SFALFQQMIE TGLESLKFAL IPPALDQVFI GNMDLSRMYG
TKCTFLIGVN DGILPARPAD DGVLSDEDRE WLKRNGAQLA ATGREQLLDE NFLIYMTLSS
PSEKLYVSYP IADSEGKTLL PSTVVKRLNE LFPDSEEKML IHEPEQLDDE AQLEFLVNKG
IALSHLAGQL GIWTRQYAIS DVWWSTYNFL MNEPDRIFSQ NILSSLFFRN KVENLNRHVS
RDLYGEHIQG SVSRMETFKA CPFSHFASHG LKLKERQFFK LEAPDIGQLF HSALKLISDR
LHELKLDWRD LTKAQCETLS SDAVERLAPK LQKEILLSSN RHHYVKQKLQ KIIARVSGIL
SEHAKASGFA PVGIELGFGG KGPLPPMRFT LKNGCTMELV GRIDRVDKAE SSKGLLLRIV
DYKSSDKGLD LAEVYYGLAL QMLTYLDLSI THSTDWLGMK ASPAGVLYFH VHDPMIQASV
PLGLDEIEKE IFKKFKMKGL LLGDQEAVKL MDTTLEQGRS NIISAGLKKD GSLRSDSDVV
AEEDFHVLRR HIRRTFQQAG EEITDGKVSI EPYKLKDRTP CTYCSYRSFC QFDESLEENE
YRILKPEKDS VILERLKKED EADGDF
