ADDB_OCEIH
ID ADDB_OCEIH Reviewed; 1166 AA.
AC Q8ERW6;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, 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 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}; OrderedLocusNames=OB1181;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC13137.1; -; Genomic_DNA.
DR RefSeq; WP_011065580.1; NC_004193.1.
DR AlphaFoldDB; Q8ERW6; -.
DR SMR; Q8ERW6; -.
DR STRING; 221109.22776863; -.
DR EnsemblBacteria; BAC13137; BAC13137; BAC13137.
DR KEGG; oih:OB1181; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR OrthoDB; 1283891at2; -.
DR PhylomeDB; Q8ERW6; -.
DR Proteomes; UP000000822; 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; -; 3.
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_0000379202"
FT DOMAIN 1..290
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 283..588
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 802
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1123
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1126
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1132
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1166 AA; 134503 MW; B14141F0648D12A9 CRC64;
MGMRFILGRS GTNKSEVILK EIKQKISTNP IGPSIFYIVP DQMTFQQEVA LFSDSETNGS
IRAQIVSFSR LAWRVLQETG GGTKQFISSV GIQMMLRKII EEKQGDWNAF QKALKKQGFL
GQLETMLTEL KRYEITPDDL RMQQSHLTDF VHQSPSEQGL TRKLSDLIYI YETFIYALQG
TYVDSEDQLQ LLIQQIKQSS ILNNADIYID GFHSFTPQEQ SVLTELMKTS NSITVALTLD
DPWKEDASEL DLFYQPSQTY HVLKQLAWEA GVPVEDPIIL DTLEGNFQNR PYFAHMEKYF
DSRPAPAYEG EVPIEIFEAV HPRAEVEGIA QQVLELIRDN RYRYRDIALL IRQPEVYHDL
IETIFNDYEL PVFIDEKRPM LHHPLIELIR SILEVVQGNW RNDAIFRVLK TGLIPSADDE
FPLTMDSIDQ LENYVIEFGI RSRHQWIGEN KWKYQRFRGF DSSAQTDRER ELQESMNRYR
DQVISAIATV DEQLRAATTV KDLCIAMYQW LEELKIPDQL EVTRKYYDDQ GLPEKGREQE
QVWDAVIQLF DEMVEIAGEE KMDLSVFQVA LDAGIETLQF SHVPPSMDHI IVGTIDRSRM
SNIRCAFLLG VNEGIWPMKP TSDGMIDEAE RLLLEQNGLK LADTSERQLL DDWFYMYLAF
TVAKDRLKIS YLLSDEEGKA KMPSQLIHRV EELFPATKNH ILLQDPEDES NTRRFVSTEL
KSRSALTAQL AKFKKGYPID PIWWEVYQWY VEHHPQGGTT HRVLQGLHYE NKPESLQKDT
VEQLYPKRIQ ASVSRLETYY RCSYQHFAKY SLNLEERRTY KLDAPDIGQL FHEALKKITE
WIHAEGNDFS ALTKSQSSHY ANRAVTELSP VLQHQILHSS NRYAYIQKKL EEVIARATFV
LGEQARLSHF SPVGLELGFG DGNNQIPSLS MLLENGYELV LRGRIDRVDK AELENNLYLR
IIDYKSSSKG LDLTEVYYGI ALQMLAYLDV VLTHSEKWLG QQADPAGVLY FHVHNPMISA
KGSMTEADIE EELFKQYKMQ GLLLSNEEIV KMMDSSLETG SSQIVPAALK KNGGFYSYSK
IADQSTFETL QNHIHQLLKS AGIDITNGSV DVNPYQHKQQ KACTYCPFHS VCQFDPVLEE
NNYRKFADIK ENDLLQLFER EGENNG
