ID   ADDB_STAAB              Reviewed;        1158 AA.
AC   Q2YWU2;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=SAB0835;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(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 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; AJ938182; CAI80523.1; -; Genomic_DNA.
DR   RefSeq; WP_000172358.1; NC_007622.1.
DR   AlphaFoldDB; Q2YWU2; -.
DR   SMR; Q2YWU2; -.
DR   KEGG; sab:SAB0835; -.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
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   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
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.
FT   CHAIN           1..1158
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379204"
FT   DOMAIN          1..275
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   DOMAIN          269..583
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         784
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1112
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1115
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"
SQ   SEQUENCE   1158 AA;  134269 MW;  41F3CFA7B8C81E7A CRC64;
     MTLHAYLGRA GTGKSTKMLT EIKQKMKADP LGDPIILIAP TQSTFQLEQA FVNDPELNGS
     LRTEVLHFER LSHRIFQEVG SYSEQKLSKA ATEMMIYNIV QEQQKYLKLY QSQAKYYGFS
     EKLTEQIQDF KKYAVTPEHL ESFIADKNMQ TRTKNKLEDI ALIYREFEQR IQNEFITGED
     ALQYFIDCMP KSEWLKCADI YIDGFHNFST IEYLIIKGLI KYAKSVTIIL TTDGNHDQFS
     LFRKPSEVLR HIEEIANELN ISIERQYFKQ SYRFNNQDLK HLEQEFDALQ INRVACQGHI
     NILESATMRE EINEIARRII VDIRDKQLRY QDIAILYRDE SYAYLFDSIL PLYNIPYNID
     TKRSMTHHPV MEMIRSLIEV IQSNWQVNPM LRLLKTDVLT ASYLKSAYLV DLLENFVLER
     GIYGKRWLDD ELFNVEHFSK MGRKAHKLTE DERNTFEQVV KLKKDVIDKI LHFEKQMSQA
     ATVKDFATAF YESMEYFELP NQLMTERDEL DLNGYHEKAE EIDQIWNGLI QILDDLVLVF
     GDEPMSMERF LEVFDIGLEQ LEFVVIPQTL DQVSIGTMDL AKVDNKQHVY LVGMNDGTMP
     QPVTASSLIT DEEKKYFEQQ ANVELSPTSD ILQMDEAFVC YVAMTRAKGN VTFSYSLMGS
     SGDDKEISPF LNQIQSLFNQ LEITNLPQYH EVNPLSLMQH AKQTKITLFE ALRAWLDDEI
     VADSWLDAYQ VIRDSDHLNQ GLDYLMSALT FDNETVKLGE TLSKDLYGKE INASVSRFEG
     YQQCPFKHYA SHGLKLNERT KYELQNFDLG DIFHSVLKYI SERINGDFKQ LDLKKIRQLT
     NEALEEILPK VQFNLLNSSA YYRYLSRRIG AIVETTLSAL KYQGTYSKFM PKHFETSFRR
     KPRTNDELIA QTLTTTQGIP INIRGQIDRI DTYTKNDTSF VNIIDYKSSE GSATLDLTKV
     YYGMQMQMMT YMDIVLQNKQ RLGLTDIVKP GGLLYFHVHE PRIKFKSWAD IDEDKLEQDL
     IKKFKLSGLV NADQTVIDAL DIRLEPKFTS DIVPVGLNKD GSLSKRGSQV ADEATIYKFI
     QHNKENFIET ASNIMDGHTE VAPLKYKQKL PCAFCSYQSV CHVDGMIDSK RYRTVDETIN
     PIEAIQNINI DDEFGGEQ