ADDB_STAA8
ID ADDB_STAA8 Reviewed; 1158 AA.
AC Q2FZT6;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=SAOUHSC_00904;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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; CP000253; ABD30029.1; -; Genomic_DNA.
DR RefSeq; WP_000172342.1; NZ_LS483365.1.
DR RefSeq; YP_499457.1; NC_007795.1.
DR AlphaFoldDB; Q2FZT6; -.
DR SMR; Q2FZT6; -.
DR STRING; 1280.SAXN108_0961; -.
DR EnsemblBacteria; ABD30029; ABD30029; SAOUHSC_00904.
DR GeneID; 3921750; -.
DR KEGG; sao:SAOUHSC_00904; -.
DR PATRIC; fig|93061.5.peg.825; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR PRO; PR:Q2FZT6; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033202; C:DNA helicase complex; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
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: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 GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
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 Pfam; PF13361; UvrD_C; 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..1158
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379214"
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; 134505 MW; BE48085F5FAFFC4E CRC64;
MTLHAYLGRA GTGKSTKMLT EIKQKMKADP LGDPIILIAP TQSTFQLEQA FVNDPELNGS
LRTEVLHFER LSHRIFQEVG SYSEQKLSKA ATEMMIYNIV QEQQKYLKLY QSQAKYYGFS
EKLTEQIQDF KKYAVTPEHL EHFIADKNMQ TRTKNKLEDI ALIYREFEQR IQNEFITGED
SLQYFIDCMP KSEWLKRADI YIDGFHNFST IEYLIIKGLI KYAKSVTIIL TTDGNHDQFS
LFRKPSEVLR HIEEIANELN ISIERQYFNQ LYRFNNQDLK HLEQEFDALQ INRVACQGHI
NILESATMRE EINEIARRII VDIRDKQLRY QDIAILYRDE SYAYLFDSIL PLYNIPYNID
TKRSMTHHPV MEMIRSLIEV IQSNWQVNPM LRLLKTDVLT ASYLKSAYLV DLLENFVLER
GIYGKRWLDD ELFNVEHFSK MGRKAHKLTE DERNTFEQVV KLKKDVIDKI LHFEKQMSQA
ETVKDFATAF YESMEYFELP NQLMTERDEL DLNGNHEKAE EIDQIWNGLI QILDDLVLVF
GDEPMSMERF LEVFDIGLEQ LEFVMIPQTL DQVSIGTMDL AKVDNKQHVY LVGMNDGTMP
QPVTASSLIT DEEKKYFEQQ ANVELSPTSD ILQMDEAFVC YVAMTRAKGD VTFSYSLMGS
SGDDKEISPF LNQIQSLFNQ LEITNIPQYH EVNPLSLMQH AKQTKITLFE ALRAWLYDEI
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 PRIKFKSWSD IDEDKLEQDL
IKKFKLSGLV NADQTVIDAL DIRLEPKFTS DIVPVGLNKD GSLSKRGSQV ADEATIYKFI
QHNKENFIET ASNIMDGHTE VAPLKYKQKL PCAFCSYQSV CHVDGMIDSK RYRTVDETIN
PIEAIQNINI NDEFGGEQ
