ADDB_STAES
ID ADDB_STAES Reviewed; 1159 AA.
AC Q8CPU0;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=SE_0663;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04260.1; -; Genomic_DNA.
DR RefSeq; NP_764218.1; NC_004461.1.
DR RefSeq; WP_001831905.1; NZ_WBME01000043.1.
DR AlphaFoldDB; Q8CPU0; -.
DR SMR; Q8CPU0; -.
DR STRING; 176280.SE_0663; -.
DR PRIDE; Q8CPU0; -.
DR EnsemblBacteria; AAO04260; AAO04260; SE_0663.
DR KEGG; sep:SE_0663; -.
DR PATRIC; fig|176280.10.peg.636; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000001411; 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 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..1159
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379219"
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 1159 AA; 134920 MW; 251115B7A1C9EAA3 CRC64;
MEFNTYIGRA GTGKSTAMLN QIKNKMKQDP LGDPIVLIAP TQSTFQLEQA FVNDSELHGS
LRTEVLHFER LSHRVFQEVG GLTEQRLSKA ALEMMIFHIV QQHESDLKLY GSQAQYYGLS
EKLAEQIQDF KKYNVTPEHL NQLIENHSIQ TRTKHKLEDI SLIYKQLESR MNGEFITTED
SLQQFIEILS QSQWIKKAEV FIDGFHNFST LEYRIIEALV QHAKQVTVLL TTDGSHHPFS
LFRKPSEVLS HLEDIANRLN INLNKTYFNT FYRYNNDDLK NLENGFDALQ FTPKHHQNHV
KIFESSSMRE EINEVARRIL KDVREADYKF RDIAILYRDE SYAYLFESIL PSYDIPFNID
TKKSMTHHPI MEMLRSLLEV IRSNWHINAM LRLFKTNVLT SQFKRSSYLI DLLENFVLER
GIYGKRWLDE DIFSIDQFSR MGRKSHQLTE GHQALYKEVI KLKKNVINKV LYFEQAMNEA
HTVKDYATSF YESLEYFELP SQLMTQRDEL ELAGLTEKAE EIDQVWNGLI QILDDLVTVF
DDQEMTLQQF LDVFDIGLEQ LEFVMIPQTL DQVSIGTMDL AKVDNKKHIY MVGMNDGILP
QTVSSSSLIT DEEKKYVEDN AHVELSPTSD ILQMDEAFVC YIAMTRSQQS VTFSYSLMGN
SGDEKEISPF LTQIKELFYD LEITNLQDLH KAQPLLMMQH SHQTKIQLFE YLRGWLDHED
IDYRWLDAYL AIRDDDQLNQ GLDYLTTSLT YDNETVQLNE ILSQQLYGKT INASVSRFEG
YQQCPFKHYA SHGLRLNERT KYELQNFDLG DIFHSVLKYI SDRIYGDFKN LDTKNIQSLT
KEALELILPK VQFNLLNSSA YYKYLSKKIG SIVETTLKAL KYQGEYSKFV PQRFETGFRK
SPKNKGELVA QPLITNQGIP INIRGQIDRI DTYTKGDHSY VNIIDYKSSE SSATLDLTKV
YYGLQMQMMT YMDIVLQNKE RLGLTDIVKP GGLLYFHVHE PRIKFKSWAD IDEDQFQKDY
IKNFKMSGLL NRDQEVLDAL DIRLEPKYNS DIVPIALTAK GAINQRSSKV ADENIIYQLI
EHNKKNFIET ASHIMDGHTE VAPLKYKQVL PCQFCNYKSV CHVDGLIDSK RYRTVDESIK
PLDLIQQLRN EGGERHDSN
