ADDB_ENTFA
ID ADDB_ENTFA Reviewed; 1196 AA.
AC Q836J9;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B {ECO:0000255|HAMAP-Rule:MF_01453};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01453};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01453};
DE AltName: Full=ATP-dependent helicase/nuclease RexB {ECO:0000255|HAMAP-Rule:MF_01453};
GN Name=rexB {ECO:0000255|HAMAP-Rule:MF_01453}; OrderedLocusNames=EF_1112;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(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. This subunit has 5' -> 3'
CC nuclease activity. {ECO:0000255|HAMAP-Rule:MF_01453}.
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_01453};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01453};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01453};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01453};
CC -!- SUBUNIT: Heterodimer of AddA and RexB. {ECO:0000255|HAMAP-
CC Rule:MF_01453}.
CC -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01453}.
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DR EMBL; AE016830; AAO80912.1; -; Genomic_DNA.
DR RefSeq; NP_814842.1; NC_004668.1.
DR RefSeq; WP_002386608.1; NZ_KE136528.1.
DR AlphaFoldDB; Q836J9; -.
DR SMR; Q836J9; -.
DR STRING; 226185.EF_1112; -.
DR EnsemblBacteria; AAO80912; AAO80912; EF_1112.
DR KEGG; efa:EF1112; -.
DR PATRIC; fig|226185.45.peg.2383; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000001415; 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_01453; AddB_type2; 1.
DR InterPro; IPR014141; DNA_helicase_suRexB.
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.
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..1196
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379364"
FT BINDING 823
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01453"
FT BINDING 1149
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01453"
FT BINDING 1152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01453"
FT BINDING 1158
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01453"
SQ SEQUENCE 1196 AA; 139018 MW; A33782250F28C052 CRC64;
MSVQFIRGTA VADLEAPLIQ ATKQWLEEDA QHEVFYLVPN HIKFEQEIQV LQKLRQLQTT
TSDSITSTRL QVFSFYRLAW YYLQHTPFYS ADVLSDAGAA MIFRKILVEA EEELQIFRGE
INKPGFIQQL FQLYQEMREG NIEIAELYPF LEKQTENPKG QDLQLKFQDL TLIFTRFQLQ
MSQYGYESAE IIQHLSEYLQ TVDLSNVQFV ISGYQQFTAR ELKLIEVLMA QAGSVKVALL
LDKQYPHDLP DPRSLFYEAG QTYHQLYQLA RQKQIPILSD YVEKKEVLIT NPDLQGLNDY
WIQSQEHLPP LSTADWRGDG LFLWRAENVK EELTHVATEI RRLVVEEGYR YKEIQVLTRD
LDCYENLLEP IFAEHEIPVY VDRDMAMDRH PLVEWIESLF AIHSYNYRYR DVLRFLRTEL
FMPMNQLATS EESLTDWLNQ RNAWRRKVDI TENVVLAYGY EGYYWSQEKD WEFIRYDFEA
EEQEDVATME EESNAIRQSL QRLLPSYFQA MISAKTGLEA ATVFYHFLLQ SGVATQLKMW
RLQAIEAGQL ETARNHEQTW DALMSLLDEY VTVYGESSFD FTTFQEIFVS GLEGLHYSKV
PTAIDQVQVR AMDLTRPGAA KVTFAIGMTE EIFPQKIENK TLLSDEERQT INDTLTENQY
LRGTTGRKIA QEPYVAYLVF SSARERLYLT YPSVKDTAQE VKPSPYFKNI QKDLNLPVFE
KNETTIFDDE TTSLAHISTY RTLIGELTRL KRQRKETQEG LLPFWLNMEK ALMNQSIAPL
AKQVFESLTH QNIPEKIDEV LAEPLYGKDI YTSVSRMESF YRCQYQYFSR YGLRLKERDV
FGLSPAATGE FFHEALDQFF KLLIMNQRNL SELTDQEVNL LAEEVLNSIL GDARFSVLTT
SSRMNYIRYQ LSQTIKKVSW ALKRQSQRSG MTTVQTEVLF GQIAAKKGIS GLELPLKNQG
KIHVRGKIDR IDQLVTPEST YLGVIDYKSS HRKFNMTEAY YGLAMQMLTY LDVALMDAVQ
LVGQEAKPAG SLYLHVHNPT LSYEGKDDIE QQMLKKYQFD GLLMKDPDLL DHLDTSLQAK
QSSLLFPIEE SAKEQIKPGR RQEDKFVTEP ELGALLSHNR NKFIEAGNQI IGGEVQLNPA
YQGKERIACR YCPFRSVCDF DVMLKENNYH RIENLSKEEI MARLLNKDEE GATEDE
