ADDB_LACLS
ID ADDB_LACLS Reviewed; 1099 AA.
AC Q033I2;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=LACR_0003;
OS Lactococcus lactis subsp. cremoris (strain SK11).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=272622;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK11;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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. 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; CP000425; ABJ71640.1; -; Genomic_DNA.
DR RefSeq; WP_011675080.1; NC_008527.1.
DR AlphaFoldDB; Q033I2; -.
DR SMR; Q033I2; -.
DR EnsemblBacteria; ABJ71640; ABJ71640; LACR_0003.
DR KEGG; llc:LACR_0003; -.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000000240; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR Pfam; PF12705; PDDEXK_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02774; rexB_recomb; 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..1099
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379381"
FT BINDING 766
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01453"
FT BINDING 1056
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01453"
FT BINDING 1059
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01453"
FT BINDING 1065
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01453"
SQ SEQUENCE 1099 AA; 127317 MW; 76A2F991E45A891C CRC64;
MEILYTEITQ DLTEGLLEIA LEELEKNRKV YYIVPSSMSF EKEKEILERL AKGSDTAVFY
LLVTRFKQLP YYFDKREKAT MKTELGTVGL SMLFRRILRS FKKDEIPLYF SLQDSAGFLE
MLIQLRAELL TANLSVENLP DNPKNQELKK ILTTFEAELS VEYANYSEFG DFTNRLADGE
FDQQLKDVTI IIDGYTRFSA EEELFIESIQ EKVARFVVGT YSDENSLTAG SETIYVGTSQ
MITRFRNKYP VELRKIASSS VNEVYSKLTR MLDLDSRFVI TDEKIELKAE DEKYFRIWEA
ENQKVEIERV AKEIRQKISQ GAFFKDFTVL VGDPAAYEIT LKEIFDLYEI PFFYAQEESM
SQHPLVIFFE SLFAIKKNNY RTDDVVNLLK SKVYTDVNLD EEVIDYFEYY VQKYKISGRK
KFTEEFIESE FSQIELVNEM REKLLGSESP LQVFLGNNRQ KTGKKWVSDL QALLENGNVM
ANMNAYFSAA ELQNEHQMAD KHEQVWQMLI STLNEFFAVF SDEKLKSVEF LDILLAGLKN
AKYRQIPANV DVVNVKDYEL VEPKTNNYIY AIGLSQTNFP RIKKNSTLLS DEERLEINQT
TDENQFIEQL NVANYQKNQF TVLSLINSAK ESLVLSMPQI MTNEQGEFSP VFQLFLKDAD
EKILQKIQGV NLFESLEHIG NSRSVIAMIG QIERELVESE ETNEDKRVFW SSIFRILVKS
NADFQKILLD LAKDIDTVNL APDTLEQIYG DKIYASVSSF ERFYNCEYQY FLENTLSLET
FENIDINSKI VGNFFHEVFE KVMKETDLSA ENFDEKLTLF LQEVDKNYSR YFTQDATARF
TWSNLEEIVR QTATVLKATV STDELKTLLT ESSFGLSKSE LGNFSVDDIY LRGRIDRLDQ
LSTDYLGVID YKSSAHSFKL QEAYDGLSLQ FMTYLDVIKQ AFPNQKIWGA LYLQFKNQPI
NLSEINQLSE IANILKESMR YDGLVLEDAA EQIKGIENIA LKNTNSYNEE EFEQLLKLNE
EHYRAAGQRL KNGKIAINPI MKRSEGIDQS GNVRGCRYCP LKSICRFEAN IHMNEHSREI
GQKSQAEILA ELKGEGRDE
