ADDB_LACLM
ID ADDB_LACLM Reviewed; 1099 AA.
AC A2RH76;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=llmg_0003;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, FUNCTION IN E.COLI, AND OPERON
RP STRUCTURE.
RX PubMed=9435243; DOI=10.1073/pnas.95.2.626;
RA El-Karoui M., Ehrlich S.D., Gruss A.;
RT "Identification of the lactococcal exonuclease/recombinase and its
RT modulation by the putative Chi sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:626-631(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
RN [3]
RP RECOGNITION OF CHI SEQUENCES.
RX PubMed=10886371; DOI=10.1046/j.1365-2443.2000.00342.x;
RA El Karoui M., Schaeffer M., Biaudet V., Bolotin A., Sorokin A., Gruss A.;
RT "Orientation specificity of the Lactococcus lactis Chi site.";
RL Genes Cells 5:453-461(2000).
RN [4]
RP EXONUCLEASE ACTIVITY, AND MUTAGENESIS OF ASP-910 AND 910-ASP--LYS-912.
RX PubMed=11395472; DOI=10.1128/jb.183.13.4071-4078.2001;
RA Quiberoni A., Biswas I., El Karoui M., Rezaiki L., Tailliez P., Gruss A.;
RT "In vivo evidence for two active nuclease motifs in the double-strand break
RT repair enzyme RexAB of Lactococcus lactis.";
RL J. Bacteriol. 183:4071-4078(2001).
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 L.lactis chi site (5'-GCGCGTG-3'), which stimulates
CC homologous recombination. This subunit has 5'->3' exonuclease activity.
CC {ECO:0000269|PubMed:9435243}.
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:0000305}.
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; AM406671; CAL96611.1; -; Genomic_DNA.
DR RefSeq; WP_011834122.1; NZ_WJVF01000016.1.
DR AlphaFoldDB; A2RH76; -.
DR SMR; A2RH76; -.
DR STRING; 416870.llmg_0003; -.
DR PRIDE; A2RH76; -.
DR EnsemblBacteria; CAL96611; CAL96611; llmg_0003.
DR KEGG; llm:llmg_0003; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR PhylomeDB; A2RH76; -.
DR BioCyc; LLAC416870:LLMG_RS00015-MON; -.
DR Proteomes; UP000000364; 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 1: Evidence at protein level;
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_0000379380"
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"
FT MUTAGEN 910..912
FT /note="Missing: Increase in UV sensitivity, some loss of
FT nuclease activity, still recognizes chi sequences. Shows
FT hyperrecombination."
FT /evidence="ECO:0000269|PubMed:11395472"
FT MUTAGEN 910
FT /note="D->A: Slight increase in UV sensitivity, slight loss
FT of nuclease activity, still recognizes chi sequence. Shows
FT hyperrecombination."
FT /evidence="ECO:0000269|PubMed:11395472"
SQ SEQUENCE 1099 AA; 127227 MW; 4AE7B5A42D8F367C CRC64;
MEILYTEITQ DLTEGLLEIA LEELEKNRKV YYIVPSSMSF EKEKEILERL AKGSDTAVFD
LLVTRFKQLP YYFDKREKAT MKTELGTVGL SMLFRRVLRS FKKDEIPLYF SLQDSAGFLE
MLIQLRAELL TANLSVENLP DNPKNQELKK ILAKFEAELS VEYANYSEFG DFTNRLVDGE
FDQQLKDVTI IIDGYTRFSA EEELFIESIQ EKVARFVVGT YSDENSLTAG SETIYVGTSQ
MITRFRNKFP VELRKIASSA VNEVYSKLTR ILDLDSRFVI TDEKIELKAE DEKYFRIWEA
ENQKVEIERV AKEIRQKIIQ GAFFKDFTVL VGDPAAYEIT LKEVFDLYEI PFFYAQEESM
SQHPLVIFFE SLFAIKKNNY RTDDVVNLLK SKVYTDANLD EEVIDYFEYY VQKYKISGRK
KFTEEFIESE FSQIELVNEM REKLLGSESP LQVFLGNNRK KTGKKWVSDL QGLLENGNVM
TNMNAYFSAA ELQNEHQMAD KHEQVWQMLI STLNEFLAVF SDEKLKSVEF LDILLAGLKN
AKYRQIPANV DVVNVKDYEL VEPKTNKYIY AIGLSQTNFP RIKKNSTLLS DEERLEINQT
TDENQFIEQL NVANYQKNQF TVLSLINSAK ESLVLSMPQI MANEQGEFSP VFQLFLKDAD
EKILQKIQGV NLFESLEHIG NSRSVIAMIG QIERELVESE ETSEDKRVFW SSIFRILVKS
NADFQKILLD LAKDIDTVNL APDTLEQIYG DKIYASVSSF ERFYNCEYQY FLENTLSLET
FENIDINSKI VGNFFHEVFE KVMKETDLSA ENFDEKLTLV LQEVDKNYSR YFTQDATARF
TWSNLEEIVR QTATVLKATV STDELKTLLT ESSFGLPKSE LGNFSVDDIY LRGRIDRLDQ
LSTDYLGAID YKSSAHSFKL QEAYDGLSLQ FMTYLDVIKQ AFPNQKIWGA LYLQFKNQPI
NLSEINQLSE IANILKESMR YEGLVLEDAA EQIKGIENIA LKKTNIYNEE EFEQLLKLNE
EHYRAAGQRL KKGKIAINPI MKRSEGIDQS GNVRGCRYCP LKSICRFEAN IHMNEHSREI
GQKSQAEILA ELKGEERDE
