ADDB_LACLA
ID ADDB_LACLA Reviewed; 1099 AA.
AC Q9CJJ0;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=LL0003;
GN ORFNames=L025, L0252;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(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 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; AE005176; AAK04101.1; -; Genomic_DNA.
DR PIR; C86625; C86625.
DR RefSeq; NP_266159.1; NC_002662.1.
DR RefSeq; WP_010905023.1; NC_002662.1.
DR AlphaFoldDB; Q9CJJ0; -.
DR SMR; Q9CJJ0; -.
DR STRING; 272623.L0252; -.
DR PaxDb; Q9CJJ0; -.
DR EnsemblBacteria; AAK04101; AAK04101; L0252.
DR KEGG; lla:L0252; -.
DR PATRIC; fig|272623.7.peg.3; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000002196; 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 InterPro; IPR011335; Restrct_endonuc-II-like.
DR Pfam; PF12705; PDDEXK_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 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;
KW Reference proteome.
FT CHAIN 1..1099
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379382"
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; 127009 MW; 3102F9150CF22820 CRC64;
MEILYTEITQ DLTEGLLEIS LEELEKNRKV YYIVPSSMSF EKEKEILERL AKGSDSAVFD
LLVTRFKQLP YYFDKREKAT TKTELGTAGL SMLFRRVLRS FSKEEIPLYF SLQDSAGFLE
MLIQLRTELL TANLSVENLP DSPKNQELKK ILSRFEEKLA NDYANYSEFG DFTSRLADGE
FDFQLKDVTI VIDGYTRFSA EEELFIESIQ DRVARFVIGT YSDENSLTAG SETIYISTSQ
MIGRFRSKFP VELRKMAFSS VNEVYNKLTK LLDLDSRFAI SDQNIEINSA DAKYFRIWEA
ENQKVEIEGV AKEIRQKISQ GAFFKDFTVL VGDPAAYEIT LKEIFELYEI PFFYAQEESM
SQHPLVIFFE SLLSIKKNNY GTDDVVNLLK SKVYTDVNLD EEVIDYFEYY VQKYKISGRK
KFTEAFNESE FSKIELVNQL RENLLGNDSP LQVFLGTNRQ KTGKKWVSDL QVLLENGNVM
ANMNTYFSEA ESENKHQMAD KHEQVWQMLI SILNEFLAVF SDEKLKSVEF LDILLAGLKN
AKYRQIPANV DVVNIKDYEL VEPKTNKYIY AIGLSQTNFP RIKKNSTLLS DEERLEINQT
TDENQFIEQL NVVNYQKNQF TVLSLVNSAK ETLVLSMPQI MANEQGEFSP VFQLFLNHSD
EKILQKIQEV NLFESLEHIG NSRSVISMIG KIERELVETE EKNDDKRVFW SSIFRILVKS
NPDFQKILLD LAKDIDTVNL SQETLDQIYG DKLYASVSSF ERFYNCEYQY FLETTLGLET
FENIDINSKI VGNFFHEVFE KVMQEEALSA ENFDEKLTKV LHDVDSNYSR YFTHDATARF
TWTNLEEIVR QTATVLKETV STDELKTLLT ESSFGLPKSE LGNFSVDDIY LRGRIDRLDQ
LSSDYLGAID YKSSAHSFKL QDAYDGLSLQ FMTYLDVIKE AFPNQKIWGA LYLQFKNQPI
NLSEINHLSE IAGLLKESMR YDGLVLEEAA DQIKAIENIT VKKSNIYNQE EFEQLLKLNE
NHYQHAGQRL KSGQIAINPI MKRSEGIDQT GNVRGCRYCP LKSICRFEAN VHMNDHSREI
GQKSQAEILA ELKGEGRNE
