ADDB_LISW6
ID ADDB_LISW6 Reviewed; 1157 AA.
AC A0AL19;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=lwe2283;
OS Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /
OS NCTC 11857 / SLCC 5334 / V8).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=386043;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8;
RX PubMed=16936040; DOI=10.1128/jb.00758-06;
RA Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT genome reduction with Listeria innocua as compared to Listeria
RT monocytogenes.";
RL J. Bacteriol. 188:7405-7415(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. 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; AM263198; CAK21701.1; -; Genomic_DNA.
DR RefSeq; WP_011703032.1; NC_008555.1.
DR AlphaFoldDB; A0AL19; -.
DR SMR; A0AL19; -.
DR STRING; 386043.lwe2283; -.
DR PRIDE; A0AL19; -.
DR EnsemblBacteria; CAK21701; CAK21701; lwe2283.
DR GeneID; 61190187; -.
DR KEGG; lwe:lwe2283; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR OrthoDB; 1283891at2; -.
DR Proteomes; UP000000779; 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; 1.
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..1157
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379198"
FT DOMAIN 1..277
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 272..578
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 794
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 1118
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1157 AA; 132447 MW; 89B48C197EAB1C82 CRC64;
MTLQIIAGKS GTGKTTHLMD EVGKKIKKTS KTYIFIVPDQ MTFQMETSFL NKESLSGMLG
TQIFSFSRLA WKILQETGGL SKTFLSQTGI EMVIRKAALD QKDKLKIFSK ATSRKGFYSE
LAKLFKEMKQ EEVSVADLEN SAINMSKSVT NKIHDISLIY QKYEELLAGK FLENEDYLRL
LADKIIESDY LNQTEIIIDG FTSFSKQELT VIEKLMEKCD KVTVSLTLNV PEIQKGLEEY
NMFKQSTEAY FALLEMAKLN KISVESDKLF LENKRAKSDS LAFLADVWGN NKFVTFEEKP
QDLAIHQANN RRAEIEGIAR EIRQLTLKGY RYQDMAILTR NISDYDVLCE TVMESFDIPI
FIDKKRAMAK HPFIEFIRSS IDAILFNWKY EPIFQAVKTE FFFDVSENTS IMRRKADILE
NYVLENGIQN KWKWEKEGDW IYRKIRGLST NLLPQTDEEL ETQAIINEMR NLIVEPLSIL
ENNLAKARTG TEFAMALYHF LEQVKAVEHL ESWRQTAEEN GYLELAREHE QAWSSVSELL
DEFVEVLGEE SLDINSFAEI VATGLDALEF SLLPPSLDQI VLSDMENAKL LDMKVIFAIG
MNDGIMPLRQ KDKGILSDQD RDSLRAENSN LKPSAKNNIG EEDLLAYKII SLPSDKLFLS
YPAADEEGKV LSESNYLRKI KGQFKKLNEE VYLTDPSLLS DEEQSSYIRS KQATLGLLTS
QLQMYKRGYP LSNVWWDAYN GYFEDTKESK VAKQVLSSLY YENKTKALHE TTAKNLFGEN
IHASVSRMEK FFSCEFQHFA QYGLKLEERA HFKLQAVDMG EIFHGAMEWI SAELKRNNQD
WGNLTEEECR QMAKLAMTFL APKIQHEILL SSKRMEYIQY KLLQIITRAT TVLNEQAKSS
AFRPIGLEVD FGLKGDIPSL KIPLKSESEL LLQGRIDRID VAEQDDRTFL RIIDYKSSSH
DLALTEVYYG LALQMLTYLD IVVTNAQKMI GKTAEPAGVL YFHMHNQFVQ ADKELSDEAI
AKELQKSSKM KGLILSDPVA VSLMDTSLEK GKSSNIIPAE IKQNGDLSAR SRTATKEEFD
KMRHFVRHKY QEAGNKILDG AVSINPYKLK ERTPCQFCGF RSFCGFDPSL TSNQYRHLTN
EKAENILTKM DIEGGTQ
