ADDB_LISIN
ID ADDB_LISIN Reviewed; 1157 AA.
AC Q929A8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=lin2369;
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(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. 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; AL596172; CAC97596.1; -; Genomic_DNA.
DR PIR; AD1728; AD1728.
DR RefSeq; WP_010991145.1; NC_003212.1.
DR AlphaFoldDB; Q929A8; -.
DR SMR; Q929A8; -.
DR STRING; 272626.lin2369; -.
DR PRIDE; Q929A8; -.
DR EnsemblBacteria; CAC97596; CAC97596; CAC97596.
DR KEGG; lin:addB; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR OrthoDB; 1283891at2; -.
DR Proteomes; UP000002513; 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 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; 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_0000379194"
FT DOMAIN 1..277
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 271..590
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; 132077 MW; 26F106C843116A71 CRC64;
MTLQIIAGKA GTGKTTHLMD EVGEKIKKTS KTYIFIVPDQ MTFQMETSFL NKQNLAGMLG
TQIFSFSRLA WKILQETGGL SKTFLSQTGI EMVIRKAALD QKDKLKIFSR ATSKKGFYSE
LAKLFKEMKQ EEISVDELEK SAANLSTSVS SKVHDISLIY QKYEELLAGK FLENEDYLRL
LADKIIESDY LNQTEIIIDG FTSFSKQELT VIEKLMQKCD KVTVSLTLNV PEIHKGLEDF
SMFKASTEAY FALLEMAKLN KIQVEPEKIL LENKRANSDS LAFLANAWGD NKYSSYEGGA
NDLTIHQANN RRAEMEGVAR EIRQLALNGY RYRDIAILTR NIGDYDILCE TVMESFDIPI
FIDKKRAMAK HPFIEFIRSS IDAILFNWKY EPIFQAVKTE FFFDVAENAT IMRRKADILE
NYVLENGIQN KWKWEKEGDW IYRKIRGLST NVLPQTDEEL ATQSVINEMR NLIVEPLSTL
ENNITKAKTG IEFAMALYHY LEQVKAVEHL ESWRQVAEEN GYLELAREHE QAWSSISELL
DEFVEVLGEE ELDVNSFSEI ITTGLDALEF SLLPPSLDQV VLADMENAKL LNMKVIFAIG
MNDGVMPLRQ KDKGILSDQD RDSLRVENSN LKPSAKNNIG EEDLLAYKIM SLPSDKLFLS
YPAADEEGKV LSESNYLRKI KGQFKNLNES VYLTDPSLLN DKEQSSYIRS KQATLGLLTS
QLQMYKRGYP LSNVWWDAYN SYFEDSKESE AAKQVLSSLY YENKTKPLQE TTAKNLFGEN
IHASVSRMEK FFSCEFQHFA QYGLKLEERA HYKLQAVDMG EIFHGAMEWI SAELKRTNRD
WGNLTEEECR QMAKLAMTFL APKIQHEILL SSKRMEYIQY KLLQIITRAT TVLNEQAKSS
AFRPIGLEVD FGLKGDIPPL KIPLQSDSEL LLQGRIDRID AAEQDDRTFL RIIDYKSSSH
DLALTEVYYG LALQMLTYLD IVVTNAQKMI GKTAEPAGVL YFHMHNQYVQ AEKELSDEAI
ARELQKSSKM KGLILSDPVA VSLMDTNLEK GKSSNIIPAE IKQNGELSAR SRTATKAEFD
KMRRFVRQKY QEAGNKILDG AVSINPYKLK EKTPCQFCGF RSFCGFDPSL ASNQYRHLTN
EKTETILTKM DIEGGTQ
