ADDB_LISMF
ID ADDB_LISMF Reviewed; 1157 AA.
AC Q71X98;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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};
GN OrderedLocusNames=LMOf2365_2301;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT pathogen Listeria monocytogenes reveal new insights into the core genome
RT components of this species.";
RL Nucleic Acids Res. 32:2386-2395(2004).
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; AE017262; AAT05067.1; -; Genomic_DNA.
DR RefSeq; WP_010959029.1; NC_002973.6.
DR AlphaFoldDB; Q71X98; -.
DR SMR; Q71X98; -.
DR PRIDE; Q71X98; -.
DR KEGG; lmf:LMOf2365_2301; -.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
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; ISS:JCVI.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004527; F:exonuclease activity; ISS:JCVI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006259; P:DNA metabolic process; ISS:JCVI.
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_0000379197"
FT DOMAIN 1..278
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 272..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; 132241 MW; 4797A39B372D75AD CRC64;
MTLQIIAGRS GTGKTTYLMD EVSVKIKQNS KTYIFIVPDQ MTFQMETSFL NKENLEGMLG
TQIFSFSRLA WKILQETGGL SKTFLSQTGI EMVIRKAALD QRDKLKIFSR ATSRKGFYAE
LANLFKEMKQ EEVSIEDMVK SATNLSTSVN NKIHDISIIY QKYEELLADK FLENEDYLRL
LAEKITESDY LNQTEIVIDG FTSFSQQELT VIGALMRKCD KVTVSLALNV PEIKHGLDEY
SMFKASTEAY YALLELAKLN SINVEEDKFF LENKRAKTES LAFLANAWGH NKFMAFKEEP
HNLSVHQANN RRAEIEGVAR EIRQLTLNGY RYQDMAILTR NLGDYDVLCE TVMESYNIPI
FIDKKRAMSK HPFIEFIRSS LDAILFNWKY EPIFQAVKTE FFFGVAEKSS VLRRKADILE
NYVLENGIQN KWKWEKEGDW IYRKIRGLST NVLPQTDGEI QTQSIINEMR SLIVNPLSTL
ELNLKKAKTG MEFALALYHF LEQVNAVERL ESWRQRAEEQ GYLELAREHE QAWSAISALL
DEFVEVLGKE TLDLNSFVEI IATGLDALEF SLLPPSLDQV VLSDMENAKL LDMKVIFAIG
MNDGVMPLRQ KDNGILSDQD RDALRAEVSN LKPSAKNNIG EEDLLAYKII SLPSDKLFLS
YPAADEEGKV LSESNYLRKI KGQFKKLSES VYLTDPGLLS DAEQSSYIRS KQATLGLLTS
QLQMYKRGYP LSSVWWDAYN SYFENGKESR MAKQVLSSLY YENKTKPLQE KTAKNLFGET
IHASVSRMEK FFSCEFQHFA QYGLKLEERG HFQLQAVDMG EIFHGAMEWI SAELKRNNLD
WGSLTDQECR QMAKLAMTFL APKIQHEILL SSKRMEYIQY KLLQIITRAT TVLNEQAKSS
AFRPVGLEVD FGLKGDIPPL KISLQANSEL LLQGRIDRID MAEQEDRTFL RIIDYKSSSH
DLALTEVYYG LALQMLTYLD IVVTNAQKMI GKTAEPAGVL YFHMHNQYVQ AEKELSDEAI
VKELQKNSKM KGLILSDPVA VSLMDTTLEK GKSSNIVPAE IKQNGELSAR SKTATREEFD
KMRHFVRHKY QEAGNKILDG AVSINPYKLK ERTPCQFCGF RSFCGFDPSL ASNQYRHLTN
EKTETILAKM NIEGGEQ
