ADDB_LISMH
ID ADDB_LISMH Reviewed; 1157 AA.
AC B8DF43;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=LMHCC_0275;
OS Listeria monocytogenes serotype 4a (strain HCC23).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=552536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HCC23;
RX PubMed=21602330; DOI=10.1128/jb.05236-11;
RA Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA Lawrence M.L.;
RT "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL J. Bacteriol. 193:3679-3680(2011).
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; CP001175; ACK38635.1; -; Genomic_DNA.
DR RefSeq; WP_012580844.1; NC_011660.1.
DR AlphaFoldDB; B8DF43; -.
DR SMR; B8DF43; -.
DR KEGG; lmh:LMHCC_0275; -.
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; 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_0000379196"
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; 132560 MW; 4788B44FF34C8980 CRC64;
MTLQIIAGRS GTGKTTHLMD EVGEKIKQNS KTYIFIVPDQ MTFQMETSFL NKENLAGMLG
TQIFSFSRLA WKILQETGGL SKTFLSQTGI EMVIRKAALD QKDKLKIFSR ATSRKGFYSE
LANLFKEMKQ EEVSIEDMVQ SATNLSTSVN NKVHDISLIY QKYEELLADK FLENEDYLRL
LAEKIADSDY LNRTEIVIDG FTSFSKQELT VIGELMRKCD KVTVSLTLNV PEIQHGLDEY
SMFKASTEAY YALLELAKLN GTQVEENKFF LENKRAKTES LAFLANTWGH NKFMSFKNEP
QNLKIHQANN RRAEIEGIAR EIRQLVLNGY RYRDIAILTR NLGDYDVLCE TVMEAYNIPT
FIDKKRAMAK HPFIEFIRSS LDAILFNWKY EPIFQAVKTE FFFDITEKSS LNRRKADILE
NYVLENGIQN KWKWEKEGDW VYRKIRGLST NVLPQTDEEI HMQSIINEMR SLIVNPLATL
ELNLRKAKTG MEFALALYHY LEQVNAVERL ESWRQRAEEQ GYLELAREHE QAWSSISALL
DEFVEVLGEE TLDLDSFTEI IGTGLDALEF SLLPPSLDQV VLSDMENAKL LDMKVIFAIG
MNDGVMPLRQ KDKGIFSDQD RDALRAEDSK LKPSAKNNIG EEDLLAYKII SLPSDKLFLS
YPAADEEGKV LSESNYLRKI KGQFNELNES VYLTDPSLLS DAEQSSYIRS KQATLGLLTS
QLQMYKRGYT LSSVWWDAYN SYFENEKESI MAKQVLSSLY YENKTKPLQE TTAKNLFGET
IHASVSRMEK FFSCEFQHYA QYGLKLEERG HFQLQAVDMG EIFHGAMEWI SAELKRNNLD
WGNLTEEECK QMAKLAMTFL APKIQHEILL SSKRMEYIQY KLLQIITRAT TVLNEQAKSS
AFRPVGLEVD FGLKGDIPPL KIPLQSDSEL LLQGRIDRID MAEQDDRTFL RIIDYKSSSH
DLALTEVYYG LALQMLTYLD IVVTNAQKMI GKTAEPAGVL YFHMHNQYVQ AEKELSDEAI
AKELQKSSKM KGLILSDPVA VSLMDTTLEK GKASTIIPAE IKQNGELSAR SRTATRAEFD
KMRQFVRHKY QEAGNKILDG AVSINPYKLK ERTPCQFCSF RSFCGFDPSL TSNQYRHLAN
EKAETILTKM DMEGGTQ
