ADDB_LISMO
ID ADDB_LISMO Reviewed; 1157 AA.
AC Q8Y510;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=lmo2268;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
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; AL591982; CAD00346.1; -; Genomic_DNA.
DR PIR; AD1358; AD1358.
DR RefSeq; NP_465792.1; NC_003210.1.
DR RefSeq; WP_010989937.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y510; -.
DR SMR; Q8Y510; -.
DR STRING; 169963.lmo2268; -.
DR PaxDb; Q8Y510; -.
DR EnsemblBacteria; CAD00346; CAD00346; CAD00346.
DR GeneID; 984656; -.
DR KEGG; lmo:lmo2268; -.
DR PATRIC; fig|169963.11.peg.2320; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR PhylomeDB; Q8Y510; -.
DR BioCyc; LMON169963:LMO2268-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033202; C:DNA helicase complex; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
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: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 GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
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;
KW Reference proteome.
FT CHAIN 1..1157
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379195"
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; 132602 MW; 21196396F35DB4E5 CRC64;
MTLQIIAGRS GTGKTTHLMD EVGEKIKQNS KTYIFIVPDQ MTFQMETSFL NKENLAGMLG
TQIFSFSRLA WKILQETGGL SKTFLSQTGI EMVIRKAALD QKDKLKIFSR ATSRKGFYSE
LANLFKEMKQ EEVSIEDMVK SATNLSTSVN NKVHDISLIY QKYEELLADK FLENEDYLRL
LAEKIADSDY LNQTEIVIDG FTSFSKQELT VIGELMRKCD KVTISLTLNV PEIQHGLDEY
SMFKASTEAY YALLELAKLN GTQVEENKFF LENKRAKTES LAFLANTWGH NKFMSFKNEP
QNLKIHQANN RRAEIEGIAR EIRQQALNGY RYRDIAILTR NLGDYDVLCE TVMEAYNIPT
FIDKKRAMAK HPFIEFIRSS LDAILFNWKY EPIFQAVKTE FFFDITEKSS LNRRKADILE
NYVLENGIQN KWKWEKEGDW IYRKIRGLST NVLPQTDEEI HMQSIINEMR NLIVNPLSTL
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 VSLMDMTLEK GKASTIIPAE IKQNGELSAR SRTATRAEFD
KMRQFVRHKY QEAGNKILDG AVSINPYKLK ERTPCQFCSF RSFCGFDPSL TSNQYRHLAN
EKAETILTKM DIEGGTQ
