ADDB_NATTJ
ID ADDB_NATTJ Reviewed; 1186 AA.
AC B2A611;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Nther_1856;
OS Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS JW/NM-WN-LF).
OC Bacteria; Firmicutes; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC Natranaerobius.
OX NCBI_TaxID=457570;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-
RT LF.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001034; ACB85428.1; -; Genomic_DNA.
DR RefSeq; WP_012448293.1; NC_010718.1.
DR AlphaFoldDB; B2A611; -.
DR SMR; B2A611; -.
DR STRING; 457570.Nther_1856; -.
DR EnsemblBacteria; ACB85428; ACB85428; Nther_1856.
DR KEGG; nth:Nther_1856; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR OrthoDB; 1283891at2; -.
DR Proteomes; UP000001683; 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 SUPFAM; SSF52540; SSF52540; 2.
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..1186
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379201"
FT DOMAIN 1..308
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 288..620
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 822
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1144
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1147
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1153
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1186 AA; 136751 MW; 48FF67765AA0B313 CRC64;
MSVKFLLGRA GSGKTSYIID SITEQLKAAP DGDPIIFLVP EQATFQMEQA ILRRSDISGF
SRLHILSFQR LSQKVLEEQG GIAKADLSDT GKEMIIKNIL LQRKDDLEIL EKVAVKSGFS
EKLSRLISEA RMYEITPEML EQISQELDLI HLKQKLQEIS QVFTDYETFL QHQGYHHQED
RLSKAGQKME GNNISFLAGS TCYIDGFSGF TPQELKLLEG LLTKCSNIEL ALTLPPQFTG
KIDDELHLFH PTLKTYNQVW ELAVNNDIEI KKSKHFPNEN EEHRSASSLP RFKDNPALAH
LEKEWGKNKI NPYDSEPTGL SIVEGTNLRN EIDKIAREIK LLVRDHGMRY KDIAVIVREL
ESYEPVIKAV FNDYKIPHFL DRKEPVHHHP LVEFLRSSVE TVISNWDYEP LFRMLKTGLL
PISSEEIFQV ENYVLAHGIS GKDWKKQGKW NFIANFDLER ENIAPSNRNK QYLSEINSIK
GKVRDTLLEF DSKLRGINKS ESLSAQFKNQ EAEEDNLLSV REISTYLWEL IEQLQIEYQL
EEWSLEAEER KDFVEMQLHN QLWDTVIDLL DQMVTFLGEQ KVTLSEYLQI IESGLANIKL
GLLPATLDQV LVGTADRSRY HEIKVLFMAG VSDGLYPAKI DDDGIIDDRE RITLRQHDVE
FAPTTEQKLY QEQYLIYNVL TQPSQKLYLS YPAADSEGRT MSPSTIISDI QEMFPELFQE
YQNDGPENDE DFRQYIIDGK KAVSNLIKLI NKVGHPEKLA EDKQQLLAYL INEHPDLFYS
TPEIKALDYK KSLSPLTQEV IDKLYPNKIA TSVSGLESFC QCPFRHFAEQ NLRLKEREYF
RLEPASLGLF YHAGLKLFWD KLQENNLTWH KLKTEEREAL VSEIVEVLSE RLKNRILLAS
ERYKYFKKKL HELLSRAVEV LSWYSDDKGF YPVGSEIGFG KDEPLSTLEL ELPSFPNKKV
QLKGRIDRID TGKKDGDLYL RVIDYKGKSK NLELRDLYYG LDLQLAAYMT VAMRNSDKLT
GDQMFPGGML YFGVENPVVP TDKPVSPAQA RDKLKSTLKM RGYLIDDEEV LDLMTREDEN
SQDLLPYKLR TSSPGFYKNS KVLSEQEFLA VLNYTESKLV ELAERVLSGE IAPYPYKDGG
YSACTYCPYL AVCQFDLNYK EHKFWNVPAK GDYLSLILEE MEEVKE
