ADDB_PELTS
ID ADDB_PELTS Reviewed; 1157 AA.
AC A5D1P4;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=PTH_1665;
OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=370438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13744 / JCM 10971 / SI;
RX PubMed=18218977; DOI=10.1101/gr.7136508;
RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT evolution in anaerobic microbiota.";
RL Genome Res. 18:442-448(2008).
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; AP009389; BAF59846.1; -; Genomic_DNA.
DR AlphaFoldDB; A5D1P4; -.
DR SMR; A5D1P4; -.
DR STRING; 370438.PTH_1665; -.
DR PRIDE; A5D1P4; -.
DR EnsemblBacteria; BAF59846; BAF59846; PTH_1665.
DR KEGG; pth:PTH_1665; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000006556; 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; -; 4.
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; 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..1157
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379203"
FT DOMAIN 1..299
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 279..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 792
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1112
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 1121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1157 AA; 129253 MW; 2AC12D658D052113 CRC64;
MSIRFIIGRA GAGKTRACLE AIRKELLARP YGPPLILLVP EQATFQIEYA LAATPGLSGF
IRARVLSFRR LAYRVLREVG GAARAHIGEL GKRMVLRRLL EQRRSELRVL GRSSGRPGFA
DTLARTLGEM KTYCIGPDEL ARAAFDLREK GGAALLADKL EDLAKLCFDL EDYLAGRFTD
PDDYLNLLAD CLELSAEVRG TEVWVDGFSG FTPQEYRVLA ALARTASRVN ITLCADPAAL
SGKIDETSLF FPVRETYDRL LKMALQERIP LERPLILGGN TARFKSPAIS HLEKYFFVRP
APPCLNCSEG VVLAAAANPK AEAEGVAREI TALCRDRGYR YRDIVILLRD VDSYAGLISS
IFADHGIPVF IDQKRPVMHH PMVELVRSAL EAVTEDWAFD PVFRYLKTDL VPLSREEVDL
LENYVLAHGI RGSRWTDGRP WEYRRELTLE EDPGLNGSES VELEKVNRIR HQATADLLEF
CRSFMQAKNV REMSTALFNL LTGLKVPEQL ESWSRQAEKE GRLEAAREHS LVWSGFTALL
DQVVEALGDE VLEPGEYAAV IDAGLESLRL GLIPPGLDQV LVASLERSRN PEMRAAFVMG
VNDGVLPART FDQGIFSDLE RERLKAAGLE LAPGGRRKFF EEQYLVYIAL TRSSERIYLS
YPLADGEGRA LMPSPIVARV KELLPDVEER VWPVEPNAAL LDDLEFVTGP RRTLSYLASQ
MREFKAGRRI DPLWWDVYSW FAAGEMREHC KRVLSGLFHS NREDRLPPAV SMALYGRPLR
ASVSGLEKFR ACPFAHFLSY GLKLKERAIF KLDAPDLGRF FHAALKLFGD RVREQGLDWG
QLDREQCQEM AGEVVDLLAP RLSSEILLST ARRRYLTGKL RRTVQRAALV LAEHSRRSKF
RPVGLELSFG PDGDLPAPVF TLADGSEMAV SGRIDRIEAA PSDEGVYLRI IDFKSGKVTV
KLTDIYHGLK LQLLAYLDVA LEHARTLTGG NGLPGAVLYF RIDDPLVNTD GPVPPGEEVE
REILKKLRMT GLVLADPKAV RLMDAGLDGI SDLIPVQIKA DGSFAARSAV LTREQFALLR
SYLRFQLASA GSEIIGGTVE IAPYRKGRYR SCQSCPFRPV CQFDLLVDGN VYRSIKDEDE
GAIWSKLGRM CRKGWGQ
