ADDB_SYMTH
ID ADDB_SYMTH Reviewed; 1165 AA.
AC Q67MD4;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=STH2174;
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863;
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(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; AP006840; BAD41159.1; -; Genomic_DNA.
DR AlphaFoldDB; Q67MD4; -.
DR SMR; Q67MD4; -.
DR STRING; 292459.STH2174; -.
DR PRIDE; Q67MD4; -.
DR EnsemblBacteria; BAD41159; BAD41159; STH2174.
DR KEGG; sth:STH2174; -.
DR eggNOG; COG3857; Bacteria.
DR HOGENOM; CLU_007838_0_0_9; -.
DR OMA; DRLENYV; -.
DR Proteomes; UP000000417; 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 InterPro; IPR011335; Restrct_endonuc-II-like.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 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..1165
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000379223"
FT DOMAIN 1..324
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT DOMAIN 282..597
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 6..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 803
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"
FT BINDING 1124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT BINDING 1130
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ SEQUENCE 1165 AA; 130035 MW; 156756FAFECDF015 CRC64;
MRFIIGGAGS GKSQRCLDEL TQAAQAAPAG PPLILLVPEQ ATFQVEQALL GSGRLKGIIR
AQVLSFQRLA WRVSLKAGGL ALPPLSDLGK QMVLRALLEK KRDDLRLFHQ VADKPGFIER
VAGSIRELRS YRQGPESLRR QLSQLEAEGL GETSLGAKLH DLALVMDELR SYIEGRFTDP
DEYLTVLAAR LEESRLLEGA EVWVDGFNGF TPQELAVLGA VMRSARQVHI SLCIPPGQLY
KAGGHHSPSD LFHPVLSTYD QLMQLAAESG VAVDPPLYLN EPLRFRGAPE LAHVERYLFR
QSAPAWPGAP ERIALVEAQN RREEVAAAAR EILRLVREEG LRFREIAVVA RDLEGYGDLA
ATLFAEHGIP AFIDRRRTVA HHPLVELLRA ALEVVVQDWA YGPVFRYLKT DLTGVSRAEI
DLLENYVIEH GIRGRAWQQQ EPWQYLRRYT LEEDAVPAGP AQQALLDEIH RIRRRATAPL
LAFQRRLQRR GRPGPTVREI TTYLFQLLDD LKVARQLEAW KAEAEQRGDL ETAREHEQVW
TRVLELFDQI VEGLGDQVLS PKVYLQVLSA GLDGLKLGLI PPGLDQVIVG TVERSRHAGV
RATLILGATE KDFPPQPAED AIFTDRERER LKQSGLDVGP TSLERLFQEQ FLTYVALTRG
SDFLWISYPL ADESGRAAAP SPVVGRMRRL FPELKPRPAA PPAPDAEAAV AQVATPRQLA
AAVARALRRA RSGYAVEPHW LDLYQCIVLD PDLHREGAAV LAAVGYEEWL RRRGTPVGRE
LARLLYGDRL VTSVSRLEAF LSCPFRHFAG YALRLQGRAE FTVSAPEFGL FYHAALSLFV
RELERDGLAW DTLTPDEAWR RMDSIIDRLA PRLQSEILLS SPQHRYLLRV IRRTLQSSLD
YLSEHVLHGE FRPVAVEVPF GEEMDGLPPV EVDLPGGGRV LLRGRIDRVD ALEGRDGRWY
VRVIDYKSGR RDLRLGDFYH GLTLQLLLYL MAVVEGGEPL LPGTRVPAGA LYLPVYDPVE
PVNAPVPPDE VRPLRRKRYQ ARGLVSDDPA VIQAMDAAGL GLIQAKLKKD GTVYKGAPVA
SPDQFRQLFA HLRRVVRACG EQILQGEAAI APYRLGPHTA CQYCAYRPVC QFDPAVEPQG
YRRLEKMDAP DVWQRVAAAG GEGDV
