ID ADDB_BACSU Reviewed; 1166 AA. AC P23477; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 2. DT 27-MAR-2024, entry version 159. DE RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B {ECO:0000255|HAMAP-Rule:MF_01452, ECO:0000303|PubMed:10756102}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01452, ECO:0000269|PubMed:10756102, ECO:0000269|PubMed:17570399}; DE AltName: Full=ATP-dependent helicase/nuclease subunit AddB {ECO:0000255|HAMAP-Rule:MF_01452}; GN Name=addB {ECO:0000255|HAMAP-Rule:MF_01452, GN ECO:0000303|PubMed:1646786, ECO:0000303|PubMed:9579061}; GN OrderedLocusNames=BSU10620; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=OG1; RX PubMed=1646786; DOI=10.1128/jb.173.12.3644-3655.1991; RA Kooistra J., Venema G.; RT "Cloning, sequencing, and expression of Bacillus subtilis genes involved in RT ATP-dependent nuclease synthesis."; RL J. Bacteriol. 173:3644-3655(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX PubMed=9579061; DOI=10.1099/00221287-144-4-859; RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H., RA Venema G., Bron S.; RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus RT subtilis chromosome contains several dysfunctional genes, the glyB marker, RT many genes encoding transporter proteins, and the ubiquitous hit gene."; RL Microbiology 144:859-875(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [4] RP SEQUENCE REVISION TO 844. RX PubMed=19383706; DOI=10.1099/mic.0.027839-0; RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.; RT "From a consortium sequence to a unified sequence: the Bacillus subtilis RT 168 reference genome a decade later."; RL Microbiology 155:1758-1775(2009). RN [5] RP SUBUNIT, AND FUNCTION IN E.COLI. RX PubMed=8387145; DOI=10.1111/j.1365-2958.1993.tb01182.x; RA Kooistra J., Haijema B.J., Venema G.; RT "The Bacillus subtilis addAB genes are fully functional in Escherichia RT coli."; RL Mol. Microbiol. 7:915-923(1993). RN [6] RP FUNCTION OF COMPLEX AS AN EXONUCLEASE AND HELICASE, MAGNESIUM COFACTOR, AND RP ATP-DEPENDENCE. RX PubMed=10756102; DOI=10.1006/jmbi.2000.3556; RA Chedin F., Ehrlich S.D., Kowalczykowski S.C.; RT "The Bacillus subtilis AddAB helicase/nuclease is regulated by its cognate RT Chi sequence in vitro."; RL J. Mol. Biol. 298:7-20(2000). RN [7] RP RECRUITS RECA TO DNA DOUBLE-STRAND BREAKS. RC STRAIN=168 / YB886 / BG214; RX PubMed=16061691; DOI=10.1083/jcb.200412090; RA Kidane D., Graumann P.L.; RT "Dynamic formation of RecA filaments at DNA double strand break repair RT centers in live cells."; RL J. Cell Biol. 170:357-366(2005). RN [8] RP CHARACTERIZATION. RC STRAIN=168 / YB886 / BG214; RX PubMed=16385024; DOI=10.1128/jb.188.2.353-360.2006; RA Sanchez H., Kidane D., Castillo Cozar M., Graumann P.L., Alonso J.C.; RT "Recruitment of Bacillus subtilis RecN to DNA double-strand breaks in the RT absence of DNA end processing."; RL J. Bacteriol. 188:353-360(2006). RN [9] RP FUNCTION AS A 5' -> 3' NUCLEASE, AND MUTAGENESIS OF ASP-961. RX PubMed=17570399; DOI=10.1016/j.jmb.2007.05.053; RA Yeeles J.T.P., Dillingham M.S.; RT "A dual-nuclease mechanism for DNA break processing by AddAB-type helicase- RT nucleases."; RL J. Mol. Biol. 371:66-78(2007). RN [10] RP COFACTOR, SUBUNIT, DNA-BINDING, AND MUTAGENESIS OF CYS-801; CYS-1121; RP CYS-1124 AND CYS-1130. RX PubMed=19129187; DOI=10.1074/jbc.m808526200; RA Yeeles J.T.P., Cammack R., Dillingham M.S.; RT "An iron-sulfur cluster is essential for the binding of broken DNA by RT AddAB-type helicase-nucleases."; RL J. Biol. Chem. 284:7746-7755(2009). RN [11] RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF RP LYS-14 AND ASP-961, AND DNA-BINDING. RX PubMed=21071401; DOI=10.1093/nar/gkq1124; RA Yeeles J.T., Gwynn E.J., Webb M.R., Dillingham M.S.; RT "The AddAB helicase-nuclease catalyses rapid and processive DNA unwinding RT using a single Superfamily 1A motor domain."; RL Nucleic Acids Res. 39:2271-2285(2011). RN [12] {ECO:0007744|PDB:3U44, ECO:0007744|PDB:3U4Q} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF ADDAB IN COMPLEX WITH DS-DNA AND RP [4FE-4S] CLUSTER, FUNCTION, SUBUNIT, AND MUTAGENESIS OF ASP-41; GLN-42; RP THR-44; PHE-68; ARG-70; TRP-73; PHE-210 AND PHE-213. RX PubMed=22307084; DOI=10.1038/emboj.2012.9; RA Saikrishnan K., Yeeles J.T., Gilhooly N.S., Krajewski W.W., RA Dillingham M.S., Wigley D.B.; RT "Insights into Chi recognition from the structure of an AddAB-type RT helicase-nuclease complex."; RL EMBO J. 31:1568-1578(2012). RN [13] {ECO:0007744|PDB:4CEH, ECO:0007744|PDB:4CEI, ECO:0007744|PDB:4CEJ} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH DNA SUBSTRATES; RP [4FE-4S] CLUSTER AND ATP ANALOG, FUNCTION, PROBABLE REACTION MECHANISM, AND RP SUBUNIT. RX PubMed=24670664; DOI=10.1038/nature13037; RA Krajewski W.W., Fu X., Wilkinson M., Cronin N.B., Dillingham M.S., RA Wigley D.B.; RT "Structural basis for translocation by AddAB helicase-nuclease and its RT arrest at chi sites."; RL Nature 508:416-419(2014). CC -!- FUNCTION: The heterodimer acts both as a highly processive, ATP- CC dependent DNA helicase and as an ATP-dependent single-stranded CC exonuclease, acting in both directions. Recognizes the B.subtilis Chi CC site (5'-AGCGG-3') which transforms the enzyme from a helicase which CC degrades both DNA strands to one with only 5' to 3' exonuclease CC activity. This generates a double-stranded DNA with a protruding 3'- CC terminated single-stranded tail suitable for the initiation of CC homologous recombination (Chi fragment). The AddB nuclease domain is CC not required for Chi fragment generation but for recognition of the Chi CC site; this subunit has 5' -> 3' nuclease activity but no helicase CC activity (PubMed:17570399, PubMed:21071401, PubMed:22307084). The CC helicase activity of isolated AddA acts on 3'-tailed substrate and CC requires AddB to bind to blunt-ended DNA (PubMed:21071401). RecA thread CC formation during DNA double-strand break repair requires RecJ or AddAB CC (PubMed:16385024). {ECO:0000269|PubMed:10756102, CC ECO:0000269|PubMed:16385024, ECO:0000269|PubMed:17570399, CC ECO:0000269|PubMed:21071401, ECO:0000269|PubMed:22307084, CC ECO:0000269|PubMed:24670664, ECO:0000269|PubMed:8387145}. CC -!- COFACTOR: CC Note=At low magnesium concentrations there is no nuclease activity, but CC helicase activity is unaffected (PubMed:10756102, PubMed:19129187, CC PubMed:21071401). {ECO:0000269|PubMed:10756102, CC ECO:0000269|PubMed:19129187, ECO:0000269|PubMed:21071401}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01452, ECO:0000269|PubMed:10756102, CC ECO:0000269|PubMed:19129187, ECO:0000269|PubMed:21071401}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01452, CC ECO:0000269|PubMed:19129187, ECO:0000269|PubMed:22307084, CC ECO:0000269|PubMed:24670664, ECO:0007744|PDB:3U44}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01452, CC ECO:0000269|PubMed:19129187, ECO:0000269|PubMed:22307084, CC ECO:0000269|PubMed:24670664, ECO:0007744|PDB:3U44, CC ECO:0007744|PDB:4CEH, ECO:0007744|PDB:4CEI, ECO:0007744|PDB:4CEJ}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=6.16 uM for ATP {ECO:0000269|PubMed:21071401}; CC Note=kcat for ATP hydrolysis by AddAB is 88 sec(-1), ATPase is CC strongly stimulated by ssDNA. {ECO:0000269|PubMed:21071401}; CC -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000255|HAMAP- CC Rule:MF_01452, ECO:0000269|PubMed:19129187, CC ECO:0000269|PubMed:21071401, ECO:0000269|PubMed:22307084, CC ECO:0000269|PubMed:24670664, ECO:0000269|PubMed:8387145}. CC -!- INTERACTION: CC P23477; P23478: addA; NbExp=4; IntAct=EBI-5247995, EBI-16098568; CC -!- MISCELLANEOUS: This enzyme is a functional homolog of the RecBCD CC enzyme; unlike the RecBCD enzyme it degrades both duplex strands CC symmetrically. CC -!- MISCELLANEOUS: Despite having conserved helicase domains, this subunit CC does not have helicase activity. The conserved residues of the helicase CC ATP-binding domain line a 3'-DNA channel in the enzyme and are CC responsible for Chi site recognition. {ECO:0000269|PubMed:22307084}. CC -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 1 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01452, ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M63489; AAA22200.1; -; Genomic_DNA. DR EMBL; Y14081; CAA74481.1; -; Genomic_DNA. DR EMBL; AL009126; CAB12902.2; -; Genomic_DNA. DR PIR; A39432; A39432. DR RefSeq; NP_388943.2; NC_000964.3. DR RefSeq; WP_003244988.1; NZ_JNCM01000035.1. DR PDB; 3U44; X-ray; 3.20 A; B=1-1166. DR PDB; 3U4Q; X-ray; 2.80 A; B=1-1166. DR PDB; 4CEH; X-ray; 3.24 A; B=1-1166. DR PDB; 4CEI; X-ray; 2.80 A; B=1-1166. DR PDB; 4CEJ; X-ray; 3.00 A; B=1-1166. DR PDBsum; 3U44; -. DR PDBsum; 3U4Q; -. DR PDBsum; 4CEH; -. DR PDBsum; 4CEI; -. DR PDBsum; 4CEJ; -. DR AlphaFoldDB; P23477; -. DR SMR; P23477; -. DR DIP; DIP-60826N; -. DR IntAct; P23477; 3. DR STRING; 224308.BSU10620; -. DR PaxDb; 224308-BSU10620; -. DR EnsemblBacteria; CAB12902; CAB12902; BSU_10620. DR GeneID; 936341; -. DR KEGG; bsu:BSU10620; -. DR PATRIC; fig|224308.179.peg.1142; -. DR eggNOG; COG3857; Bacteria. DR InParanoid; P23477; -. DR OrthoDB; 9758506at2; -. DR PhylomeDB; P23477; -. DR BioCyc; BSUB:BSU10620-MONOMER; -. DR Proteomes; UP000001570; 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-UniRule. DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule. DR Gene3D; 3.90.320.10; -; 1. DR Gene3D; 6.10.140.1030; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3. DR HAMAP; MF_01452; AddB_type1; 1. DR InterPro; IPR049035; ADDB_N. DR InterPro; IPR014140; DNA_helicase_suAddB. DR InterPro; IPR014017; DNA_helicase_UvrD-like_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011604; PDDEXK-like_dom_sf. DR InterPro; IPR038726; PDDEXK_AddAB-type. DR NCBIfam; TIGR02773; addB_Gpos; 1. DR PANTHER; PTHR30591; RECBCD ENZYME SUBUNIT RECC; 1. DR PANTHER; PTHR30591:SF1; RECBCD ENZYME SUBUNIT RECC; 1. DR Pfam; PF21445; ADDB_N; 1. DR Pfam; PF12705; PDDEXK_1; 1. DR Pfam; PF13361; UvrD_C; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1. DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; ATP-binding; DNA damage; DNA repair; DNA-binding; KW Exonuclease; Helicase; Hydrolase; Iron; Iron-sulfur; Metal-binding; KW Nuclease; Nucleotide-binding; Reference proteome. FT CHAIN 1..1166 FT /note="ATP-dependent helicase/deoxyribonuclease subunit B" FT /id="PRO_0000064450" FT DOMAIN 1..278 FT /note="UvrD-like helicase ATP-binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452" FT DOMAIN 281..586 FT /note="UvrD-like helicase C-terminal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452" FT BINDING 10 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000312|PDB:4CEI, ECO:0000312|PDB:4CEJ" FT BINDING 11 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000312|PDB:4CEI, ECO:0000312|PDB:4CEJ" FT BINDING 14 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:24670664, FT ECO:0000312|PDB:4CEI, ECO:0000312|PDB:4CEJ" FT BINDING 15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:24670664, FT ECO:0000312|PDB:4CEI, ECO:0000312|PDB:4CEJ" FT BINDING 16 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000312|PDB:4CEI, ECO:0000312|PDB:4CEJ" FT BINDING 236 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000312|PDB:4CEI, ECO:0000312|PDB:4CEJ" FT BINDING 283 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:24670664, FT ECO:0000312|PDB:4CEI, ECO:0000312|PDB:4CEJ" FT BINDING 801 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452, FT ECO:0000269|PubMed:22307084, ECO:0000269|PubMed:24670664, FT ECO:0007744|PDB:3U44, ECO:0007744|PDB:4CEH, FT ECO:0007744|PDB:4CEI, ECO:0007744|PDB:4CEJ" FT BINDING 1121 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452, FT ECO:0000269|PubMed:22307084, ECO:0000269|PubMed:24670664, FT ECO:0007744|PDB:3U44, ECO:0007744|PDB:4CEH, FT ECO:0007744|PDB:4CEI, ECO:0007744|PDB:4CEJ" FT BINDING 1124 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452, FT ECO:0000269|PubMed:22307084, ECO:0000269|PubMed:24670664, FT ECO:0007744|PDB:3U44, ECO:0007744|PDB:4CEH, FT ECO:0007744|PDB:4CEI, ECO:0007744|PDB:4CEJ" FT BINDING 1130 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01452, FT ECO:0000269|PubMed:22307084, ECO:0000269|PubMed:24670664, FT ECO:0007744|PDB:3U44, ECO:0007744|PDB:4CEH, FT ECO:0007744|PDB:4CEI, ECO:0007744|PDB:4CEJ" FT MUTAGEN 14 FT /note="K->A: No change in AddABATPase activity, KM and kcat FT for ATP hydrolysis are unchanged, helicase rate and FT processivity are unchanged, enzyme-Chi-DNA complex is FT 3-fold less stable." FT /evidence="ECO:0000269|PubMed:21071401" FT MUTAGEN 41 FT /note="D->A: No longer recognizes the Chi sequence nor FT generates the Chi fragment." FT /evidence="ECO:0000269|PubMed:22307084" FT MUTAGEN 42 FT /note="Q->A: No longer recognizes the Chi sequence nor FT generates the Chi fragment." FT /evidence="ECO:0000269|PubMed:22307084" FT MUTAGEN 44 FT /note="T->A: No longer recognizes the Chi sequence nor FT generates the Chi fragment." FT /evidence="ECO:0000269|PubMed:22307084" FT MUTAGEN 68 FT /note="F->A: Reduced recognition of the Chi sequence, FT reduced generation of the Chi fragment." FT /evidence="ECO:0000269|PubMed:22307084" FT MUTAGEN 70 FT /note="R->A: No longer recognizes the Chi sequence nor FT generates the Chi fragment." FT /evidence="ECO:0000269|PubMed:22307084" FT MUTAGEN 73 FT /note="W->A: Reduced recognition of the Chi sequence, FT reduced generation of the Chi fragment." FT /evidence="ECO:0000269|PubMed:22307084" FT MUTAGEN 210 FT /note="F->A: No longer recognizes the Chi sequence nor FT generates the Chi fragment." FT /evidence="ECO:0000269|PubMed:22307084" FT MUTAGEN 213 FT /note="F->A: Wild-type Chi fragment generation." FT /evidence="ECO:0000269|PubMed:22307084" FT MUTAGEN 801 FT /note="C->A: Loss of iron-sulfur group binding, loss of FT DNA-binding." FT /evidence="ECO:0000269|PubMed:19129187" FT MUTAGEN 961 FT /note="D->A: Loss of 5'-3' nuclease activity, helicase and FT DNA-binding are unaltered; when associated with A-1172 in FT AddA nearly complete loss of bith nuclease activities." FT /evidence="ECO:0000269|PubMed:17570399, FT ECO:0000269|PubMed:21071401" FT MUTAGEN 1121 FT /note="C->A: Loss of iron-sulfur group binding, loss of FT DNA-binding." FT /evidence="ECO:0000269|PubMed:19129187" FT MUTAGEN 1124 FT /note="C->A: Loss of iron-sulfur group binding, loss of FT DNA-binding." FT /evidence="ECO:0000269|PubMed:19129187" FT MUTAGEN 1130 FT /note="C->A: Loss of iron-sulfur group binding, loss of FT DNA-binding." FT /evidence="ECO:0000269|PubMed:19129187" FT CONFLICT 843..844 FT /note="EQ -> DE (in Ref. 1; AAA22200 and 2; CAA74481)" FT /evidence="ECO:0000305" FT STRAND 3..8 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 14..28 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 35..38 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 44..51 FT /evidence="ECO:0007829|PDB:3U4Q" FT TURN 55..57 FT /evidence="ECO:0007829|PDB:4CEI" FT STRAND 58..66 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 68..79 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 89..102 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 103..106 FT /evidence="ECO:0007829|PDB:3U4Q" FT TURN 110..113 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 114..116 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 118..132 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 137..144 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 155..175 FT /evidence="ECO:0007829|PDB:3U4Q" FT TURN 177..179 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 183..185 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 186..193 FT /evidence="ECO:0007829|PDB:3U4Q" FT TURN 194..196 FT /evidence="ECO:0007829|PDB:3U44" FT HELIX 198..200 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 204..207 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 215..227 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 229..236 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 242..244 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 248..251 FT /evidence="ECO:0007829|PDB:4CEH" FT HELIX 253..268 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 273..278 FT /evidence="ECO:0007829|PDB:3U4Q" FT TURN 283..286 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 288..295 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 296..298 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 310..319 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 320..336 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 342..344 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 345..350 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 352..354 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 356..365 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 370..374 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 382..395 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 400..407 FT /evidence="ECO:0007829|PDB:3U4Q" FT TURN 408..410 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 411..413 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 415..417 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 419..436 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 441..444 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 445..447 FT /evidence="ECO:0007829|PDB:4CEJ" FT STRAND 457..459 FT /evidence="ECO:0007829|PDB:4CEI" FT HELIX 465..494 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 498..511 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 514..527 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 531..554 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 562..575 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 584..586 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 588..595 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 602..607 FT /evidence="ECO:0007829|PDB:3U4Q" FT TURN 611..616 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 622..624 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 626..634 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 645..658 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 662..672 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 674..676 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 683..691 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 698..700 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 704..706 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 709..712 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 713..715 FT /evidence="ECO:0007829|PDB:4CEI" FT HELIX 719..734 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 742..750 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 756..763 FT /evidence="ECO:0007829|PDB:3U4Q" FT TURN 764..767 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 777..783 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 786..788 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 792..800 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 802..808 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 824..843 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 848..850 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 853..867 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 868..870 FT /evidence="ECO:0007829|PDB:3U4Q" FT TURN 872..874 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 875..878 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 880..904 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 910..924 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 927..931 FT /evidence="ECO:0007829|PDB:3U4Q" FT TURN 932..934 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 935..951 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 954..966 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 971..975 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 981..997 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 1001..1010 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 1024..1033 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 1037..1042 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 1045..1051 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 1056..1059 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 1061..1064 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 1071..1073 FT /evidence="ECO:0007829|PDB:4CEI" FT HELIX 1082..1104 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 1113..1115 FT /evidence="ECO:0007829|PDB:4CEI" FT HELIX 1121..1123 FT /evidence="ECO:0007829|PDB:4CEI" FT HELIX 1127..1130 FT /evidence="ECO:0007829|PDB:3U4Q" FT STRAND 1134..1136 FT /evidence="ECO:0007829|PDB:3U4Q" FT HELIX 1149..1159 FT /evidence="ECO:0007829|PDB:3U4Q" SQ SEQUENCE 1166 AA; 134645 MW; FA63593585A4CA73 CRC64; MGAEFLVGRS GSGKTKLIIN SIQDELRRAP FGKPIIFLVP DQMTFLMEYE LAKTPDMGGM IRAQVFSFSR LAWRVLQHTG GMSRPFLTST GVQMLLRKLI EEHKQEFKVY QKASDKSGFT AQVERMLTEF KRYCLEPEDI RRMAESGTAS EYRGERVLSE KLHDLSILYQ QMEKSLADQY LHSEDYLTLL AEHIPLAEDI KGAHIYVDGF YQFTPQEFRV LEQLMVHAEH ITFSLTADKP SYEREPHELE LFRMTGKTYY RLHQKAKELN LDITYKELSG TERHTKTPEL AHLEAQYEAR PAIPYAEKQE ALTVMQAANR RAELEGIARE IHALVREKGY RYKDVAILAR QPEDYKDMVK EVFADYEIPY FIDGKASMLN HPLIEFIRSS LDVLKGNWRY EAVFRCVKTE LLFPLNEPKA KVREQVDQLE NYCIAYGIKG DRWTKGDRFQ YRRFVSLDDD FAQTDQEIEM ENMLNDTRDW IVPPLFQLQK RMKKAKTVQE KAEALYRYLE ETDVPLKLDQ ERQRAEDDGR IIEAQQHQQA WDAVIQLLEE FVEMMGDDEI SLDLFQQMIE AGAESLTFSL IPPALDQVFV GNMDLSRMYG TSCTFVLGAN DGVLPARPDE NGVLSDDDRE WLKTIGVELS SGGRERLLDE HFLIYMAFSS PSDRLYVSYP IADAEGKTLL PSMIVKRLEE LFPHHKERLL TNEPEQVSDE EQLMYVVNKS VAQSFTASQL RLWTREYDIS DVWWSTYNVL MSEQDRLQSK KLFSSLFFRN EVKQLERSVS RQLYGERIQG SVSRMETFNA CPFSHFASHG LHLKERQFFK LEAPDIGQLF HSSLKLISDR LREQKLDWRD LTKEQCELFS YDAVERLAPK LQKEILLSSN RHYYVKEKLQ KIVTRVSGIL SEHAKASGFV PIGLELGFGG KGPLPPLTFQ LKNGCTMELV GRIDRVDKAE SSKGLLLRIV DYKSSDKGLD LAEVYYGLAL QMLTYLDLSI THSADWLGMR ATPAGVLYFH IHDPMIQSNL PLGLDEIEQE IFKKFKMKGL LLGDQEVVRL MDTTLQEGRS NIINAGLKKD GSLRSDSAAV GEKEFDLLTK HVRRTFQEAG EQITDGRVSI EPYKMKNKTP CTYCAFKSVC QFDESLEENE YRPLKAEKDK TILEWIKKEA DGNEHS //